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Discussie - Crucell - Crucell's Revolutionary Antibody for Universal Therapy Against Flu

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zaterdag 28 februari 2009 17:58
Geachte M.

Bedankt voor uw opbouwende kritiek.


Ik mis je punt even, zeker indien een combinatie mab die de H1 tot en met H16 aanpakt.
Indien vanuit Percivia een hoger rendament gaat halen (bijvoorbeeld al van 27 naar 40, of zelfs, zoals in Crucells presentatie miscchien wel naar 100)dan weegt dat enorm op het kostenaspect. De marges en/of het kostenaspect kunnen worden aangepast, zeker in een situatie van massaproductie.
Wat was het huidige rendament van een regulier griepvaccine? 2 to 4?


Wat ik bedoelde met een gewone verkoudheid is, dat deze altijd overgaat en doorgaans door andere virussen dan de influenza of para-influenza virussen wordt veroorzaakt.


zaterdag 28 februari 2009 19:43
Another antibody against diverse flu strains found
Robert Roos News Editor
Feb 27, 2009 (CIDRAP News) – For the second time this week, scientists have reported the discovery of a human antibody that, at least in theory, could lead to development of a vaccine or drug effective against most types of influenza A, including the deadly H5N1 avian flu virus.
A team from the Scripps Research Institute in La Jolla, Calif., and the Dutch company Crucell Holland BV describe the new antibody, called CR6261, in a report in Science. They write that the antibody recognizes a stable, or nonmutating, region of the hemagglutinin (HA) protein in the 1918 pandemic flu virus and a 2004 strain of the H5N1 virus.
As it is described, the antibody targets the same general region of the HA protein as do the monoclonal antibodies described in the report published Feb 22: the stem or neck of the molecule, which sits on the surface of the virus and helps it bind to host cells. And like the earlier report, the new one says the antibody neutralizes the virus by blocking it from fusing with cells.
"The antibody neutralizes the virus by blocking conformational rearrangements associated with membrane fusion," the Science report states. "Identification of the CR6261 epitope [the HA site the antibody targets] provides a lead for the design of antivirals and takes a significant step towards the development of a durable and cross-protective 'universal' vaccine against influenza A," it concludes.
The National Institute of Allergy and Infectious Diseases, which provided funding for both studies released this week, said in a statement yesterday, "Taken together, these studies provide a blueprint for efforts to develop new antiviral drugs as well as a potential universal flu vaccine."
The scientists, with Damian C. Ekiert of Scripps as first author, write that they isolated CR6261 from a healthy, vaccinated person by mixing a serum sample with HA from an H5 virus. In a previously reported study, they found that CR6261 neutralized several influenza A subtypes, including H1, H2, H5, H6, H8, and H9. They also found that it protected mice from H1N1 and H5N1 viruses when administered up to 5 days after infection.
To determine which part of the HA molecule the antibody targets and how it neutralizes the virus, the team studied the crystal structures of the antibody in combination with HAs from the 1918 H1N1 virus and a 2004 Vietnam strain of the H5N1 virus. They found that the antibody attaches to the base of the proteins rather than to the mushroom-shaped head—the portion targeted by existing flu vaccines.
In further experiments, the scientists concluded that the antibody prevents HA from initiating the process of fusing the viral membrane with the host cell membrane. "CR6261 appears to neutralize the virus by stabilizing the pre-fusion state and preventing the pH-dependent fusion of viral and cellular membranes," the report says.
The researchers also analyzed more than 5,000 HA genetic sequences in a flu database in an effort to learn why certain flu subtypes, such as H3 and H7, are not neutralized by CR6261. They concluded that the masking of a certain site on the HA molecule by glycoproteins (glycosylation) is the probable reason. From this analysis, they concluded that the antibody probably can neutralize HAs from 12 of the 16 influenza A subtypes: H1, H2, H4-H6, H8, H9, H11-H14, and H16.
The presence of the CR6261 epitope in a wide range of influenza viruses "suggests a critical role in membrane fusion," indicating the possibility of using it to develop new antiviral drugs and a broadly protective vaccine, the researchers write.
Experts who were not involved in the study said the latest findings are very similar to those reported earlier this week in Nature Structural and Molecular Biology.
John Treanor, MD, a vaccine researcher and professor of microbiology and immunology at the University of Rochester in New York, called the idea of using the "fusion region" of HA to develop a vaccine interesting, though not entirely new. "It's a long way to go between knowing you have an antibody that can recognize that region and making a vaccine," he said.
If the CR6261 target region were used to make a vaccine designed to induce the immune system to generate similar antibodies, immunogenicity could be a challenge, Treanor said. "Bear in mind that you don't really make this antibody when you're exposed [to flu viruses], or you don't make much of it. So presumably you'd have to cook up some way of presenting the epitope in such a way as to make it immunogenic."
He said the findings certainly raise the possibility making CR6261 antibodies for use as a flu treatment. "I don't have any doubt that we could do that. I will say that if the experience with palivizumab is any guide, you'd expect this type of passive antibody approach to be much more effective for prevention than for treatment."
Palivizumab is a human monoclonal antibody used to protect certain vulnerable children from serious infections with respiratory syncytial virus, he said.
Dr. Richard Webby, a virologist, flu researcher, and associate member of the Department of Infectious Diseases at St. Jude Children's Research Hospital in Memphis, called the latest findings "great stuff."
Given that monoclonal antibodies are already used to treat certain diseases, the findings certainly point to a possibility of antibody-based therapies for flu, he said.
"There are some limitations on the wider use of this approach, cost being the major one," he said. "As production techniques improve and costs come down, it becomes a little bit more viable."
Webby added that antibody-based flu therapies have been "very, very effective" in animal models, surpassing other drugs. "So I absolutely think it's an avenue that needs to be pursued aggressively."
As for the vaccine possibilities, he noted that a number of researchers are trying to make vaccines that induce immunity to more stable parts of influenza viruses, including sites on the HA, and have had mixed success. "There's no doubt that if we want to produce a more cross-reactive vaccine against influenza, we have to understand more about these cross-reactive epitopes," he said.
http://www.cidrap.umn.edu/cidrap/content/influenza/panflu/news/feb2709antibody.html

zaterdag 28 februari 2009 19:45
Published Online February 26, 2009
Science DOI: 10.1126/science.1171491
REPORTS
Submitted on January 27, 2009
Accepted on February 19, 2009

Antibody Recognition of a Highly Conserved Influenza Virus Epitope
Damian C. Ekiert 1, Gira Bhabha 1, Marc-André Elsliger 1, Robert H. E. Friesen 2, Mandy Jongeneelen 2, Mark Throsby 2, Jaap Goudsmit 2, Ian A. Wilson 3*
1 Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
2 Crucell Holland BV, Archimedesweg 4-6, 2301 CA Leiden, The Netherlands.
3 Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.; The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
* To whom correspondence should be addressed.
Ian A. Wilson , E-mail: wilson@scripps.edu
Influenza virus presents a significant and persistent threat to public health worldwide, and current vaccines provide immunity to viral isolates similar to the vaccine strain. High-affinity antibodies against a conserved epitope could provide immunity to the diverse influenza subtypes and protection against future pandemic viruses. Co-crystal structures were determined at 2.2 and 2.7 Å resolutions for broadly neutralizing human antibody CR6261 Fab in complexes with the major surface antigen (hemagglutinin, HA) from viruses responsible for the 1918 H1N1 influenza pandemic and a recent lethal case of H5N1 avian influenza. In contrast to other structurally characterized influenza antibodies, CR6261 recognizes a highly conserved helical region in the membrane-proximal stem of HA1/HA2. The antibody neutralizes the virus by blocking conformational rearrangements associated with membrane fusion. The CR6261 epitope identified here should accelerate the design and implementation of improved vaccines that can elicit CR6261-like antibodies, as well as antibody-based therapies for the treatment of influenza.
http://www.sciencemag.org/cgi/content/abstract/1171491

Thursday, Feb. 26, 2009
NIAID MEDIA AVAILABILITY
Flu Virus Foiled Again
Second Research Team Finds Same Common Achilles’ Heel in Seasonal and Pandemic Flu Viruses

WHAT: Researchers at The Scripps Research Institute in La Jolla, California, supported in part by the National Institutes of Health, have identified a common Achilles’ heel in a wide range of seasonal and pandemic influenza A viruses. The study found an infection-fighting protein, or human antibody, that neutralizes various influenza A virus subtypes by attaching to these viruses in the same place. This common attachment site provides a constant region of the flu virus for scientists to target in an effort to develop a so-called universal flu vaccine. Such a vaccine would overcome the annual struggle to make the seasonal flu vaccine match next year’s circulating flu strains and might help blunt emerging pandemic influenza viruses as well.
The study provides data about the antibody attachment site that are similar to the findings of another research group, reported on February 22, 2009. Taken together, these studies provide a blueprint for efforts to develop new antiviral drugs as well as a potential universal influenza vaccine.

The Scripps research team, led by Ian A. Wilson, Ph.D., in collaboration with researchers at the biopharmaceutical company Crucell Holland (The Netherlands), discovered the potent antibody during a systematic examination of blood samples taken from healthy individuals who previously had been vaccinated with the ordinary seasonal flu vaccine. Using sophisticated screening technologies, the scientific team isolated antibodies that recognize flu viruses to which the average person has never been exposed, such as H5N1 avian flu viruses. Through this process, the scientists found one antibody called CR6261 that had broad neutralizing capabilities. Subsequently, they found several antibodies similar to CR6261 in other donors as well. With the help of a robotic crystallization laboratory, the Scripps team quickly determined the detailed three-dimensional structures of this antibody when bound to the H1 virus that caused the 1918 pandemic flu as well as to an H5 virus with pandemic potential. CR6261 bound to a relatively hidden part in the stem below the mushroom-shaped head of the hemagglutinin protein, one of two major surface proteins found on the flu virus.
The National Institute of Allergy and Infectious Diseases, the National Institute of General Medical Sciences, and the National Cancer Institute, all components of the National Institutes of Health, provided funding to this study.
ARTICLE: DC Ekiert et al. Antibody recognition of a highly conserved influenza virus epitope. Science DOI 10.1126/science.1171491 (2009).
WHO: NIAID Director Anthony S. Fauci, M.D., is available to comment on this study.
CONTACT: To schedule interviews, please contact Laurie K. Doepel, 301-402-1663, or niaidnews@niaid.nih.gov.

maandag 2 maart 2009 06:17
March 2, 2009
Volume 87, Number 09
p. 11
Structural Biology
Skeleton Key May Defuse Flu
Antibodies bind a flu protein nook common to many viral strains
Carmen Drahl
A FAMILY OF ANTIBODIES neutralizes multiple types of flu by targeting a weak spot in the virus, according to a pair of studies. The discovery could point the way to treatments that shield people from both seasonal and pandemic flu.
Every new year brings a new flu season and a new flu vaccine to go with it. Flu vaccines are developed by predicting which types of flu will dominate the coming season, structural biologist Ian A. Wilson of the Scripps Research Institute says. "If anything different comes along, the vaccine won't be as effective," he says.
Most vaccines elicit antibodies to hemagglutinin, a protein on the virus's surface. But the region of hemagglutinin that the antibodies target mutates rapidly, allowing viruses to elude human immune systems. Now, independent teams led by Wilson and Wayne A. Marasco of the Dana-Farber Cancer Institute, in Boston, have found antibodies targeting a portion of hemagglutinin that is less variable and is consistent in many types of flu.
Each team started with a library containing large numbers of antibodies compiled from human volunteers. Marasco's library was built in-house, whereas Wilson collaborated with Dutch biotechnology company Crucell. They fished out antibodies of interest by using avian flu hemagglutinin as their lure. With Ruben O. Donis of the Centers for Disease Control & Prevention, Marasco found that his handful of hits suppressed disparate types of flu in mice, a finding replicated by Wilson's team.
The antibodies are versatile because they don't interact with hemagglutinin's variable region. Two other groups found similar antibodies last year, but they didn't unambiguously describe their mechanism of action.
Now, to get at the mechanism, Marasco and Dana-Farber colleague Jianhua Sui teamed with Robert C. Liddington and William C. Hwang of the Burnham Institute for Medical Research, in La Jolla, Calif., to obtain a crystal structure of an antibody bound to avian flu hemagglutinin (Nat. Struct. Mol. Biol., DOI: 10.1038/nsmb.1566).
Independently, Wilson and Damian C. Ekiert obtained that structure, as well as one of an antibody bound to hemagglutinin from the 1918 epidemic flu (Science, DOI: 10.1126/science.1171491). In every structure, the antibody targets the same pocket, which is in the stem of hemagglutinin rather than its variable head.
The stem pocket is conserved because it is involved in a conformational change that's crucial for viral infection, Wilson says. With an antibody bound in this pocket, hemagglutinin can no longer change its shape, a step required before the virus can fuse with a cell and send in its genetic material.
Physicians might someday be able to inject this type of antibody into people infected with the flu, or the stem pocket could be used to make a new vaccine that doesn't need retooling every year, Marasco says.
"Hopefully, these works will provide a starting point for rational vaccine design and ultimately improve the therapeutic treatment of influenza," says Zihe Rao, an expert in crystallography of flu proteins at Tsinghua University, in Beijing.
http://pubs.acs.org/cen/news/87/i09/8709notw4.html

Dana-Farber video:
http://pubs.acs.org/cen/multimedia/87/flu/index.html?keepThis=true&TB_iframe=true&height=208&width=291
maandag 2 maart 2009 06:22
Team Finds Immune Molecule that Attacks Wide Range of Flu Viruses
By Renee Twombly and Mika Ono
Researchers at The Scripps Research Institute report the characterization of an immune system molecule that targets what appears to be an "Achilles heel" of a wide range of influenza viruses – including the viruses responsible for past global pandemics, those causing current common infections, and strains of bird flu believed to pose future world threats.
The discovery of the molecule, an antibody known as CR6261, is good news for researchers who hope to design a flu vaccine that would give humans lifelong protection against a majority of influenza viruses. The antibody also has the potential to treat those who are unvaccinated and become infected with the flu.
The team's findings were published in the February 26, 2009, issue of Science Express, an advance, online publication of selected research papers from the prestigious journal Science.
"This is very exciting because it marks the first step toward the Holy Grail of influenza vaccinology – the development of a durable and cross-protective universal influenza virus vaccine," says the study's senior investigator, Ian Wilson, a professor in the Department of Molecular Biology and a member of The Skaggs Institute for Chemical Biology at Scripps Research. "Such a flu vaccine could be given to a person just once and act as a universal protectant for most subtypes of influenza, even against pandemic viruses."
Flu vaccines now offer protection only for the specific strains of influenza that public health officials believe to be currently circulating in the population. This involves a lot of guesswork about which strains will be most prevalent and, because the virus is constantly mutating, this guesswork must be repeated year after year.
According to the U.S. Centers for Disease Control, in the United States more than 200,000 people are typically hospitalized from flu complications every year, and about 36,000 people die from the illness. But that is in a normal year. Over the past century, three major human influenza pandemics (the Spanish Flu of 1918-1919, the Asian Flu of 1957-1958, and the Hong Kong Flu of 1968-1969) have devastated the human population, killing around 50-100 million people worldwide.
Broad Action
In the new research paper, the scientists, composed of a team from Scripps Research and the biopharmaceutical company Crucell, in the Netherlands, show that the CR6261 antibody attaches to the virus that caused the devastating 1918 "Spanish flu" and to a virus of the "H5" class of avian influenza that jumped from chickens to a human in Vietnam in 2004 The scientists at Crucell previously demonstrated in laboratory experiments that this antibody can neutralize common, seasonal flu viruses.
"We can see exactly how and where the antibody grabs on to these influenza viruses," says the study's first author, Damian Ekiert, a graduate student in the Scripps Research Kellogg School of Science and Technology working in the Wilson laboratory. "And we can see that this same mode of interaction occurs in viruses that are very different from each other."
Wilson says the discovery was possible because of the modern tools that the research team employed, such as phage display to isolate antibodies from human blood, and a state-of-the-art robotic crystallization laboratory that helps solve the structures of microbial antigens much more quickly than in the past.
"I have been working with influenza virus antigens since 1987, and I find it just amazing to suddenly see antibodies now appear that we had no idea existed," Wilson says.
Researchers at Scripps Research and collaborating institutions have long been looking for influenza antibodies with a broader spectrum of action. To find these antibodies, the researchers extracted white blood cells from a healthy immunized volunteer to make a library of antibodies to look for antibodies that interact with viruses that the donors could not have come into contact with before, such as H5 avian influenza that has spread only from chickens to humans, but not from humans to humans.
The researchers found one such antibody in the blood of a donor who had recently been vaccinated with a flu shot to protect against H1 influenza virus, one of the seasonal subtypes that most commonly circulates in humans. That antibody was isolated and named CR6261—although some of the researchers later dubbed it "Supermantibody" when they began to realize how effective it was.
CR6261-like antibodies have now also been found in other people. According to Ekiert, it is likely that many people, if not all, have these antibodies, but the body doesn't always produce or use them efficiently.
Solving the Puzzle
The next step for the researchers was to understand exactly how CR6261 recognized and responded to such a broad array of influenza viruses.
To do that, Ekiert led the successful effort to solve two crystal structures: one with the antibody bound to the hemagglutinin H1 virus that caused the 1918 pandemic and another with the antibody glued to the hemagglutinin from the 2004 Vietnam H5 avian influenza.
Influenza antibodies, including those induced by current vaccines, target mushroom-shaped proteins known as hemagglutinin (HA) that stud the outer coat of a virus particle to help the virus infect cells of a host organism, such as humans.
What the Scripps Research scientists found is that CR6261 latches on to the "stalk" of the mushroom-like hemagglutinin particle, near where the protein juts out from the viral coat, and that this binding area, known as an epitope, is the same in both the H1 and H5 viruses. The scientists then analyzed the genome of more than 5,000 different influenza viruses and found the epitope's sequence is nearly identical in all of them, suggesting that this part of the virus is much more highly conserved than the virus's constantly mutating cap.
This insight into the way the CR6261 antibody binds to the virus's structure makes sense, the researchers say. It helps explains why the antibody may not be as powerful as it needs to be to attack influenza. "The epitope it needs to latch on to is at the base of the stalk of the hemagglutinin protein, so it is difficult to get to because these proteins are packed together tightly on the viral coat," Ekiert says. "Plus, most antibodies try to attack the mushroom cap of the hemagglutinin proteins because that is much more accessible, and so this probably sets up a huge competition between antibodies."
"Certain regions of the hemagglutinin protein are like big red flags to the immune system, but they are functionally unimportant," Wilson says. "The task now is to figure out how to suppress reactivity with those regions and enhance the immune system's attack on this conserved epitope."
maandag 2 maart 2009 06:23
vervolg.
It may also be possible that some people who rarely if ever contract the flu may have CR6261-like antibodies that are more efficient than others in neutralizing influenza viruses.
So far, the researchers have shown the CR6261 antibody works against many of the 16 different subtypes of influenza viruses. The antibody neutralized every H1 virus that the group tested, including those that have caused pandemics over the past 100 years. The antibody also worked on the H5 bird viruses that are not yet circulating in humans. However, the CR6261 antibody is not effective for the H3 subclass, which is a common human influenza virus, because a sugar molecule blocks the epitope.
"If a sugar is the only impediment in the way, we think there is a way around that in vaccine design," Wilson says. "Even so, this antibody could still potentially hit 12 out of the 16 influenza viral subtypes. We now have a blueprint upon which to design the next generation of anti-virals, and that is why we are so enthusiastic about these findings as they give hope that it may indeed be possible to generate a universal vaccine against influenza virus, as well as provide immediate protection when used as an antibody therapeutic."
In addition to Wilson and Ekiert, authors of the paper "Antibody recognition of a highly conserved epitope across influenza viruses" are Gira Bhabha and Marc-André Elsliger of Scripps Research, and Robert Friesen, Mandy Jongeneelen, Mark Throsby, and Jaap Goudsmit of Crucell Holland BV, Leiden, The Netherlands.
The work was funded by a grant from the National Institutes of Health, a predoctoral fellowship from the ARCS Foundation and the Skaggs Institute. Facilities supporting this work were funded by the NIH National Institute of General Medical Sciences, the National Cancer Institute, and the U.S. Department of Energy.
http://www.scripps.edu/newsandviews/e_20090302/flu.html
maandag 2 maart 2009 07:40
Hebben ze nu die mAb's alleen ontdekt en geisoleerd, of zou C hem ook al produceren?
maandag 2 maart 2009 18:09
Tamiflu-Resistant H1N1 Flu Virus Prevalence Increasing
By John Gever, Senior Editor, MedPage Today
Published: March 02, 2009
Reviewed by Dori F. Zaleznik, MD; Associate Clinical Professor of Medicine, Harvard Medical School, Boston.
ATLANTA, March 2 -- More than 12% of H1N1 influenza A infections in the U.S. last season were resistant to oseltamivir (Tamiflu) and the prevalence appears to be rising dramatically, according to a team of CDC-led researchers.

Moreover, the resistant strains appear no less virulent, debunking earlier suggestions that oseltamivir resistance would make the virus less dangerous.

Those findings emerged from a study of 1,155 H1N1 isolates from the 2007-2008 season by Nila J. Dharan, M.D., of the CDC, and colleagues from that agency and from several state public health laboratories, and reported online in the Journal of the American Medical Association
Mid-season data reported in February 2008 showed oseltamivir resistance on the rise generally among all flu virus serotypes. (See: Resistance to Oseltamivir (Tamiflu) Grows Higher)
Dr. Dharan examined records of 274 individual infections with H1N1 viruses, including 99 showing oseltamivir resistance.
"We found no significant difference in our comparison of the clinical symptoms and outcomes of untreated patients with oseltamivir-resistant and oseltamivir-susceptible influenza A(H1N1) infections," the researchers wrote.
One exception was that fewer hospitalizations were seen among those with resistant strains (2% versus 8%, P=0.005).
But virtually identical percentages of untreated patients took medications for fever and missed work or school, the researchers found.
Among patients who received antiviral agents, illness severity and outcomes were also similar.
Of 47 patients with resistant strains who received oseltamivir, five were hospitalized and four died.
Patient factors including demographics and flu vaccination history did not affect the likelihood of contracting oseltamivir-resistant H1N1 strains.
Dr. Dharan and colleagues also determined that rates of oseltamivir usage within a state did not correlate with the prevalence of resistant strains.
Of 22 states analyzed, only one had records of high oseltamivir usage (as measured by filled prescriptions) and high proportions of resistant strains, whereas four had high drug usage and low rates of resistant infection. Six states had relatively low levels of oseltamivir use and high rates of resistant infection.
The researchers also noted that early surveillance data for the current season have suggested that more than 90% of H1N1 viruses -- the most common now in circulation -- are resistant to oseltamivir. (See: Mild Flu Season So Far May Still Have Punch)
In an accompanying editorial, David M. Weinstock, M.D., and Gianna Zuccotti, M.D., both from Harvard, said the study helps "dispel the notion that oseltamivir resistance compromises virulence."
They also pointed to a small Dutch study, also reported online this week in JAMA, suggesting that one particular oseltamivir resistant strain may be even deadlier than normal for H1N1 viruses.
"The widespread belief that oseltamivir would retain activity against epidemic influenza strains has crumbled," Drs. Weinstock and Zuccotti wrote.
They added that this should not be surprising, given that a variety of studies have shown rising resistance to the drug beginning in the 2006-2007 season.
"For now, the best tools to mitigate influenza infection are tried-and-true -- vaccination, social distancing, hand washing, and common sense," they concluded.
http://www.medpagetoday.com/InfectiousDisease/URItheFlu/13072

http://jama.ama-assn.org/cgi/reprint/2009.294v1.pdf
http://jama.ama-assn.org/cgi/reprint/2009.297v1.pdf
*****************************

This makes it a potentially powerful antibody against a broad range of influenza strains. Fears of a flu pandemic are fuelled by the rising number of flu strains that have mutated in ways that make them resistant to oseltamivir.

Importantly, the study showed that CR6261 provides immediate protection against the influenza virus, suggesting that it will be able to prevent disease spread. In contrast, oseltamivir was less efficacious and in some cases not effective at all.

The advantages of the mAb over oseltamivir may also be important for protecting or treating people at risk of severe illness or death due to seasonal flu. These include the elderly and immune-suppressed individuals.
http://investors.crucell.com/C/132631/PR/200812/1276654_5_5.html
http://www.plosone.org/article/fetchObjectAttachment.action?uri=info%3Adoi%2F10.1371%2Fjournal.pone.0003942&representation=PDF
http://hugin.info/132631/R/1208066/249155.pdf

Preclinical study demonstrated antibody strongly outperformed oseltamivir
Provides immediate protection against influenza virus, suggesting ability to prevent
disease spread. Oseltamivir less efficacious and in some cases not effective at all
http://hugin.info/132631/R/1287817/289432.pdf

Oseltamivir will not be reliable in preventing viral spread as resistance may emerge
http://hugin.info/132631/R/1156548/223246.pdf
maandag 2 maart 2009 18:13
flosz schreef:

They also pointed to a small Dutch study, also reported online this week in JAMA, suggesting that one particular oseltamivir resistant strain may be even deadlier than normal for H1N1 viruses.

??? Enigszins degenererend niet waar?
maandag 2 maart 2009 18:54
Nee hoor, helemaal niet en ook niet denigrerend imo. (Deze studie is overigens geen verwijzing naar Crucell zoals je kunt zien).
zaterdag 21 maart 2009 11:23
Confirmation of Bogoch Replikins Influenza Patents By Harvard-CDC and Scripps-Crucell Data (March 20, 2009)

Boston, March 20, 2009. Replikins, Ltd. announced today that data recently published from Harvard-CDC and Scripps-Crucell in Nature1 and Science2 confirms the 2001 discoveries by Dr. Samuel and Elenore Bogoch of peptides in the hemagglutinin unit of influenza, which they named Replikins, which are shared across flu strains, conserved over time, associated with the last three pandemics of 1918, 1957 and 1968, as well as current H5N1 outbreaks, and are the basis of broad spectrum flu vaccines. The Replikins sequences, as specified by the Bogoches, are the subject of granted patents from 2001 and a 2005 monograph3.
The amino acid contact points between the neutralizing antibody and the virus that the Harvard-CDC and Scripps-Crucell investigators both observed, out of over 500 possible sites, are in the influenza Replikins. The confirming groups' data also verified the Bogoch 2001 findings of conservation of these very Replikins peptides over decades, and the sharing of Replikins between strains of influenza, making general flu vaccines possible for the first time.
The Replikins peptides, associated with rapid replication, are quantitatively trackable and predictive of the intensity, timing, and country of outbreak. The company's FluForecast® software has correctly predicted recent H5N1 outbreaks and the countries in which they were going to occur.4
Replikins, which are quantitatively related to lethality in influenza and other infectious diseases, such as HIV, anthrax, and malaria, as well as cancer, and a range of animal diseases, are the subject of synthetic vaccines in development at the Company.
1. Sui, J. et al. "Structural and functional bases for broad-spectrum neutralization of avian and human influenza A viruses.", Nature Structural and Molecular Biology, published online:22 February,2009, doi:10.1038-nsmb.1566.
2. Ekeirt, D.C. et al, "Antibody Recognition of a Highly Conserved Influenza Virus Epitope", Science DOI: 10.1126-science.1171491, Science Published online, Feb. 26 2009
3. Bogoch S. and Bogoch, E.S. Replikins, the Chemistry of Rapid Replication. With examples in influenza, HIV, AIDS, SARS, Malaria, and Cancer. Begell House,Inc. New York, Wallingford, U.K. ISBN 1-56700-200-5, 2005.
4. On-line: see 'Replikins Press', 2006 - 2008. (Press release #12 Indonesia Reports Experiencing Human H5N1 Mortality Increase, as Predicted Last Year by Replikins' FluForecast® Quantitative Virus Analysis (June 8, 2007)

REPLIKINS, Ltd. 38 the Fenway, Boston, MA 02215.
Contact: jjosephson@replikins.com
http://www.replikins.com/release.html#article25
zaterdag 21 maart 2009 14:50
flosz schreef:

Confirmation of Bogoch Replikins Influenza Patents By Harvard-CDC and Scripps-Crucell Data (March 20, 2009)

Boston, March 20, 2009. Replikins, Ltd. announced today that data recently published from Harvard-CDC and Scripps-Crucell in Nature1 and Science2 confirms the 2001 discoveries by Dr. Samuel and Elenore Bogoch of peptides in the hemagglutinin unit of influenza, which they named Replikins, which are shared across flu strains, conserved over time, associated with the last three pandemics of 1918, 1957 and 1968, as well as current H5N1 outbreaks, and are the basis of broad spectrum flu vaccines. The Replikins sequences, as specified by the Bogoches, are the subject of granted patents from 2001 and a 2005 monograph3.
...

Vrij vertaald: De onderzoekers van Crucell en Harvard hebben nu, in 2009, bevestigd wat wij, de Bogochjes van de firma Replikins, al in 2001 hebben ontdekt: de universele plekken van de verschillende griepvirussen, die nauwelijks veranderen, en bij al die griepvirussen hetzelfde zijn. Waarop vervolgens universele antibodies op te maken zijn. Wij hadden ze al "replikins" genoemd. En we hebben de patenten er al op.
zaterdag 21 maart 2009 18:55
flosz schreef:

Confirmation of Bogoch Replikins Influenza Patents By Harvard-CDC and Scripps-Crucell Data (March 20, 2009)

AB. Clever boys and Girls.
maandag 23 maart 2009 12:15
Het universele griepvaccin
Nieuwe antistoffen pakken virussen bij de wortels aan

Eén prik die beschermt tegen alle mogelijke griepvirussen, kan dat? Het lijkt er ineens wel op. Twee groepen onderzoekers hebben onafhankelijk van elkaar dezelfde truc gevonden om de virussen de voet dwars te zetten.
De dreigende taal van een paar jaar geleden hoor je niet vaak meer, maar het gevaar van een wereldwijde slachting door een nieuw griepvirus bestaat nog steeds. Hoe de dader er precies uit zal zien, dat kunnen virologen niet voorspellen. En dus proberen ze een wapen te vinden dat álle griepvirussen aankan.
Antistoffen die korte metten maken met iedere denkbare griepvariant hebben ze niet, schrijven twee groepen onderzoekers deze week in de wetenschappelijke tijdschriften Nature Structural & Molecular Biology en Science. Maar het scheelt toch niet veel. Ze hebben, onafhankelijk van elkaar, menselijke antistoffen ontdekt die meerdere gevaarlijke griepvirussen herkennen.
Onder die virussen waren twee echte killers: de veroorzaker van de vogelgriep die de afgelopen jaren in Azië honderden mensenlevens eiste, en het virus achter de Spaanse griep, die in 1918 en 1919 minstens vijftig miljoen mensen fataal werd. Bij mensen zijn de nieuwe antistoffen nog niet getest.

Levenslang
Normale antistoffen tegen griepvirussen kunnen maar één versie van de ziekteverwekker aan. Je lichaam maakt deze complexe moleculen na een griepinfectie, en voor de rest van je leven blijven ze in je bloed aanwezig, altijd alert op de griepvirussen van toen.
Ze passen op de oppervlaktemoleculen van hun ‘eigen’ virus als een sleutel in een slot. Zelfs na negentig jaar kunnen ze hun beschermende werk nog doen. Maar tegen een nieuw virus kunnen ze niks beginnen.
De verschillen tussen griepvirussen zitten vooral aan de buitenkant, in de eiwitten hemagglutinine (H) en neuraminidase (N). Verschillende vormen daarvan hebben allemaal een nummer gekregen. En daarom heet de veroorzaker van de Spaanse griep H1N1, en het recente vogelgriepvirus H5N1. De vogelgriep die Nederland in 2003 teisterde en één man het leven kostte, was van het type H7N7.

Afgetroefd
Onderzoekers van het Nederlandse bedrijf Crucell hebben samen met collega’s van het Californische Scripps Institute veel tijd en moeite gestoken in het selecteren van antistoffen die het H-eiwit van meerdere griepvirussen kunnen herkennen. Ze wisten er meerdere uit het bloed van een gezonde vrijwilliger te vissen. Met de beste gingen ze aan de slag. Die antistof bleek aan te grijpen op een onderdeel van het viruseiwit dat bij twaalf van de zestien typen griepverwekkers precies hetzelfde is, schrijven ze in Science.
Helaas voor de Nederlanders zijn ze afgetroefd door concurrenten die net iets eerder vergelijkbare resultaten naar buiten brachten, die nog indrukwekkender zijn ook. Onderzoekers uit een aantal Amerikaanse labs onthulden vijf dagen eerder dat ze wel negen verschillende antistoffen hebben gevonden die hetzelfde kunnen. De krachtigste hebben ze bovendien al op muizen hebben getest.
Die muizen werden bijna allemaal goed beschermd, of ze de antistoffen nu voor of vlak na de griepinfectie toegediend kregen. Controlemuizen gingen binnen twee weken dood, op één taai beestje na.
De antistoffen werken tegen meerdere virussen omdat ze een onderdeel van het H-eiwit herkennen dat maar in twee vormen voorkomt. Blijkbaar zijn dit de enige vormen die geschikt zijn voor het werk dat het eiwit moet doen: de fusie tot stand brengen tussen het membraan dat het virus omhult en het celmembraan van de menselijke cel waar het zijn ziekmakende inhoud in kwijt wil.

Onbereikbaar
Dat deel van het eiwit zit niet helemaal aan de buitenkant, maar dicht tegen het membraan van het virus aan. Onbereikbaar voor antistoffen, zou je denken, want die zouden zich eerst door de buitenste laag heen moeten wringen. De muizenproef bewijst dat ze dat toch kunnen.
Je kunt je afvragen waarom het menselijk lichaam zelf niet op het idee komt om dit type antistoffen te maken. De reden is waarschijnlijk simpel: antistoffen tegen de buitenste laag van het virus zijn veel eenvoudiger te maken, en ook nog eens effectiever. Tegen dat ene virus dan.
Vooruitkijken, dat kan het lichaam niet, dus de snelste methode om het virus te verslaan wint altijd. Mensen kunnen wél nadenken over de toekomst en proberen die naar hun hand te zetten. Bijvoorbeeld door de antistoffen tegen griep al paraat te hebben voordat het virus zich aandient. Dat kan door vaccinatie.

Inenten
Nu zijn er twee manieren waarop je iemand kunt inenten tegen griep. De ene is door kant-en-klare antistoffen in te spuiten. Dat zou in principe nu al kunnen met de nieuw gevonden antistoffen, mits ze op grote schaal gekweekt kunnen worden – en dat zal wel lukken. Een nadeel van deze methode is, dat de bescherming na een tijdje minder wordt. Bovendien is het denkbaar dat de vreemde antistoffen het lichaam zelf aanvallen.
De tweede methode is iets inspuiten dat het afweersysteem stimuleert om eigenhandig de gewenste antistoffen te gaan maken. Zoiets gebeurt nu al – dat is de jaarlijkse griepprik – maar daarbij worden alleen antistoffen opgewekt die passen bij specifieke virussen, waarvan verwacht wordt dat ze in het komende jaar zullen toeslaan.
Dat kan waarschijnlijk dus beter: door losse onderdelen van de twee versies van het H-eiwit in te spuiten, die zelf ongevaarlijk zijn, of een type eiwit dat daar sterk op lijkt. Als dat goed werkt, zou iemand in één klap beschermd zijn tegen alle griepvirussen die er bestaan. Zoiets zou miljoenen levens kunnen redden.
Zo ver is het nog niet. Het staat natuurlijk ook niet voor honderd procent vast dat het zo ver komt. Maar het zou goed kunnen. En het mooiste is misschien wel, dat ook andere virussen met een soortgelijke aanpak bestreden kunnen worden. Ook ebola en hiv hebben stukken eiwit die altijd hetzelfde zijn.
Elmar Veerman

Naschrift: De resultaten van de andere groep zijn helemaal niet indrukwekkender, vindt een woordvoerder van Crucell. Want zijn bedrijf rapporteerde al in december vorig jaar http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0003942 over dit type antistoffen, en had de beste toen ook al met succes op muizen getest. http://investors.crucell.com/C/132631/PR/200812/1276654_5_5.html Dus wie heeft wie nou afgetroefd?

Jianhua Sui e.a.: Structural and functional bases for broad-spectrum neutralization of avian and human influenza A viruses, Nature Structural & Molecular Biology, 22 februari 2009
Damian C. Ekiert e.a.: Antibody recognition of a highly conserved influenza virus epitope, Sciencexpress, 26 februari 2009
http://noorderlicht.vpro.nl/artikelen/41559557/
maandag 23 maart 2009 14:01
Cover Story - Drug delivery
Haas, M. SciBX 2(10); doi:10.1038/scibx.2009.388
Published online March 12 2009


Bulking up immunity with instant Abs
by Michael J. Haas, Senior Writer

When Pfizer Inc. bought CovX Pharmaceuticals Inc. in 2007, the driver of the deal was the biotech's CovX-Body technology, which used a single antibody as a scaffold on which to build multiple product candidates that could be given via infusion. Pfizer may earn bonus miles from its acquisition, as CovX's cofounder at The Scripps Research Institute has now devised a way to produce the antibody therapeutics entirely in vivo, potentially obviating the need for infusions.
The technology, which is already licensed to Pfizer, uses a vaccine to induce the antibody scaffold, then a chemical agent to modify and direct the antibody against a specific disease target, thereby providing what the Scripps team has termed "instant immunity."
The group has shown proof of principle in mouse models of cancer and thinks the technology for chemically programmed antibodies could work against infectious diseases.
Unlike most antibodies, which bind their targets noncovalently, the antibody scaffolds used by Pfizer and Scripps are capable of binding their targets covalently, so that antibody and target fuse into a single molecule. Such antibodies were first reported in 1995 by a team led by Carlos Barbas III, chair of molecular biology at Scripps. The group found that mice injected with a small molecule (1,3-diketone) always developed antibodies that could covalently bind that molecule.1
According to team member Richard Lerner, now president at Scripps as well as a professor of chemistry and immunochemistry, this led to the hypothesis that the antibodies could be programmed against disease targets by linking a target-specific molecule to the antibody-inducing diketone.
Lerner and Barbas formed CovX in 2002 to commercialize these antibodies.

Abs training
The first-generation therapeutics are produced ex vivo and must be delivered by infusion. The latest Scripps work, also led by Barbas, investigated whether therapeutic antibodies could be produced and programmed entirely in vivo.
First, the team ascertained whether the anti-diketone antibody scaffold could find and bind a programming agent in vivo. To do this, they inoculated healthy mice with a vaccine based on a 1,3-diketone. Sixty-five days later they injected the mice with a programming agent composed of a diketone linked to an inhibitor of two antiangiogenic integrins: integrin v 3 and integrin v 5.
Experiments on serum pooled from the treated mice confirmed that the antibodies and programming agent had indeed found one another in vivo and fused into programmed antibodies (see Figure 1, "Production of chemically programmed antibodies in vivo"). http://www.nature.com/scibx/journal/v2/n10/fig_tab/scibx.2009.388_F1.html

The team repeated the treatment with the vaccine and programming agent in mouse models of colon cancer and melanoma and observed decreases in tumor growth of more than 75% compared with that seen in controls.
The findings were published in the Proceedings of the National Academy of Sciences.2
In the paper, the team also suggested that programmed antibodies could induce immunity against infectious diseases such as HIV, malaria and pandemic flu.
To do so, Lerner told SciBX that humans could be inoculated with the diketone at any time to induce the programmable antibodies. "You could then give a chemical programming agent as needed to activate this reservoir of antibodies" against an emerging disease or even a chemical threat such as nerve gas to confer immunity almost instantaneously, he said. Lerner added that chemical programming agents could be taken orally.
Barbas noted that the approach would have lower production and prescription costs than infused antibody therapies.

Abs vantage points
Other researchers agreed that the technology is ready to test in cancer and potentially autoimmune disease, but they said direct evidence for its effectiveness against infectious disease is lacking.

Fons Uytdehaag, senior director of R&D strategy development at vaccine company Crucell N.V., said the Scripps approach has a big advantage over immunization with recombinant or vectored vaccines because it induces a universal immune response and memory, then rapidly directs that response against a disease target with the chemical programming agent.
Eric Guenzi, associate director of immunology research at cancer and autoimmune disease company MediGene AG, agreed that the instant immunity conferred by programmed antibodies offers a major selling point over conventional vaccines or infused antibody therapy.
"You could use this approach to re-create and reprogram therapeutic agents—which previously would have to be injected—by inducing instant immunity through vaccination with reactive compounds," he said. "With this system, your body does the job."
Guenzi said the results in cancer were promising, but he wanted to see animal studies showing that programmed antibodies could induce regression in established tumors and prevent metastasis. "It would be highly relevant to check the efficacy of the reprogrammed antibodies after the tumor has been established" for 2–3 weeks instead of beginning treatment before increasing tumor volume or tumor growth were measurable, as the Barbas collaborators did in their study, he said.
Guenzi also wanted to see experiments against more established cancer targets. "To my knowledge, the efficacy of inhibitors of v 3 and v 5 integrins has not been established in the clinic," he said.
Nevertheless, Guenzi noted that past approaches to treating cancer with therapeutic antibodies required adjuvant therapy. "Here they showed inhibition of tumor growth without recourse to adjuvant therapy, which is a clear advantage," he said.
Guenzi said the Barbas team's approach also allowed control over the immune response to self-antigens, which would avoid long-term safety issues that could arise when vaccinating against self-antigens.
"This is the first time I've read about something that combines an immunization approach with a short, intense reaction that controls the immune response and the memory of immune response," he said. "If you stop taking the programming agent, you stop the reactions, making the immune response controllable and reversible. This is a very important point for both cancer and autoimmune conditions."
Robert Rickert, associate professor of inflammatory diseases at the Burnham Institute for Medical Research, agreed that the technology provides a broad platform that could apply to multiple diseases. "The key will be to find appropriate therapeutic molecules or peptides that can be combined with the diketone" to make programming agents that are as effective as those used in the PNAS study, he said.
Barbas said his group has not encountered any significant difficulties in synthesizing programming agents. "Usually there is a site on a therapeutic peptide or small molecule that can be used for linkage" to the diketone, he said.

maandag 23 maart 2009 14:02
Ab extensions
There was less consensus about whether the technology could extend to infectious diseases.
Rickert said the technology's effectiveness against infection needs to be demonstrated, "but it is a perfectly valid extrapolation to make from these findings. The challenge with targeting pathogens will be that they are constantly evolving and mutating."
Thus, he said a programming agent should direct antibodies against a conserved site on a pathogen. Otherwise, the agent would be useless once the pathogen mutates—for example, as seasonal flu does.
MediGene's Guenzi was more cautious. "There is no evidence in the paper that this system could be used for non–self-antigens," he said.
Crucell's Uytdehaag agreed that preventing infection with programmed antibodies was a long way off. "For vaccination against viral diseases, it remains to be demonstrated whether programmed antibodies can neutralize—not just bind—a virus," he said.
Uytdehaag said that success in treating malaria, HIV and flu would depend on developing chemical programming agents with high affinity for the pathogens. He agreed with Rickert that such agents should target highly conserved epitopes to prevent escape mutations.
Uytdehaag also said there would be logistical issues in using the programmable antibodies for many infectious diseases.
"The broad and universal applicability of the technology to create instant immunity in the event of, for example, a flu pandemic, would require a pre-existing immunity to the [diketone] in the general population," he said. "Mass immunization early in life to generate a long-lived memory B cell response to the diketone is theoretically possible, but there may be ethical and regulatory issues involved with such an approach."
Rickert disagreed, noting that the diketone used by the Barbas team was inert, did not accumulate in the body and had no known human toxicity.
Lerner concurred with Rickert, adding that the compounds used by CovX and Pfizer to induce the antibody scaffolds have long-standing safety records in humans. Thus, he didn't anticipate significant ethical or regulatory hurdles to generating pre-existing, programmable immunity in the general population.
Barbas said his group has developed a variety of different antibodies that are also suitable for chemical programming and just as versatile as the anti-diketone antibodies. He added that his group is working to advance the technology described in PNAS to treat HIV, influenza and cancer.
Lerner said Scripps holds all of the IP related to chemically programmed antibodies and Pfizer has licensed the rights.
http://www.nature.com/scibx/journal/v2/n10/full/scibx.2009.388.html
donderdag 26 maart 2009 04:39
Cover Story - Infectious disease
Haas, M. SciBX 2(9); doi:10.1038/scibx.2009.344
Published online March 5 2009
Anti-flubodies
by Michael J. Haas, Senior Writer

Two separate teams have isolated human antibodies that neutralize many variants of influenza antigen hemagglutinin A and prevent viral entry and infection. Both teams are developing their antibodies as therapeutics but are going after different markets: one is targeting pandemic flu outbreaks whereas the other wants to use its antibodies to treat or prevent seasonal flu in immunocompromised populations.
Though potentially useful additions to the anti-influenza armamentarium, the antibodies are not likely to replace vaccines as the primary defense against the disease.
Influenza antigen hemagglutinin A is a protein expressed on the viral surface that has two main regions: a globular head that enables viral attachment and fusion and a stem region that is buried in the viral envelope and undergoes a conformational change to allow viral entry and infection after fusion. There are 16 different hemagglutinin subtypes that fall into two groups. The 10 subtypes in Group 1 include H1, which occurs most frequently in seasonal influenza strains but also includes the pandemic 1918 flu virus, and H5, which includes the highly pathogenic strains of avian flu. Among the six Group 2 subtypes is H3, which also occurs in seasonal flu strains.
Another surface protein, neuraminidase, helps mature virus exit the infected host cell so that it can infect a new cell. Neuraminidase has nine subtypes, each of which can occur in combination with any hemagglutinin subtype. Thus, influenza viruses are designated according to their specific hemagglutinin and neuraminidase subtype—for example, H5N1.
Influenza infections and vaccinations mostly stimulate antibodies against the hemagglutinin head because it is exposed to the immune system during viral fusion and entry. The problem is that the head region mutates readily without losing its attachment or fusion function, thereby evading anti-hemagglutinin antibodies.
Such mutations also make it difficult to predict which influenza strain will be in circulation from one season to the next. Thus, there is a market for therapeutics or prophylactics that are simultaneously effective against many strains of seasonal and/or pandemic strains.
A team from the Dana-Farber Cancer Institute, the Burnham Institute for Medical Research and the Centers for Disease Control and Prevention (CDC) set out to isolate antibodies that would block multiple strains of H5N1 influenza.
They screened a human antibody library against recombinant H5 and isolated three leads that neutralized all nine Group 1 subtypes that they tested against in human cell lines.
Mice injected with any of three antibodies one hour before challenge with H5N1 or up to 48 hours after viral challenge survived and showed few or no clinical signs of infection. The antibodies also protected mice from two lethal strains of H1N1.
X-ray crystallography of an H5 hemagglutinin-antibody cocrystal showed that the antibody bound an epitope on the hemagglutinin stem that is conserved across all Group 1 subtypes.
All six Group 2 subtypes had a different conserved epitope at this stem position.
In a report in Nature Structural and Molecular Biology, the team said their results suggest that the antibodies could provide broad-spectrum protection against pandemic and seasonal flu viruses.1
On a conference call, team coleader Wayne Marasco, associate professor of medicine at Dana-Farber and Harvard Medical School, said the group is developing the antibodies primarily to contain pandemic outbreaks. The antibodies would be given to family members, co-workers and healthcare workers who come in close contact with an infected individual, he said.
"These antibodies are ready to go," team coleader Robert Liddington told SciBX. They could "snuff out a pandemic."
Liddington is professor and director of the infectious disease program at Burnham. Ruben Donis, chief of the CDC's molecular virology and vaccines branch, also co-led the Nature Structural and Molecular Biology study.

Another flu in the ointment
In addition to the Nature Structural and Molecular Biology paper, two papers from Crucell N.V. and others described the identification of human antibodies that could neutralize different hemagglutinin subtypes and detailed the underlying mechanism of how the neutralization occurred.2, 3
In a paper published in PLoS One, the team constructed combinatorial display libraries using antibodies recovered from the serum of individuals inoculated against H1N1 virus and then screened those libraries against recombinant H5 hemagglutinin. The lead antibody from that screen, CR6261, neutralized all six Group 1 subtypes of hemagglutinin it was tested against; the team did not test the other four subtypes.
The antibody also protected mice from challenge with lethal strains of H5N1 or H1N1.
In a follow-on study in Science, another Crucell-led team reported structural studies of an H5 hemagglutinin–CR6261 cocrystal that showed that the antibody targeted the same conserved epitope identified in the Nature Structural and Molecular Biology study.
The PLoS One team, led by Crucell CSO Jaap Goudsmit, also included researchers from The University of Hong Kong's Queen Mary Hospital, Algonomics N.V., Wageningen University, Johann Wolfgang Goethe University and Bambino Gesú Children's Hospital.
The Science team was led by Ian Wilson, professor of molecular biology at The Scripps Research Institute, and included Goudsmit and other researchers from both Crucell and Scripps.
Scripps' Wilson told SciBX that a team of researchers from Scripps and Sea Lane Biotechnologies LLC had previously reported antibodies that neutralized both the H1 and H5 subtypes.4 However, the researchers could not identify the actual hemagglutinin epitope targeted by the antibodies because they did not have a hemagglutinin-antibody cocrystal structure.

donderdag 26 maart 2009 04:40
New flu tools
Although the antibodies identified by the Nature Structural and Molecular Biology and Crucell teams could help treat or prevent both seasonal and pandemic influenza, logistical and commercial drawbacks might limit utility.
Penny Heaton, CMO of Novavax Inc., noted that more than one dose probably would be required during the course of a season or pandemic because the typical antibody has a half-life of four to six weeks.
Thus, she said, "antibodies are not the be-all or end-all treatment for pandemic or seasonal flu."
Novavax has virus-like particle (VLP)-based vaccines against pandemic influenza in Phase II testing and expects to begin two Phase IIa trials of a VLP-based vaccine against seasonal flu this year.
Bill Enright, president and CEO of Vaxin Inc., agreed that half-life is important.
Vaxin is developing seasonal and pandemic influenza vaccines that express H1 or H5 in an adenovirus vector. The pandemic vaccine is in Phase I testing; the company hopes to begin Phase II testing of the seasonal vaccine this year. The vaccines are delivered by intranasal inhalation rather than intramuscular injection.
"We have seen immune responses to our vaccines that last more than one year," Enright said.
Alan Shaw, president and CEO of VaxInnate Corp., also thinks an influenza antibody would face several hurdles. He said the doses needed to protect mice in both the Nature Structural and Molecular Biology and Crucell studies translated to huge doses in humans: about 1,500 mg for a 100-kg person. Thus, Shaw thinks it would be very hard to produce and distribute sufficient quantities of the antibodies and that production and prescription costs would be prohibitive.
VaxInnate has H1- and H5-based vaccines in Phase I testing for seasonal and pandemic influenza.
Both Larry Smith, VP of vaccine research at Vical Inc., and George Kemble, VP of R&D and general manager of vaccines at the MedImmune Inc. subsidiary of AstraZeneca plc, agreed that the antibodies faced major logistical hurdles.
Smith pointed to the unknown treatment dose, unknown duration of protection and potentially high cost of antibody protection as significant disadvantages.
Last year Vical completed Phase I testing of a plasmid DNA vaccine encoding H5 to prevent pandemic influenza.
"The quantity of material required to protect an adult population from infection for three to six months or more during a pandemic is staggering," Kemble said.
He suggested that using the antibodies to treat individual cases of influenza would be a more manageable option. "Having another tool at the bedside to intervene in what could be a severe or lethal infection would complement, but not replace," prophylactic vaccinations, he said.
MedImmune markets FluMist, a live attenuated influenza vaccine (LAIV) to prevent seasonal flu. The company also has an LAIV in Phase I testing to prevent pandemic flu.
Goudsmit noted that Crucell's CR6261 also protected ferrets from influenza up to six days after infection at doses that are feasible in humans. The company plans to develop CR6261 to treat or prevent seasonal influenza in at-risk populations. These include children, the elderly and immunocompromised individuals who are not always well protected by marketed vaccines.
According to Goudsmit, seasonal flu infects about 200,000 elderly people in the U.S.—of which about 35,000 die—and the U.S. represents about half of the $2.2 billion global market of elderly patients. "The size of the problem observed in these populations with seasonal flu vaccines indicates a major unmet medical need," he said.
On the pandemic front, Heaton said antibodies might not be the best approach.
"Pandemic infection is so aggressive that the early-stage immune response causes respiratory problems" and eventually pneumonia, she noted. The reason is the virus spreads through the respiratory system quickly—a process that is inhibited primarily by the immune response to neuraminidase. Thus, an anti-hemagglutinin antibody might not halt respiratory spread of a pandemic virus.
Heaton said Novavax's pandemic and seasonal influenza vaccines offer broader protection than antibodies because they are based on recombinant hemagglutinin, neuraminidase and one other viral surface protein, matrix protein 1. She said this combination induces three distinct immune responses in a vaccinated individual: antibodies against hemagglutinin, a cell-mediated response to neuraminidase that slows the progression to pneumonia and the induction of cytotoxic lymphocytes that kill infected cells.
Heaton added that it was almost impossible to completely prevent viral entry. Thus, "depending on an anti-hemagglutinin antibody alone is a very tall order," she said.
Vical's Smith agreed. Although developing a vaccine from the findings of the Nature Structural and Molecular Biology and Crucell teams would require more work than developing the antibodies, "vaccination ultimately would be a better strategy for controlling the morbidity and mortality of influenza viruses," he said.

Antibody flight plans
Marasco said the Nature Structural and Molecular Biology team will seek partners in government or industry to develop the antibodies. The team hopes to take the antibodies into the clinic by the winter of 2011–2012.
Liddington said the team's other priorities include isolating antibodies against the Group 2 epitope and performing additional screens to identify back-up antibodies against Group 1 subtypes. A combination of antibodies targeting Group 1 and Group 2 subtypes could be used against any flu virus, he said.
Indeed, Goudsmit said Crucell has already isolated an antibody that targets the conserved Group 2 epitope and plans to develop it in combination with CR6261 to treat or prevent seasonal flu in at-risk populations.
The company expects to start clinical trials within the next two years, he said.
The findings reported in Nature Structural and Molecular Biology are patented by Dana-Farber and Burnham and are available for licensing, according to Ruth Emyanitoff, senior licensing manager at Dana-Farber. The findings reported in PLoS One and Science are patented by Crucell.
http://www.nature.com/scibx/journal/v2/n9/pdf/scibx.2009.344.pdf
donderdag 26 maart 2009 07:32
Crucell teams could help treat or prevent both seasonal and pandemic influenza, logistical and commercial drawbacks might limit utility.
Voor logostiek en commerce zijn oplossingen te bedenken.
Ik denk dat we 500 mega productie faciliteiten nodig hebben om aan de vraag te voldoen bij een pandemie.
Regeringen wereldwijd kunnen Crucell inhuren om dit voor ze te regelen.( uiteraard moeten ze vooruit betalen)
Eddy


maandag 18 mei 2009 19:34
flosz schreef:

Published Online February 26, 2009
Science DOI: 10.1126/science.1171491
REPORTS
Submitted on January 27, 2009
Accepted on February 19, 2009

Antibody Recognition of a Highly Conserved Influenza Virus Epitope
Damian C. Ekiert 1, Gira Bhabha 1, Marc-André Elsliger 1, Robert H. E. Friesen 2, Mandy Jongeneelen 2, Mark Throsby 2, Jaap Goudsmit 2, Ian A. Wilson 3*
1 Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
2 Crucell Holland BV, Archimedesweg 4-6, 2301 CA Leiden, The Netherlands.
3 Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.; The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
* To whom correspondence should be addressed.
Ian A. Wilson , E-mail: wilson@scripps.edu
Influenza virus presents a significant and persistent threat to public health worldwide, and current vaccines provide immunity to viral isolates similar to the vaccine strain. High-affinity antibodies against a conserved epitope could provide immunity to the diverse influenza subtypes and protection against future pandemic viruses. Co-crystal structures were determined at 2.2 and 2.7 Å resolutions for broadly neutralizing human antibody CR6261 Fab in complexes with the major surface antigen (hemagglutinin, HA) from viruses responsible for the 1918 H1N1 influenza pandemic and a recent lethal case of H5N1 avian influenza. In contrast to other structurally characterized influenza antibodies, CR6261 recognizes a highly conserved helical region in the membrane-proximal stem of HA1/HA2. The antibody neutralizes the virus by blocking conformational rearrangements associated with membrane fusion. The CR6261 epitope identified here should accelerate the design and implementation of improved vaccines that can elicit CR6261-like antibodies, as well as antibody-based therapies for the treatment of influenza.
http://www.sciencemag.org/cgi/content/abstract/1171491




Perspective abstract
________________________________________
Nature Immunology 10, 573 - 578 (2009)
Published online: 18 May 2009 | doi:10.1038/ni.1746
HIV-1 and influenza antibodies: seeing antigens in new ways
Peter D Kwong1 & Ian A Wilson2
________________________________________
Abstract
New modes of humoral recognition have been identified by studies of antibodies that neutralize human immunodeficiency virus type 1 and influenza A viruses. Understanding how such modes of antibody-antigen recognition can occur in the context of sophisticated mechanisms of humoral evasion has implications for the development of effective vaccines. Here we describe eight modes of antibody recognition first observed with human immunodeficiency virus type 1. Similarities to four of these modes have been identified with antibodies to a conserved 'stem' epitope on influenza A viruses. We outline how each of these different modes of antibody recognition is particularly suited to overcoming a specific viral evasion tactic and assess potential routes of re-elicitation in vaccine settings.
Top of page
________________________________________
1. Peter D. Kwong is with the Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland, USA.
e-mail: pdkwong@nih.gov
2. Ian A. Wilson is in the Department of Molecular Biology and the Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California, USA.
http://www.nature.com/ni/journal/v10/n6/abs/ni.1746.html
dinsdag 16 juni 2009 01:48
http://www.sciencemag.org/cgi/data/1171491/DC1/1
 
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71.917
27.985
27.651
18.697
17.841
8.791
6.668
5.941
4.180
2.957


 
 


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