Haemagglutinin mutations responsible for the binding of H5N1 influenza A viruses to human-type receptors
Pandemic potential The fact that the H5N1 bird flu virus circulating in Asia, Europe and Africa is unable to attach to human-type cell receptors has helped to prevent it from causing a worldwide epidemic of a human variant of the disease. Now a study of H5N1 isolates from some of the few humans that...
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| Published in | Nature Vol. 444; no. 7117; pp. 378 - 382 |
|---|---|
| Main Authors | , , , , , , , , , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
London
Nature Publishing Group UK
16.11.2006
Nature Publishing Nature Publishing Group |
| Subjects | |
| Online Access | Get full text |
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| Abstract | Pandemic potential
The fact that the H5N1 bird flu virus circulating in Asia, Europe and Africa is unable to attach to human-type cell receptors has helped to prevent it from causing a worldwide epidemic of a human variant of the disease. Now a study of H5N1 isolates from some of the few humans that have been infected (from Vietnam and Thailand) has identified two mutations in a viral haemagglutinin that allow it to bind to both human and avian receptors. These mutations might be of use as molecular markers for assessing the pandemic potential of H5N1 field isolates.
H5N1 influenza A viruses have spread to numerous countries in Asia, Europe and Africa, infecting not only large numbers of poultry, but also an increasing number of humans, often with lethal effects
1
,
2
. Human and avian influenza A viruses differ in their recognition of host cell receptors: the former preferentially recognize receptors with saccharides terminating in sialic acid-α2,6-galactose (SAα2,6Gal), whereas the latter prefer those ending in SAα2,3Gal (refs
3–6
). A conversion from SAα2,3Gal to SAα2,6Gal recognition is thought to be one of the changes that must occur before avian influenza viruses can replicate efficiently in humans and acquire the potential to cause a pandemic. By identifying mutations in the receptor-binding haemagglutinin (HA) molecule that would enable avian H5N1 viruses to recognize human-type host cell receptors, it may be possible to predict (and thus to increase preparedness for) the emergence of pandemic viruses. Here we show that some H5N1 viruses isolated from humans can bind to both human and avian receptors, in contrast to those isolated from chickens and ducks, which recognize the avian receptors exclusively. Mutations at positions 182 and 192 independently convert the HAs of H5N1 viruses known to recognize the avian receptor to ones that recognize the human receptor. Analysis of the crystal structure of the HA from an H5N1 virus used in our genetic experiments shows that the locations of these amino acids in the HA molecule are compatible with an effect on receptor binding. The amino acid changes that we identify might serve as molecular markers for assessing the pandemic potential of H5N1 field isolates. |
|---|---|
| AbstractList | H5N1 influenza A viruses have spread to numerous countries in Asia, Europe and Africa, infecting not only large numbers of poultry, but also an increasing number of humans, often with lethal effects. Human and avian influenza A viruses differ in their recognition of host cell receptors: the former preferentially recognize receptors with saccharides terminating in sialic acid-alpha2,6-galactose (SAalpha2,6Gal), whereas the latter prefer those ending in SAalpha2,3Gal (refs 3-6). A conversion from SAalpha2,3Gal to SAalpha2,6Gal recognition is thought to be one of the changes that must occur before avian influenza viruses can replicate efficiently in humans and acquire the potential to cause a pandemic. By identifying mutations in the receptor-binding haemagglutinin (HA) molecule that would enable avian H5N1 viruses to recognize human-type host cell receptors, it may be possible to predict (and thus to increase preparedness for) the emergence of pandemic viruses. Here we show that some H5N1 viruses isolated from humans can bind to both human and avian receptors, in contrast to those isolated from chickens and ducks, which recognize the avian receptors exclusively. Mutations at positions 182 and 192 independently convert the HAs of H5N1 viruses known to recognize the avian receptor to ones that recognize the human receptor. Analysis of the crystal structure of the HA from an H5N1 virus used in our genetic experiments shows that the locations of these amino acids in the HA molecule are compatible with an effect on receptor binding. The amino acid changes that we identify might serve as molecular markers for assessing the pandemic potential of H5N1 field isolates. Pandemic potential The fact that the H5N1 bird flu virus circulating in Asia, Europe and Africa is unable to attach to human-type cell receptors has helped to prevent it from causing a worldwide epidemic of a human variant of the disease. Now a study of H5N1 isolates from some of the few humans that have been infected (from Vietnam and Thailand) has identified two mutations in a viral haemagglutinin that allow it to bind to both human and avian receptors. These mutations might be of use as molecular markers for assessing the pandemic potential of H5N1 field isolates. H5N1 influenza A viruses have spread to numerous countries in Asia, Europe and Africa, infecting not only large numbers of poultry, but also an increasing number of humans, often with lethal effects 1 , 2 . Human and avian influenza A viruses differ in their recognition of host cell receptors: the former preferentially recognize receptors with saccharides terminating in sialic acid-α2,6-galactose (SAα2,6Gal), whereas the latter prefer those ending in SAα2,3Gal (refs 3–6 ). A conversion from SAα2,3Gal to SAα2,6Gal recognition is thought to be one of the changes that must occur before avian influenza viruses can replicate efficiently in humans and acquire the potential to cause a pandemic. By identifying mutations in the receptor-binding haemagglutinin (HA) molecule that would enable avian H5N1 viruses to recognize human-type host cell receptors, it may be possible to predict (and thus to increase preparedness for) the emergence of pandemic viruses. Here we show that some H5N1 viruses isolated from humans can bind to both human and avian receptors, in contrast to those isolated from chickens and ducks, which recognize the avian receptors exclusively. Mutations at positions 182 and 192 independently convert the HAs of H5N1 viruses known to recognize the avian receptor to ones that recognize the human receptor. Analysis of the crystal structure of the HA from an H5N1 virus used in our genetic experiments shows that the locations of these amino acids in the HA molecule are compatible with an effect on receptor binding. The amino acid changes that we identify might serve as molecular markers for assessing the pandemic potential of H5N1 field isolates. H5N1 influenza A viruses have spread to numerous countries in Asia, Europe and Africa, infecting not only large numbers of poultry, but also an increasing number of humans, often with lethal effects. Human and avian influenza A viruses differ in their recognition of host cell receptors: the former preferentially recognize receptors with saccharides terminating in sialic acid-[greek letter alpha] 2,6-galactose (SA [greek letter alpha]2,6Gal), whereas the latter prefer those ending in SA [greek letter alpha]2,3Gal. A conversion from SA[greek letter alpha]2,3Gal to SA[greek letter alpha]2,6Gal recognition is thought to be one of the changes that must occur before avian influenza viruses can replicate efficiently in humans and acquire the potential to cause a pandemic. By identifying mutations in the receptor-binding haemagglutinin (HA) molecule that would enable avian H5N1 viruses to recognize human-type host cell receptors, it may be possible to predict (and thus to increase preparedness for) the emergence of pandemic viruses. Here we show that some H5N1 viruses isolated from humans can bind to both human and avian receptors, in contrast to those isolated from chickens and ducks, which recognize the avian receptors exclusively. Mutations at positions 182 and 192 independently convert the HAs of H5N1 viruses known to recognize the avian receptor to ones that recognize the human receptor. Analysis of the crystal structure of the HA from an H5N1 virus used in our genetic experiments shows that the locations of these amino acids in the HA molecule are compatible with an effect on receptor binding. The amino acid changes that we identify might serve as molecular markers for assessing the pandemic potential of H5N1 field isolates. H5N1 influenza A viruses have spread to numerous countries in Asia, Europe and Africa, infecting not only large numbers of poultry, but also an increasing number of humans, often with lethal effects. Human and avian influenza A viruses differ in their recognition of host cell receptors: the former preferentially recognize receptors with saccharides terminating in sialic acid-alpha2,6-galactose (SAalpha2,6Gal), whereas the latter prefer those ending in SAalpha2,3Gal (refs 3-6). A conversion from SAalpha2,3Gal to SAalpha2,6Gal recognition is thought to be one of the changes that must occur before avian influenza viruses can replicate efficiently in humans and acquire the potential to cause a pandemic. By identifying mutations in the receptor-binding haemagglutinin (HA) molecule that would enable avian H5N1 viruses to recognize human-type host cell receptors, it may be possible to predict (and thus to increase preparedness for) the emergence of pandemic viruses. Here we show that some H5N1 viruses isolated from humans can bind to both human and avian receptors, in contrast to those isolated from chickens and ducks, which recognize the avian receptors exclusively. Mutations at positions 182 and 192 independently convert the HAs of H5N1 viruses known to recognize the avian receptor to ones that recognize the human receptor. Analysis of the crystal structure of the HA from an H5N1 virus used in our genetic experiments shows that the locations of these amino acids in the HA molecule are compatible with an effect on receptor binding. The amino acid changes that we identify might serve as molecular markers for assessing the pandemic potential of H5N1 field isolates.H5N1 influenza A viruses have spread to numerous countries in Asia, Europe and Africa, infecting not only large numbers of poultry, but also an increasing number of humans, often with lethal effects. Human and avian influenza A viruses differ in their recognition of host cell receptors: the former preferentially recognize receptors with saccharides terminating in sialic acid-alpha2,6-galactose (SAalpha2,6Gal), whereas the latter prefer those ending in SAalpha2,3Gal (refs 3-6). A conversion from SAalpha2,3Gal to SAalpha2,6Gal recognition is thought to be one of the changes that must occur before avian influenza viruses can replicate efficiently in humans and acquire the potential to cause a pandemic. By identifying mutations in the receptor-binding haemagglutinin (HA) molecule that would enable avian H5N1 viruses to recognize human-type host cell receptors, it may be possible to predict (and thus to increase preparedness for) the emergence of pandemic viruses. Here we show that some H5N1 viruses isolated from humans can bind to both human and avian receptors, in contrast to those isolated from chickens and ducks, which recognize the avian receptors exclusively. Mutations at positions 182 and 192 independently convert the HAs of H5N1 viruses known to recognize the avian receptor to ones that recognize the human receptor. Analysis of the crystal structure of the HA from an H5N1 virus used in our genetic experiments shows that the locations of these amino acids in the HA molecule are compatible with an effect on receptor binding. The amino acid changes that we identify might serve as molecular markers for assessing the pandemic potential of H5N1 field isolates. H5N1 influenza A viruses have spread to numerous countries in Asia, Europe and Africa, infecting not only large numbers of poultry, but also an increasing number of humans, often with lethal effects. Human and avian influenza A viruses differ in their recognition of host cell receptors: the former preferentially recognize receptors with saccharides terminating in sialic acid- alpha 2,6-galactose (SA alpha 2,6Gal), whereas the latter prefer those ending in SA alpha 2,3Gal (refs 3-6). A conversion from SA alpha 2,3Gal to SA alpha 2,6Gal recognition is thought to be one of the changes that must occur before avian influenza viruses can replicate efficiently in humans and acquire the potential to cause a pandemic. By identifying mutations in the receptor-binding haemagglutinin (HA) molecule that would enable avian H5N1 viruses to recognize human-type host cell receptors, it may be possible to predict (and thus to increase preparedness for) the emergence of pandemic viruses. Here we show that some H5N1 viruses isolated from humans can bind to both human and avian receptors, in contrast to those isolated from chickens and ducks, which recognize the avian receptors exclusively. Mutations at positions 182 and 192 independently convert the HAs of H5N1 viruses known to recognize the avian receptor to ones that recognize the human receptor. Analysis of the crystal structure of the HA from an H5N1 virus used in our genetic experiments shows that the locations of these amino acids in the HA molecule are compatible with an effect on receptor binding. The amino acid changes that we identify might serve as molecular markers for assessing the pandemic potential of H5N1 field isolates. H5N1 influenza A viruses have spread to numerous countries in Asia, Europe and Africa, infecting not only large numbers of poultry, but also an increasing number of humans, often with lethal effects. Human and avian influenza A viruses differ in their recognition of host cell receptors: the former preferentially recognize receptors with saccharides terminating in sialic acid-alpha2,6-galactose (SAalpha2,6Gal), whereas the latter prefer those ending in SAalpha2,3Gal. A conversion from SAalpha2,3Gal to SAalpha2,6Gal recognition is thought to be one of the changes that must occur before avian influenza viruses can replicate efficiently in humans and acquire the potential to cause a pandemic. By identifying mutations in the receptor-binding haemagglutinin (HA) molecule that would enable avian H5N1 viruses to recognize human-type host cell receptors, it may be possible to predict (and thus to increase preparedness for) the emergence of pandemic viruses. Here we show that some H5N1 viruses isolated from humans can bind to both human and avian receptors, in contrast to those isolated from chickens and ducks, which recognize the avian receptors exclusively. Mutations at positions 182 and 192 independently convert the HAs of H5N1 viruses known to recognize the avian receptor to ones that recognize the human receptor. Analysis of the crystal structure of the HA from an H5N1 virus used in our genetic experiments shows that the locations of these amino acids in the HA molecule are compatible with an effect on receptor binding. The amino acid changes that we identify might serve as molecular markers for assessing the pandemic potential of H5N1 field isolates. [PUBLICATION ABSTRACT] |
| Audience | Academic |
| Author | Le, Mai Q. Nidom, Chairul A. Suzuki, Yasuo Suzuki, Takashi Lin, Yipu Muramoto, Yukiko Murata, Takeomi Gamblin, Steven J. Kiso, Maki Kiso, Makoto Kawaoka, Yoshihiro Sakai-Tagawa, Yuko Hay, Alan Skehel, John J. Usui, Taiichi Haire, Lesley F. Stevens, David J. Russell, Rupert J. Ito, Mutsumi Sawada, Toshihiko Shinya, Kyoko Yamada, Shinya Horimoto, Taisuke |
| Author_xml | – sequence: 1 givenname: Shinya surname: Yamada fullname: Yamada, Shinya organization: Division of Virology, Department of Microbiology and Immunology, Core Research for Evolutional Science and Technology, Japan Science and Technology Agency – sequence: 2 givenname: Yasuo surname: Suzuki fullname: Suzuki, Yasuo organization: Core Research for Evolutional Science and Technology, Japan Science and Technology Agency, College of Life and Health Sciences, Chubu University – sequence: 3 givenname: Takashi surname: Suzuki fullname: Suzuki, Takashi organization: Core Research for Evolutional Science and Technology, Japan Science and Technology Agency, Department of Biochemistry, University of Shizuoka, School of Pharmaceutical Sciences and COE Program in the 21st Century – sequence: 4 givenname: Mai Q. surname: Le fullname: Le, Mai Q. organization: National Institute of Hygiene and Epidemiology – sequence: 5 givenname: Chairul A. surname: Nidom fullname: Nidom, Chairul A. organization: Avian Influenza Laboratory, Tropical Disease Centre, Airlangga University – sequence: 6 givenname: Yuko surname: Sakai-Tagawa fullname: Sakai-Tagawa, Yuko organization: Division of Virology, Department of Microbiology and Immunology, Core Research for Evolutional Science and Technology, Japan Science and Technology Agency – sequence: 7 givenname: Yukiko surname: Muramoto fullname: Muramoto, Yukiko organization: Division of Virology, Department of Microbiology and Immunology, Core Research for Evolutional Science and Technology, Japan Science and Technology Agency – sequence: 8 givenname: Mutsumi surname: Ito fullname: Ito, Mutsumi organization: Division of Virology, Department of Microbiology and Immunology, Core Research for Evolutional Science and Technology, Japan Science and Technology Agency – sequence: 9 givenname: Maki surname: Kiso fullname: Kiso, Maki organization: Division of Virology, Department of Microbiology and Immunology, Core Research for Evolutional Science and Technology, Japan Science and Technology Agency – sequence: 10 givenname: Taisuke surname: Horimoto fullname: Horimoto, Taisuke organization: Division of Virology, Department of Microbiology and Immunology, Core Research for Evolutional Science and Technology, Japan Science and Technology Agency – sequence: 11 givenname: Kyoko surname: Shinya fullname: Shinya, Kyoko organization: The Avian Zoonosis Research Centre, Tottori University – sequence: 12 givenname: Toshihiko surname: Sawada fullname: Sawada, Toshihiko organization: Department of Applied Bioorganic Chemistry, The United Graduate School of Agricultural Science, Gifu University – sequence: 13 givenname: Makoto surname: Kiso fullname: Kiso, Makoto organization: Department of Applied Bioorganic Chemistry, The United Graduate School of Agricultural Science, Gifu University – sequence: 14 givenname: Taiichi surname: Usui fullname: Usui, Taiichi organization: Department of Applied Biological Chemistry, Shizuoka University – sequence: 15 givenname: Takeomi surname: Murata fullname: Murata, Takeomi organization: Department of Applied Biological Chemistry, Shizuoka University – sequence: 16 givenname: Yipu surname: Lin fullname: Lin, Yipu organization: MRC National Institute for Medical Research – sequence: 17 givenname: Alan surname: Hay fullname: Hay, Alan organization: MRC National Institute for Medical Research – sequence: 18 givenname: Lesley F. surname: Haire fullname: Haire, Lesley F. organization: MRC National Institute for Medical Research – sequence: 19 givenname: David J. surname: Stevens fullname: Stevens, David J. organization: MRC National Institute for Medical Research – sequence: 20 givenname: Rupert J. surname: Russell fullname: Russell, Rupert J. organization: MRC National Institute for Medical Research, Centre for Biomolecular Sciences, University of St Andrews – sequence: 21 givenname: Steven J. surname: Gamblin fullname: Gamblin, Steven J. organization: MRC National Institute for Medical Research – sequence: 22 givenname: John J. surname: Skehel fullname: Skehel, John J. organization: MRC National Institute for Medical Research – sequence: 23 givenname: Yoshihiro surname: Kawaoka fullname: Kawaoka, Yoshihiro email: kawaoka@ims.u-tokyo.ac.jp organization: Division of Virology, Department of Microbiology and Immunology, International Research Centre for Infectious Diseases, Institute of Medical Science, University of Tokyo, Core Research for Evolutional Science and Technology, Japan Science and Technology Agency, Department of Pathobiological Sciences, University of Wisconsin-Madison |
| BackLink | http://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=18270909$$DView record in Pascal Francis https://www.ncbi.nlm.nih.gov/pubmed/17108965$$D View this record in MEDLINE/PubMed |
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| Cites_doi | 10.1006/viro.1997.8526 10.1038/4371108a 10.1073/pnas.201401198 10.1126/science.311.5763.932a 10.1128/JVI.74.18.8502-8512.2000 10.1016/0042-6822(83)90507-X 10.1093/glycob/cwg032 10.1126/science.1124513 10.1126/science.1122818 10.1006/viro.1994.1100 10.3201/eid1201.051024 10.1016/j.virol.2003.11.030 10.1107/S0907444998003254 10.1016/0042-6822(83)90150-2 10.1002/rmv.319 10.1006/viro.1994.1615 10.1128/JVI.67.4.1761-1764.1993 10.1073/pnas.96.16.9345 10.1128/JCM.30.3.655-662.1992 10.1128/JVI.79.15.9926-9932.2005 10.1093/emboj/21.5.865 10.1006/viro.1995.1405 10.1038/440435a 10.1107/S0108767390010224 |
| ContentType | Journal Article |
| Copyright | Springer Nature Limited 2006 2007 INIST-CNRS COPYRIGHT 2006 Nature Publishing Group Copyright Nature Publishing Group Nov 16, 2006 |
| Copyright_xml | – notice: Springer Nature Limited 2006 – notice: 2007 INIST-CNRS – notice: COPYRIGHT 2006 Nature Publishing Group – notice: Copyright Nature Publishing Group Nov 16, 2006 |
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| Keywords | Human Hemagglutinin Host specificity Orthomyxoviridae Binding site Molecular marker Infection Virus Avian influenza Influenzavirus A(H5N1) Vertebrata Biological fixation Influenzavirus A Avian influenzavirus Viral disease Replication Chicken Mutation Aves Aminoacid sequence Biological receptor |
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| References | K Shinya (BFnature05264_CR21) 2005; 79 G Neumann (BFnature05264_CR8) 1999; 96 RG Webster (BFnature05264_CR1) 2006; 12 K Shinya (BFnature05264_CR20) 2004; 320 CT Hardy (BFnature05264_CR12) 1995; 211 GN Rogers (BFnature05264_CR4) 1983; 127 LV Gubareva (BFnature05264_CR13) 1994; 199 T Kuiken (BFnature05264_CR16) 2006; 312 Z Otwinowski (BFnature05264_CR24) 1993 Y Ha (BFnature05264_CR9) 2001; 98 AT Brunger (BFnature05264_CR26) 1998; 54 EK Subbarao (BFnature05264_CR19) 1993; 67 M Matrosovich (BFnature05264_CR3) 2000; 74 TA Jones (BFnature05264_CR14) 1991; 47 ML Clements (BFnature05264_CR18) 1992; 30 QM Le (BFnature05264_CR7) 2005; 437 MC Zambon (BFnature05264_CR6) 2001; 11 Y Ha (BFnature05264_CR23) 2002; 21 GN Rogers (BFnature05264_CR5) 1983; 131 J Stevens (BFnature05264_CR10) 2006; 312 K Totani (BFnature05264_CR22) 2003; 13 K Shinya (BFnature05264_CR15) 2006; 440 M Enserink (BFnature05264_CR2) 2006; 311 BFnature05264_CR25 MB Eisen (BFnature05264_CR11) 1997; 232 RJ Connor (BFnature05264_CR17) 1994; 205 |
| References_xml | – volume: 232 start-page: 19 year: 1997 ident: BFnature05264_CR11 publication-title: Virology doi: 10.1006/viro.1997.8526 – volume: 437 start-page: 1108 year: 2005 ident: BFnature05264_CR7 publication-title: Nature doi: 10.1038/4371108a – volume: 98 start-page: 11181 year: 2001 ident: BFnature05264_CR9 publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.201401198 – volume: 311 start-page: 932 year: 2006 ident: BFnature05264_CR2 publication-title: Science doi: 10.1126/science.311.5763.932a – volume: 74 start-page: 8502 year: 2000 ident: BFnature05264_CR3 publication-title: J. Virol. doi: 10.1128/JVI.74.18.8502-8512.2000 – volume: 131 start-page: 394 year: 1983 ident: BFnature05264_CR5 publication-title: Virology doi: 10.1016/0042-6822(83)90507-X – volume: 13 start-page: 315 year: 2003 ident: BFnature05264_CR22 publication-title: Glycobiology doi: 10.1093/glycob/cwg032 – volume: 312 start-page: 404 year: 2006 ident: BFnature05264_CR10 publication-title: Science doi: 10.1126/science.1124513 – volume: 312 start-page: 394 year: 2006 ident: BFnature05264_CR16 publication-title: Science doi: 10.1126/science.1122818 – volume: 199 start-page: 89 year: 1994 ident: BFnature05264_CR13 publication-title: Virology doi: 10.1006/viro.1994.1100 – volume: 12 start-page: 3 year: 2006 ident: BFnature05264_CR1 publication-title: Emerg. Infect. Dis. doi: 10.3201/eid1201.051024 – volume: 320 start-page: 258 year: 2004 ident: BFnature05264_CR20 publication-title: Virology doi: 10.1016/j.virol.2003.11.030 – volume: 54 start-page: 905 year: 1998 ident: BFnature05264_CR26 publication-title: Acta Crystallogr. D doi: 10.1107/S0907444998003254 – volume: 127 start-page: 361 year: 1983 ident: BFnature05264_CR4 publication-title: Virology doi: 10.1016/0042-6822(83)90150-2 – volume: 11 start-page: 227 year: 2001 ident: BFnature05264_CR6 publication-title: Rev. Med. Virol. doi: 10.1002/rmv.319 – volume: 205 start-page: 17 year: 1994 ident: BFnature05264_CR17 publication-title: Virology doi: 10.1006/viro.1994.1615 – start-page: 556 volume-title: Data Collection and Processing year: 1993 ident: BFnature05264_CR24 – volume: 67 start-page: 1761 year: 1993 ident: BFnature05264_CR19 publication-title: J. Virol. doi: 10.1128/JVI.67.4.1761-1764.1993 – volume: 96 start-page: 9345 year: 1999 ident: BFnature05264_CR8 publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.96.16.9345 – volume: 30 start-page: 655 year: 1992 ident: BFnature05264_CR18 publication-title: J. Clin. Microbiol. doi: 10.1128/JCM.30.3.655-662.1992 – volume: 79 start-page: 9926 year: 2005 ident: BFnature05264_CR21 publication-title: J. Virol. doi: 10.1128/JVI.79.15.9926-9932.2005 – volume: 21 start-page: 865 year: 2002 ident: BFnature05264_CR23 publication-title: EMBO J. doi: 10.1093/emboj/21.5.865 – volume: 211 start-page: 302 year: 1995 ident: BFnature05264_CR12 publication-title: Virology doi: 10.1006/viro.1995.1405 – volume: 440 start-page: 435 year: 2006 ident: BFnature05264_CR15 publication-title: Nature doi: 10.1038/440435a – volume: 47 start-page: 110 year: 1991 ident: BFnature05264_CR14 publication-title: Acta Crystallogr. A doi: 10.1107/S0108767390010224 – ident: BFnature05264_CR25 |
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| Snippet | Pandemic potential
The fact that the H5N1 bird flu virus circulating in Asia, Europe and Africa is unable to attach to human-type cell receptors has helped to... H5N1 influenza A viruses have spread to numerous countries in Asia, Europe and Africa, infecting not only large numbers of poultry, but also an increasing... |
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| SubjectTerms | Amino acids Animal viral diseases Animals Aquatic birds Avian flu Binding sites Biological and medical sciences Cell Line Cellular biology Chickens Crystal structure Crystallography, X-Ray Dogs Fundamental and applied biological sciences. Psychology Genetics Hemagglutinin Glycoproteins, Influenza Virus - chemistry Hemagglutinin Glycoproteins, Influenza Virus - genetics Hemagglutinin Glycoproteins, Influenza Virus - metabolism Human viral diseases Humanities and Social Sciences Humans Infectious diseases Influenza A Virus, H5N1 Subtype - chemistry Influenza A Virus, H5N1 Subtype - genetics Influenza A Virus, H5N1 Subtype - metabolism Lethal effects letter Medical sciences Microbiology multidisciplinary Mutation Mutation - genetics Pandemics Poultry Receptors, Virus - chemistry Receptors, Virus - metabolism Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains Saccharides Science Science (multidisciplinary) Viral diseases Viral diseases of the respiratory system and ent viral diseases Virology |
| Title | Haemagglutinin mutations responsible for the binding of H5N1 influenza A viruses to human-type receptors |
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