Biological and Structural Characterization of a Host-Adapting Amino Acid in Influenza Virus
Two amino acids (lysine at position 627 or asparagine at position 701) in the polymerase subunit PB2 protein are considered critical for the adaptation of avian influenza A viruses to mammals. However, the recently emerged pandemic H1N1 viruses lack these amino acids. Here, we report that a basic am...
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| Published in | PLoS pathogens Vol. 6; no. 8; p. e1001034 |
|---|---|
| Main Authors | , , , , , , , , , , , , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Public Library of Science
01.08.2010
Public Library of Science (PLoS) |
| Subjects | |
| Online Access | Get full text |
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| Abstract | Two amino acids (lysine at position 627 or asparagine at position 701) in the polymerase subunit PB2 protein are considered critical for the adaptation of avian influenza A viruses to mammals. However, the recently emerged pandemic H1N1 viruses lack these amino acids. Here, we report that a basic amino acid at position 591 of PB2 can compensate for the lack of lysine at position 627 and confers efficient viral replication to pandemic H1N1 viruses in mammals. Moreover, a basic amino acid at position 591 of PB2 substantially increased the lethality of an avian H5N1 virus in mice. We also present the X-ray crystallographic structure of the C-terminus of a pandemic H1N1 virus PB2 protein. Arginine at position 591 fills the cleft found in H5N1 PB2 proteins in this area, resulting in differences in surface shape and charge for H1N1 PB2 proteins. These differences may affect the protein's interaction with viral and/or cellular factors, and hence its ability to support virus replication in mammals. |
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| AbstractList | Two amino acids (lysine at position 627 or asparagine at position 701) in the polymerase subunit PB2 protein are considered critical for the adaptation of avian influenza A viruses to mammals. However, the recently emerged pandemic H1N1 viruses lack these amino acids. Here, we report that a basic amino acid at position 591 of PB2 can compensate for the lack of lysine at position 627 and confers efficient viral replication to pandemic H1N1 viruses in mammals. Moreover, a basic amino acid at position 591 of PB2 substantially increased the lethality of an avian H5N1 virus in mice. We also present the X-ray crystallographic structure of the C-terminus of a pandemic H1N1 virus PB2 protein. Arginine at position 591 fills the cleft found in H5N1 PB2 proteins in this area, resulting in differences in surface shape and charge for H1N1 PB2 proteins. These differences may affect the protein's interaction with viral and/or cellular factors, and hence its ability to support virus replication in mammals. Two amino acids (lysine at position 627 or asparagine at position 701) in the polymerase subunit PB2 protein are considered critical for the adaptation of avian influenza A viruses to mammals. However, the recently emerged pandemic H1N1 viruses lack these amino acids. Here, we report that a basic amino acid at position 591 of PB2 can compensate for the lack of lysine at position 627 and confers efficient viral replication to pandemic H1N1 viruses in mammals. Moreover, a basic amino acid at position 591 of PB2 substantially increased the lethality of an avian H5N1 virus in mice. We also present the X-ray crystallographic structure of the C-terminus of a pandemic H1N1 virus PB2 protein. Arginine at position 591 fills the cleft found in H5N1 PB2 proteins in this area, resulting in differences in surface shape and charge for H1N1 PB2 proteins. These differences may affect the protein's interaction with viral and/or cellular factors, and hence its ability to support virus replication in mammals. Influenza viruses that originate from avian species likely have to acquire adapting amino acid changes to replicate efficiently in mammals. Two amino acid changes in the polymerase PB2 protein--a glutamic acid to lysine change at position 627 or an aspartic acid to asparagine change at position 701--are known to allow influenza viruses of avian origin to replicate efficiently in mammals. Interestingly, the pandemic H1N1 viruses (which possess an avian-like PB2 gene) do not encode the 'human-type' amino acids PB2-627K and PB2-701N. Here, we report that a basic amino acid at position 591 of PB2 can compensate for the lack of PB2-627K and allows efficient replication of highly pathogenic H5N1 and pandemic H1N1 viruses in mammalian species. We also present the X-ray crystal structure of the C-terminal portion of a pandemic H1N1 PB2 protein. The basic amino acid at position 591 fills a distinctive cleft found in the PB2 proteins of H5N1 viruses. We also speculate on the biological significance of the altered surface of the H1N1 PB2 protein. Two amino acids (lysine at position 627 or asparagine at position 701) in the polymerase subunit PB2 protein are considered critical for the adaptation of avian influenza A viruses to mammals. However, the recently emerged pandemic H1N1 viruses lack these amino acids. Here, we report that a basic amino acid at position 591 of PB2 can compensate for the lack of lysine at position 627 and confers efficient viral replication to pandemic H1N1 viruses in mammals. Moreover, a basic amino acid at position 591 of PB2 substantially increased the lethality of an avian H5N1 virus in mice. We also present the X-ray crystallographic structure of the C-terminus of a pandemic H1N1 virus PB2 protein. Arginine at position 591 fills the cleft found in H5N1 PB2 proteins in this area, resulting in differences in surface shape and charge for H1N1 PB2 proteins. These differences may affect the protein's interaction with viral and/or cellular factors, and hence its ability to support virus replication in mammals. Influenza viruses that originate from avian species likely have to acquire adapting amino acid changes to replicate efficiently in mammals. Two amino acid changes in the polymerase PB2 protein—a glutamic acid to lysine change at position 627 or an aspartic acid to asparagine change at position 701—are known to allow influenza viruses of avian origin to replicate efficiently in mammals. Interestingly, the pandemic H1N1 viruses (which possess an avian-like PB2 gene) do not encode the ‘human-type’ amino acids PB2-627K and PB2-701N. Here, we report that a basic amino acid at position 591 of PB2 can compensate for the lack of PB2-627K and allows efficient replication of highly pathogenic H5N1 and pandemic H1N1 viruses in mammalian species. We also present the X-ray crystal structure of the C-terminal portion of a pandemic H1N1 PB2 protein. The basic amino acid at position 591 fills a distinctive cleft found in the PB2 proteins of H5N1 viruses. We also speculate on the biological significance of the altered surface of the H1N1 PB2 protein. Two amino acids (lysine at position 627 or asparagine at position 701) in the polymerase subunit PB2 protein are considered critical for the adaptation of avian influenza A viruses to mammals. However, the recently emerged pandemic H1N1 viruses lack these amino acids. Here, we report that a basic amino acid at position 591 of PB2 can compensate for the lack of lysine at position 627 and confers efficient viral replication to pandemic H1N1 viruses in mammals. Moreover, a basic amino acid at position 591 of PB2 substantially increased the lethality of an avian H5N1 virus in mice. We also present the X-ray crystallographic structure of the C-terminus of a pandemic H1N1 virus PB2 protein. Arginine at position 591 fills the cleft found in H5N1 PB2 proteins in this area, resulting in differences in surface shape and charge for H1N1 PB2 proteins. These differences may affect the protein's interaction with viral and/or cellular factors, and hence its ability to support virus replication in mammals.Two amino acids (lysine at position 627 or asparagine at position 701) in the polymerase subunit PB2 protein are considered critical for the adaptation of avian influenza A viruses to mammals. However, the recently emerged pandemic H1N1 viruses lack these amino acids. Here, we report that a basic amino acid at position 591 of PB2 can compensate for the lack of lysine at position 627 and confers efficient viral replication to pandemic H1N1 viruses in mammals. Moreover, a basic amino acid at position 591 of PB2 substantially increased the lethality of an avian H5N1 virus in mice. We also present the X-ray crystallographic structure of the C-terminus of a pandemic H1N1 virus PB2 protein. Arginine at position 591 fills the cleft found in H5N1 PB2 proteins in this area, resulting in differences in surface shape and charge for H1N1 PB2 proteins. These differences may affect the protein's interaction with viral and/or cellular factors, and hence its ability to support virus replication in mammals. Two amino acids (lysine at position 627 or asparagine at position 701) in the polymerase subunit PB2 protein are considered critical for the adaptation of avian influenza A viruses to mammals. However, the recently emerged pandemic H1N1 viruses lack these amino acids. Here, we report that a basic amino acid at position 591 of PB2 can compensate for the lack of lysine at position 627 and confers efficient viral replication to pandemic H1N1 viruses in mammals. Moreover, a basic amino acid at position 591 of PB2 substantially increased the lethality of an avian H5N1 virus in mice. We also present the X-ray crystallographic structure of the C-terminus of a pandemic H1N1 virus PB2 protein. Arginine at position 591 fills the cleft found in H5N1 PB2 proteins in this area, resulting in differences in surface shape and charge for H1N1 PB2 proteins. These differences may affect the protein's interaction with viral and/or cellular factors, and hence its ability to support virus replication in mammals. |
| Audience | Academic |
| Author | Lank, Simon M. Myler, Peter J. Staker, Bart L. Watanabe, Tokiko Phan, Isabelle Wiseman, Roger W. Raymond, Amy Kim, Jin Hyun Bimber, Benjamin N. Imai, Masaki Shinya, Kyoko Stewart, Lance J. Nidom, Chairul A. Watanabe, Shinji Kawaoka, Yoshihiro Hatta, Masato O'Connor, David H. Sakai-Tagawa, Yuko Sakabe, Saori Neumann, Gabriele Stacy, Robin Smith, Eric Ito, Mutsumi Yamada, Shinya Ozawa, Makoto Li, Chengjun |
| AuthorAffiliation | 9 Departments of Global Health and Medical Education & Biomedical Informatics, University of Washington, Seattle, Washington, United States of America 10 Faculty of Veterinary Medicine, Tropical Disease Centre, Airlangga University, Surabaya, Indonesia 3 Emerald BioStructures, Inc., Bainbridge Island, Washington, United States of America 6 Department of Special Pathogens, International Research Center for Infectious Diseases, Institute of Medical Science, University of Tokyo, Tokyo, Japan 1 Division of Virology, Department of Microbiology and Immunology, Institute of Medical Science, University of Tokyo, Tokyo, Japan 7 ERATO Infection-Induced Host Responses Project, Saitama, Japan 2 Influenza Research Institute, Department of Pathobiological Sciences, School of Veterinary Medicine, University of Wisconsin-Madison, Madison, Wisconsin, United States of America 8 Seattle Biomedical Research Institute, Seattle, Washington, United States of America 11 Collaborating Research Center-Emerging and Reem |
| AuthorAffiliation_xml | – name: 3 Emerald BioStructures, Inc., Bainbridge Island, Washington, United States of America – name: 5 Department of Microbiology and Infectious Diseases, Kobe University, Hyogo, Japan – name: 8 Seattle Biomedical Research Institute, Seattle, Washington, United States of America – name: 13 Department of Pathology and Laboratory Medicine, University of Wisconsin-Madison, Madison, Wisconsin, United States of America – name: 1 Division of Virology, Department of Microbiology and Immunology, Institute of Medical Science, University of Tokyo, Tokyo, Japan – name: 12 Wisconsin National Primate Research Center, University of Wisconsin-Madison, Madison, Wisconsin, United States of America – name: University of Maryland, United States of America – name: 2 Influenza Research Institute, Department of Pathobiological Sciences, School of Veterinary Medicine, University of Wisconsin-Madison, Madison, Wisconsin, United States of America – name: 7 ERATO Infection-Induced Host Responses Project, Saitama, Japan – name: 6 Department of Special Pathogens, International Research Center for Infectious Diseases, Institute of Medical Science, University of Tokyo, Tokyo, Japan – name: 4 Seattle Structural Genomics Center for Infectious Disease, Washington, United States of America – name: 14 Creative Research Initiative, Sousei, Hokkaido University, Sapporo, Japan – name: 10 Faculty of Veterinary Medicine, Tropical Disease Centre, Airlangga University, Surabaya, Indonesia – name: 11 Collaborating Research Center-Emerging and Reemerging Infectious Diseases, Tropical Disease Centre, Airlangga University, Surabaya, Indonesia – name: 9 Departments of Global Health and Medical Education & Biomedical Informatics, University of Washington, Seattle, Washington, United States of America |
| Author_xml | – sequence: 1 givenname: Shinya surname: Yamada fullname: Yamada, Shinya – sequence: 2 givenname: Masato surname: Hatta fullname: Hatta, Masato – sequence: 3 givenname: Bart L. surname: Staker fullname: Staker, Bart L. – sequence: 4 givenname: Shinji surname: Watanabe fullname: Watanabe, Shinji – sequence: 5 givenname: Masaki surname: Imai fullname: Imai, Masaki – sequence: 6 givenname: Kyoko surname: Shinya fullname: Shinya, Kyoko – sequence: 7 givenname: Yuko surname: Sakai-Tagawa fullname: Sakai-Tagawa, Yuko – sequence: 8 givenname: Mutsumi surname: Ito fullname: Ito, Mutsumi – sequence: 9 givenname: Makoto surname: Ozawa fullname: Ozawa, Makoto – sequence: 10 givenname: Tokiko surname: Watanabe fullname: Watanabe, Tokiko – sequence: 11 givenname: Saori surname: Sakabe fullname: Sakabe, Saori – sequence: 12 givenname: Chengjun surname: Li fullname: Li, Chengjun – sequence: 13 givenname: Jin Hyun surname: Kim fullname: Kim, Jin Hyun – sequence: 14 givenname: Peter J. surname: Myler fullname: Myler, Peter J. – sequence: 15 givenname: Isabelle surname: Phan fullname: Phan, Isabelle – sequence: 16 givenname: Amy surname: Raymond fullname: Raymond, Amy – sequence: 17 givenname: Eric surname: Smith fullname: Smith, Eric – sequence: 18 givenname: Robin surname: Stacy fullname: Stacy, Robin – sequence: 19 givenname: Chairul A. surname: Nidom fullname: Nidom, Chairul A. – sequence: 20 givenname: Simon M. surname: Lank fullname: Lank, Simon M. – sequence: 21 givenname: Roger W. surname: Wiseman fullname: Wiseman, Roger W. – sequence: 22 givenname: Benjamin N. surname: Bimber fullname: Bimber, Benjamin N. – sequence: 23 givenname: David H. surname: O'Connor fullname: O'Connor, David H. – sequence: 24 givenname: Gabriele surname: Neumann fullname: Neumann, Gabriele – sequence: 25 givenname: Lance J. surname: Stewart fullname: Stewart, Lance J. – sequence: 26 givenname: Yoshihiro surname: Kawaoka fullname: Kawaoka, Yoshihiro |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/20700447$$D View this record in MEDLINE/PubMed |
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| Copyright | COPYRIGHT 2010 Public Library of Science Yamada et al. 2010 2010 Yamada et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited: Yamada S, Hatta M, Staker BL, Watanabe S, Imai M, et al. (2010) Biological and Structural Characterization of a Host-Adapting Amino Acid in Influenza Virus. PLoS Pathog 6(8): e1001034. doi:10.1371/journal.ppat.1001034 |
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| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 ObjectType-Article-2 ObjectType-Feature-1 Conceived and designed the experiments: M. Hatta, B. Staker, S. Watanabe, T. Watanabe, P. Myler, I. Phan, A. Raymond, E. Smith, R. Stacy, S. Lank, R. Wiseman, B. Bimber, D. O'Connor, L. Stewart, Y. Kawaoka. Performed the experiments: S. Yamada, M. Hatta, B. Staker, M. Imai, K. Shinya, Y. Sakai-Tagawa, M. Ito, M. Ozawa, T. Watanabe, S. Sakabe, C. Li, J. Kim, P. Myler, I. Phan, A. Raymond, E. Smith, R. Stacy, S. Lank, R. Wiseman, B. Bimber, D. O'Connor, L. Stewart. Analyzed the data: B. Staker, P. Myler, I. Phan, A. Raymond, E. Smith, R. Stacy, S. Lank, R. Wiseman, B. Bimber, D. O'Connor, L. Stewart, Y. Kawaoka. Contributed reagents/materials/analysis tools: C. Nidom. Wrote the paper: G. Neumann, Y. Kawaoka. |
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| Snippet | Two amino acids (lysine at position 627 or asparagine at position 701) in the polymerase subunit PB2 protein are considered critical for the adaptation of... Two amino acids (lysine at position 627 or asparagine at position 701) in the polymerase subunit PB2 protein are considered critical for the adaptation of... |
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| SubjectTerms | Amino acids Amino Acids - chemistry Animals Birds Crystallography, X-Ray Genetic aspects Host-virus relationships Humans Influenza A Virus, H1N1 Subtype - genetics Influenza A Virus, H1N1 Subtype - pathogenicity Influenza A Virus, H1N1 Subtype - physiology Influenza virus Influenza viruses Pandemics Physiological aspects Protein Structure, Quaternary Proteins Viral Proteins - chemistry Viral Proteins - genetics Virology Virology/Animal Models of Infection Virology/Mechanisms of Resistance and Susceptibility, including Host Genetics Virology/Viral and Gene Regulation Virology/Virulence Factors and Mechanisms Virulence - genetics Virus Replication |
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| Title | Biological and Structural Characterization of a Host-Adapting Amino Acid in Influenza Virus |
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