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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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Autores principales: Yamada, Shinya, Hatta, Masato, Staker, Bart L., Watanabe, Shinji, Imai, Masaki, Shinya, Kyoko, Sakai-Tagawa, Yuko, Ito, Mutsumi, Ozawa, Makoto, Watanabe, Tokiko, Sakabe, Saori, Li, Chengjun, Kim, Jin Hyun, Myler, Peter J., Phan, Isabelle, Raymond, Amy, Smith, Eric, Stacy, Robin, Nidom, Chairul A., Lank, Simon M., Wiseman, Roger W., Bimber, Benjamin N., O'Connor, David H., Neumann, Gabriele, Stewart, Lance J., Kawaoka, Yoshihiro
Formato: Texto
Lenguaje:English
Publicado: Public Library of Science 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2916879/
https://www.ncbi.nlm.nih.gov/pubmed/20700447
http://dx.doi.org/10.1371/journal.ppat.1001034
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author Yamada, Shinya
Hatta, Masato
Staker, Bart L.
Watanabe, Shinji
Imai, Masaki
Shinya, Kyoko
Sakai-Tagawa, Yuko
Ito, Mutsumi
Ozawa, Makoto
Watanabe, Tokiko
Sakabe, Saori
Li, Chengjun
Kim, Jin Hyun
Myler, Peter J.
Phan, Isabelle
Raymond, Amy
Smith, Eric
Stacy, Robin
Nidom, Chairul A.
Lank, Simon M.
Wiseman, Roger W.
Bimber, Benjamin N.
O'Connor, David H.
Neumann, Gabriele
Stewart, Lance J.
Kawaoka, Yoshihiro
author_facet Yamada, Shinya
Hatta, Masato
Staker, Bart L.
Watanabe, Shinji
Imai, Masaki
Shinya, Kyoko
Sakai-Tagawa, Yuko
Ito, Mutsumi
Ozawa, Makoto
Watanabe, Tokiko
Sakabe, Saori
Li, Chengjun
Kim, Jin Hyun
Myler, Peter J.
Phan, Isabelle
Raymond, Amy
Smith, Eric
Stacy, Robin
Nidom, Chairul A.
Lank, Simon M.
Wiseman, Roger W.
Bimber, Benjamin N.
O'Connor, David H.
Neumann, Gabriele
Stewart, Lance J.
Kawaoka, Yoshihiro
author_sort Yamada, Shinya
collection PubMed
description 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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spelling pubmed-29168792010-08-10 Biological and Structural Characterization of a Host-Adapting Amino Acid in Influenza Virus Yamada, Shinya Hatta, Masato Staker, Bart L. Watanabe, Shinji Imai, Masaki Shinya, Kyoko Sakai-Tagawa, Yuko Ito, Mutsumi Ozawa, Makoto Watanabe, Tokiko Sakabe, Saori Li, Chengjun Kim, Jin Hyun Myler, Peter J. Phan, Isabelle Raymond, Amy Smith, Eric Stacy, Robin Nidom, Chairul A. Lank, Simon M. Wiseman, Roger W. Bimber, Benjamin N. O'Connor, David H. Neumann, Gabriele Stewart, Lance J. Kawaoka, Yoshihiro PLoS Pathog Research Article 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. Public Library of Science 2010-08-05 /pmc/articles/PMC2916879/ /pubmed/20700447 http://dx.doi.org/10.1371/journal.ppat.1001034 Text en Yamada et al. http://creativecommons.org/licenses/by/4.0/ 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 properly credited.
spellingShingle Research Article
Yamada, Shinya
Hatta, Masato
Staker, Bart L.
Watanabe, Shinji
Imai, Masaki
Shinya, Kyoko
Sakai-Tagawa, Yuko
Ito, Mutsumi
Ozawa, Makoto
Watanabe, Tokiko
Sakabe, Saori
Li, Chengjun
Kim, Jin Hyun
Myler, Peter J.
Phan, Isabelle
Raymond, Amy
Smith, Eric
Stacy, Robin
Nidom, Chairul A.
Lank, Simon M.
Wiseman, Roger W.
Bimber, Benjamin N.
O'Connor, David H.
Neumann, Gabriele
Stewart, Lance J.
Kawaoka, Yoshihiro
Biological and Structural Characterization of a Host-Adapting Amino Acid in Influenza Virus
title Biological and Structural Characterization of a Host-Adapting Amino Acid in Influenza Virus
title_full Biological and Structural Characterization of a Host-Adapting Amino Acid in Influenza Virus
title_fullStr Biological and Structural Characterization of a Host-Adapting Amino Acid in Influenza Virus
title_full_unstemmed Biological and Structural Characterization of a Host-Adapting Amino Acid in Influenza Virus
title_short Biological and Structural Characterization of a Host-Adapting Amino Acid in Influenza Virus
title_sort biological and structural characterization of a host-adapting amino acid in influenza virus
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2916879/
https://www.ncbi.nlm.nih.gov/pubmed/20700447
http://dx.doi.org/10.1371/journal.ppat.1001034
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