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Article: The K526R substitution in viral protein ​PB2 enhances the effects of E627K on influenza virus replication

TitleThe K526R substitution in viral protein ​PB2 enhances the effects of E627K on influenza virus replication
Authors
KeywordsBiological sciences
Microbiology
Virology
Issue Date2014
PublisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/ncomms/index.html
Citation
Nature Communications, 2014, v. 5, article no. 5509 How to Cite?
AbstractHost-adaptive strategies, such as the E627K substitution in the ​PB2 protein, are critical for replication of avian influenza A viruses in mammalian hosts. Here we show that mutation ​PB2-K526R is present in some human H7N9 influenza isolates, in nearly 80% of H5N1 human isolates from Indonesia and, in conjunction with E627K, in almost all seasonal H3N2 viruses since 1970. Polymerase complexes containing ​PB2-526R derived from H7N9, H5N1 or H3N2 viruses exhibit increased polymerase activity. ​PB2-526R also enhances viral transcription and replication in cells. In comparison with viruses carrying 627K, H7N9 viruses carrying both 526R and 627K replicate more efficiently in mammalian (but not avian) cells and in mouse lung tissues, and cause greater body weight loss and mortality in infected mice. ​PB2-K526R interacts with nuclear export protein and our results suggest that it contributes to enhance replication for certain influenza virus subtypes, particularly in combination with 627K.
Persistent Identifierhttp://hdl.handle.net/10722/207685
ISSN
2015 Impact Factor: 11.329
2015 SCImago Journal Rankings: 6.539
PubMed Central ID

 

DC FieldValueLanguage
dc.contributor.authorSong, W-
dc.contributor.authorWang, P-
dc.contributor.authorMok, BWY-
dc.contributor.authorLau, SY-
dc.contributor.authorHuang, X-
dc.contributor.authorWu, WL-
dc.contributor.authorZheng, M-
dc.contributor.authorWen, X-
dc.contributor.authorYang, S-
dc.contributor.authorChen, Y-
dc.contributor.authorLi, L-
dc.contributor.authorYuen, KY-
dc.contributor.authorChen, H-
dc.date.accessioned2015-01-16T01:31:18Z-
dc.date.available2015-01-16T01:31:18Z-
dc.date.issued2014-
dc.identifier.citationNature Communications, 2014, v. 5, article no. 5509-
dc.identifier.issn2041-1723-
dc.identifier.urihttp://hdl.handle.net/10722/207685-
dc.description.abstractHost-adaptive strategies, such as the E627K substitution in the ​PB2 protein, are critical for replication of avian influenza A viruses in mammalian hosts. Here we show that mutation ​PB2-K526R is present in some human H7N9 influenza isolates, in nearly 80% of H5N1 human isolates from Indonesia and, in conjunction with E627K, in almost all seasonal H3N2 viruses since 1970. Polymerase complexes containing ​PB2-526R derived from H7N9, H5N1 or H3N2 viruses exhibit increased polymerase activity. ​PB2-526R also enhances viral transcription and replication in cells. In comparison with viruses carrying 627K, H7N9 viruses carrying both 526R and 627K replicate more efficiently in mammalian (but not avian) cells and in mouse lung tissues, and cause greater body weight loss and mortality in infected mice. ​PB2-K526R interacts with nuclear export protein and our results suggest that it contributes to enhance replication for certain influenza virus subtypes, particularly in combination with 627K.-
dc.languageeng-
dc.publisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/ncomms/index.html-
dc.relation.ispartofNature Communications-
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.subjectBiological sciences-
dc.subjectMicrobiology-
dc.subjectVirology-
dc.titleThe K526R substitution in viral protein ​PB2 enhances the effects of E627K on influenza virus replicationen_US
dc.typeArticleen_US
dc.identifier.emailSong, W: wjsong@hkucc.hku.hk-
dc.identifier.emailWang, P: puiwang@hkucc.hku.hk-
dc.identifier.emailMok, BWY: bobomok@HKUCC.hku.hk-
dc.identifier.emailLau, SY: lausiuying@hotmail.com-
dc.identifier.emailYuen, KY: kyyuen@hku.hk-
dc.identifier.emailChen, H: hlchen@hku.hk-
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.1038/ncomms6509-
dc.identifier.pmcid4263149-
dc.identifier.hkuros247898-
dc.identifier.volume5-
dc.publisher.placeUnited Kingdom-

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