Mutations of two transmembrane cysteines of hemagglutinin (HA) from influenza A H3N2 virus affect HA thermal stability and fusion activity
Identifieur interne : 000D53 ( Istex/Curation ); précédent : 000D52; suivant : 000D54Mutations of two transmembrane cysteines of hemagglutinin (HA) from influenza A H3N2 virus affect HA thermal stability and fusion activity
Auteurs : Shun Xu [République populaire de Chine] ; Jianqiang Zhou [République populaire de Chine] ; Kang Liu [République populaire de Chine] ; Qiliang Liu [République populaire de Chine] ; Chunyi Xue [République populaire de Chine] ; Xiaoming Li [République populaire de Chine] ; Jing Zheng [République populaire de Chine] ; Dongyu Luo [République populaire de Chine] ; Yongchang Cao [République populaire de Chine]Source :
- Virus Genes [ 0920-8569 ] ; 2013-08-01.
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Abstract
Abstract: Influenza A H3N2 virus caused 1968 Hong Kong influenza pandemic, and has since been one of the most prevalent seasonal influenza viruses in global populations, representing a credible pandemic candidate in future. Previous studies have established that the hemagglutinin (HA) protein is the predominant antigen and executes receptor binding and membrane fusion. Homologous sequence analysis of all HA subtypes of influenza viruses revealed that two cysteine residues (540 and 544) are uniquely present in the transmembrane domain (TM) of HA proteins from all influenza A H3N2 viruses. However, the functions of these two cysteines have not been fully studied. Here, we generated three mutants (C540S, C544L, and 2C/SL) to investigate the effects of the two TM cysteines on the biological functions of H3 HA. We herein presented evidences that the mutations of one or two of the cysteines did not affect the proper expressions of HA proteins in cells, and more importantly all mutant H3 HAs showed decreased thermal stability but increased fusion activity in comparison with wildtype HA. Our results taken together demonstrated that the two TM cysteines are important for the biological functions of H3 HA proteins.
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DOI: 10.1007/s11262-013-0924-0
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Guangzhou</wicri:regionArea></affiliation></author><author><name sortKey="Liu, Kang" sort="Liu, Kang" uniqKey="Liu K" first="Kang" last="Liu">Kang Liu</name><affiliation wicri:level="1"><mods:affiliation>State Key Laboratory of Biocontrol, Life Sciences School, Sun Yat-sen University, 510006, Guangzhou, People’s Republic of China</mods:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>State Key Laboratory of Biocontrol, Life Sciences School, Sun Yat-sen University, 510006, Guangzhou</wicri:regionArea></affiliation></author><author><name sortKey="Liu, Qiliang" sort="Liu, Qiliang" uniqKey="Liu Q" first="Qiliang" last="Liu">Qiliang Liu</name><affiliation wicri:level="1"><mods:affiliation>State Key Laboratory of Biocontrol, Life Sciences School, Sun Yat-sen University, 510006, Guangzhou, People’s Republic of China</mods:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>State Key Laboratory of Biocontrol, 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Chine</country></affiliation></author></analytic><monogr></monogr><series><title level="j">Virus Genes</title><title level="j" type="abbrev">Virus Genes</title><idno type="ISSN">0920-8569</idno><idno type="eISSN">1572-994X</idno><imprint><publisher>Springer US; http://www.springer-ny.com</publisher><pubPlace>Boston</pubPlace><date type="published" when="2013-08-01">2013-08-01</date><biblScope unit="volume">47</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="20">20</biblScope><biblScope unit="page" to="26">26</biblScope></imprint><idno type="ISSN">0920-8569</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0920-8569</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cysteine</term><term>Fusion activity</term><term>H3N2</term><term>Influenza virus</term><term>Thermal stability</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Influenza A H3N2 virus caused 1968 Hong Kong influenza pandemic, and has since been one of the most prevalent seasonal influenza viruses in global populations, representing a credible pandemic candidate in future. Previous studies have established that the hemagglutinin (HA) protein is the predominant antigen and executes receptor binding and membrane fusion. Homologous sequence analysis of all HA subtypes of influenza viruses revealed that two cysteine residues (540 and 544) are uniquely present in the transmembrane domain (TM) of HA proteins from all influenza A H3N2 viruses. However, the functions of these two cysteines have not been fully studied. Here, we generated three mutants (C540S, C544L, and 2C/SL) to investigate the effects of the two TM cysteines on the biological functions of H3 HA. We herein presented evidences that the mutations of one or two of the cysteines did not affect the proper expressions of HA proteins in cells, and more importantly all mutant H3 HAs showed decreased thermal stability but increased fusion activity in comparison with wildtype HA. Our results taken together demonstrated that the two TM cysteines are important for the biological functions of H3 HA proteins.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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