Detection of respiratory syncytial virus fusion protein variants between 2009 and 2012 in China
Respiratory syncytial virus (RSV) causes respiratory tract infection, particularly acute lower respiratory tract infection (ALRTI), in early childhood. The RSV fusion protein (F protein) is an important surface protein, and it is the target of both cytotoxic T lymphocytes (CTL) and neutralizing anti...
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| Veröffentlicht in: | Archives of virology 2014-05, Vol.159 (5), p.1089-1098 |
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| creator | Xia, Qiuling Zhou, Lili Peng, Caijing Hao, Rui Ni, Ke Zang, Na Ren, Luo Deng, Yu Xie, Xiaohong He, Linli Tian, Daiyin Wang, Lijia Huang, Ailong Zhao, Yao Zhao, Xiaodong Fu, Zhou Tu, Wenwei Liu, Enmei |
| description | Respiratory syncytial virus (RSV) causes respiratory tract infection, particularly acute lower respiratory tract infection (ALRTI), in early childhood. The RSV fusion protein (F protein) is an important surface protein, and it is the target of both cytotoxic T lymphocytes (CTL) and neutralizing antibodies; thus, it may be useful as a candidate for vaccine research. This study investigated the genetic diversity of the RSV F protein. To this end, a total of 1800 nasopharyngeal aspirates from hospitalized children with ALRTI were collected for virus isolation between June 2009 and March 2012. There were 333 RSV-positive cases (277 cases of RSV A, 55 of RSV B, and 1 with both RSV A and RSV B), accounting for 18.5 % of the total cases. Next, 130 clinical strains (107 of RSV A, 23 of RSV B) were selected for F gene sequencing. Phylogenetic analysis revealed that the F gene sequence is highly conserved, with significant amino acid changes at residues 16, 25, 45, 102, 122, 124, 209, and 447. Mutations in human histocompatibility leukocyte antigen (HLA)-restricted CTL epitopes were also observed. Variations in RSV A F protein at the palivizumab binding site 276 (N→S) increased between 2009 and 2012 and became predominant. Western blot analysis and microneutralization data showed a substitution at residue 276 (N→S) in RSV A that did not cause resistance to palivizumab. In conclusion, the RSV F gene is geographically and temporally conserved, but limited genetic variations were still observed. These data could be helpful for the development of vaccines against RSV infection. |
| doi_str_mv | 10.1007/s00705-013-1870-9 |
| format | Article |
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The RSV fusion protein (F protein) is an important surface protein, and it is the target of both cytotoxic T lymphocytes (CTL) and neutralizing antibodies; thus, it may be useful as a candidate for vaccine research. This study investigated the genetic diversity of the RSV F protein. To this end, a total of 1800 nasopharyngeal aspirates from hospitalized children with ALRTI were collected for virus isolation between June 2009 and March 2012. There were 333 RSV-positive cases (277 cases of RSV A, 55 of RSV B, and 1 with both RSV A and RSV B), accounting for 18.5 % of the total cases. Next, 130 clinical strains (107 of RSV A, 23 of RSV B) were selected for F gene sequencing. Phylogenetic analysis revealed that the F gene sequence is highly conserved, with significant amino acid changes at residues 16, 25, 45, 102, 122, 124, 209, and 447. Mutations in human histocompatibility leukocyte antigen (HLA)-restricted CTL epitopes were also observed. Variations in RSV A F protein at the palivizumab binding site 276 (N→S) increased between 2009 and 2012 and became predominant. Western blot analysis and microneutralization data showed a substitution at residue 276 (N→S) in RSV A that did not cause resistance to palivizumab. In conclusion, the RSV F gene is geographically and temporally conserved, but limited genetic variations were still observed. These data could be helpful for the development of vaccines against RSV infection.</description><identifier>ISSN: 0304-8608</identifier><identifier>EISSN: 1432-8798</identifier><identifier>DOI: 10.1007/s00705-013-1870-9</identifier><identifier>PMID: 24297488</identifier><language>eng</language><publisher>Vienna: Springer-Verlag</publisher><subject>Amino Acid Sequence ; Antibodies ; Antigens ; binding sites ; Biomedical and Life Sciences ; Biomedicine ; Child ; Child development ; Child, Preschool ; childhood ; children ; China - epidemiology ; cytotoxic T-lymphocytes ; Cytotoxicity ; Epitopes ; Female ; Gene Expression Regulation, Viral ; genes ; Genetic diversity ; genetic variation ; Hospitals ; Humans ; Infant ; Infections ; Infectious Diseases ; Laboratories ; Leukocytes ; Male ; Medical Microbiology ; Medicine ; Molecular Sequence Data ; Mutation ; neutralizing antibodies ; nucleotide sequences ; Original Article ; Phylogeny ; Proteins ; Respiratory syncytial virus ; Respiratory Syncytial Virus Infections - epidemiology ; Respiratory Syncytial Virus Infections - virology ; Respiratory Syncytial Viruses - genetics ; Respiratory Syncytial Viruses - metabolism ; respiratory system ; surface proteins ; T-Lymphocytes, Cytotoxic ; Vaccines ; Viral Fusion Proteins - genetics ; Viral Fusion Proteins - metabolism ; Virology ; viruses ; Western blotting</subject><ispartof>Archives of virology, 2014-05, Vol.159 (5), p.1089-1098</ispartof><rights>Springer-Verlag Wien 2013</rights><rights>Springer-Verlag Wien 2014</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c495t-d0a63b0edda61a1a308d0df037baa81979fdca9f7235f4029fb03d45dd4630c03</citedby><cites>FETCH-LOGICAL-c495t-d0a63b0edda61a1a308d0df037baa81979fdca9f7235f4029fb03d45dd4630c03</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00705-013-1870-9$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00705-013-1870-9$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27903,27904,41467,42536,51297</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24297488$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Xia, Qiuling</creatorcontrib><creatorcontrib>Zhou, Lili</creatorcontrib><creatorcontrib>Peng, Caijing</creatorcontrib><creatorcontrib>Hao, Rui</creatorcontrib><creatorcontrib>Ni, Ke</creatorcontrib><creatorcontrib>Zang, Na</creatorcontrib><creatorcontrib>Ren, Luo</creatorcontrib><creatorcontrib>Deng, Yu</creatorcontrib><creatorcontrib>Xie, Xiaohong</creatorcontrib><creatorcontrib>He, Linli</creatorcontrib><creatorcontrib>Tian, Daiyin</creatorcontrib><creatorcontrib>Wang, Lijia</creatorcontrib><creatorcontrib>Huang, Ailong</creatorcontrib><creatorcontrib>Zhao, Yao</creatorcontrib><creatorcontrib>Zhao, Xiaodong</creatorcontrib><creatorcontrib>Fu, Zhou</creatorcontrib><creatorcontrib>Tu, Wenwei</creatorcontrib><creatorcontrib>Liu, Enmei</creatorcontrib><title>Detection of respiratory syncytial virus fusion protein variants between 2009 and 2012 in China</title><title>Archives of virology</title><addtitle>Arch Virol</addtitle><addtitle>Arch Virol</addtitle><description>Respiratory syncytial virus (RSV) causes respiratory tract infection, particularly acute lower respiratory tract infection (ALRTI), in early childhood. The RSV fusion protein (F protein) is an important surface protein, and it is the target of both cytotoxic T lymphocytes (CTL) and neutralizing antibodies; thus, it may be useful as a candidate for vaccine research. This study investigated the genetic diversity of the RSV F protein. To this end, a total of 1800 nasopharyngeal aspirates from hospitalized children with ALRTI were collected for virus isolation between June 2009 and March 2012. There were 333 RSV-positive cases (277 cases of RSV A, 55 of RSV B, and 1 with both RSV A and RSV B), accounting for 18.5 % of the total cases. Next, 130 clinical strains (107 of RSV A, 23 of RSV B) were selected for F gene sequencing. Phylogenetic analysis revealed that the F gene sequence is highly conserved, with significant amino acid changes at residues 16, 25, 45, 102, 122, 124, 209, and 447. Mutations in human histocompatibility leukocyte antigen (HLA)-restricted CTL epitopes were also observed. Variations in RSV A F protein at the palivizumab binding site 276 (N→S) increased between 2009 and 2012 and became predominant. Western blot analysis and microneutralization data showed a substitution at residue 276 (N→S) in RSV A that did not cause resistance to palivizumab. In conclusion, the RSV F gene is geographically and temporally conserved, but limited genetic variations were still observed. These data could be helpful for the development of vaccines against RSV infection.</description><subject>Amino Acid Sequence</subject><subject>Antibodies</subject><subject>Antigens</subject><subject>binding sites</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Child</subject><subject>Child development</subject><subject>Child, Preschool</subject><subject>childhood</subject><subject>children</subject><subject>China - epidemiology</subject><subject>cytotoxic T-lymphocytes</subject><subject>Cytotoxicity</subject><subject>Epitopes</subject><subject>Female</subject><subject>Gene Expression Regulation, Viral</subject><subject>genes</subject><subject>Genetic diversity</subject><subject>genetic variation</subject><subject>Hospitals</subject><subject>Humans</subject><subject>Infant</subject><subject>Infections</subject><subject>Infectious Diseases</subject><subject>Laboratories</subject><subject>Leukocytes</subject><subject>Male</subject><subject>Medical Microbiology</subject><subject>Medicine</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><subject>neutralizing antibodies</subject><subject>nucleotide sequences</subject><subject>Original Article</subject><subject>Phylogeny</subject><subject>Proteins</subject><subject>Respiratory syncytial virus</subject><subject>Respiratory Syncytial Virus Infections - epidemiology</subject><subject>Respiratory Syncytial Virus Infections - virology</subject><subject>Respiratory Syncytial Viruses - genetics</subject><subject>Respiratory Syncytial Viruses - metabolism</subject><subject>respiratory system</subject><subject>surface proteins</subject><subject>T-Lymphocytes, Cytotoxic</subject><subject>Vaccines</subject><subject>Viral Fusion Proteins - genetics</subject><subject>Viral Fusion Proteins - metabolism</subject><subject>Virology</subject><subject>viruses</subject><subject>Western blotting</subject><issn>0304-8608</issn><issn>1432-8798</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNqNkUuPFCEURonROG3rD3CjJG7clF5eVbA07TOZxIXOmtwqYGTSTbVAjel_L50ajXFh3ACBcz_gHkKeMnjFAIbXpQ2gOmCiY3qAztwjGyYF7_Rg9H2yAQGy0z3oC_KolBuAtiHUQ3LBJTeD1HpD7Ftf_VTjnOgcaPblGDPWOZ9oOaXpVCPu6W3MS6FhKWfqmOfqY6K3mCOmWujo6w_vE-UAhmJybcE4bcTuW0z4mDwIuC_-yd28JVfv333dfewuP3_4tHtz2U3SqNo5wF6M4J3DniFDAdqBCyCGEVEzM5jgJjRh4EIFCdyEEYSTyjnZC5hAbMnLNbe97_viS7WHWCa_32Py81IsU1xKZnrT_w_KDOOytXVLXvyF3sxLTu0jZwp033qoG8VWaspzKdkHe8zxgPlkGdizKLuKsi3RnkVZ02qe3SUv48G73xW_zDSAr0BpR-na5z-u_kfq87Uo4GzxOsdir740H7Kp14NSSvwEusalQQ</recordid><startdate>20140501</startdate><enddate>20140501</enddate><creator>Xia, Qiuling</creator><creator>Zhou, Lili</creator><creator>Peng, Caijing</creator><creator>Hao, Rui</creator><creator>Ni, Ke</creator><creator>Zang, Na</creator><creator>Ren, Luo</creator><creator>Deng, Yu</creator><creator>Xie, Xiaohong</creator><creator>He, Linli</creator><creator>Tian, Daiyin</creator><creator>Wang, Lijia</creator><creator>Huang, Ailong</creator><creator>Zhao, Yao</creator><creator>Zhao, Xiaodong</creator><creator>Fu, Zhou</creator><creator>Tu, Wenwei</creator><creator>Liu, Enmei</creator><general>Springer-Verlag</general><general>Springer Vienna</general><general>Springer Nature B.V</general><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20140501</creationdate><title>Detection of respiratory syncytial virus fusion protein variants between 2009 and 2012 in China</title><author>Xia, Qiuling ; Zhou, Lili ; Peng, Caijing ; Hao, Rui ; Ni, Ke ; Zang, Na ; Ren, Luo ; Deng, Yu ; Xie, Xiaohong ; He, Linli ; Tian, Daiyin ; Wang, Lijia ; Huang, Ailong ; Zhao, Yao ; Zhao, Xiaodong ; Fu, Zhou ; Tu, Wenwei ; Liu, Enmei</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c495t-d0a63b0edda61a1a308d0df037baa81979fdca9f7235f4029fb03d45dd4630c03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Amino Acid Sequence</topic><topic>Antibodies</topic><topic>Antigens</topic><topic>binding sites</topic><topic>Biomedical and Life Sciences</topic><topic>Biomedicine</topic><topic>Child</topic><topic>Child development</topic><topic>Child, Preschool</topic><topic>childhood</topic><topic>children</topic><topic>China - 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genetics</topic><topic>Viral Fusion Proteins - metabolism</topic><topic>Virology</topic><topic>viruses</topic><topic>Western blotting</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Xia, Qiuling</creatorcontrib><creatorcontrib>Zhou, Lili</creatorcontrib><creatorcontrib>Peng, Caijing</creatorcontrib><creatorcontrib>Hao, Rui</creatorcontrib><creatorcontrib>Ni, Ke</creatorcontrib><creatorcontrib>Zang, Na</creatorcontrib><creatorcontrib>Ren, Luo</creatorcontrib><creatorcontrib>Deng, Yu</creatorcontrib><creatorcontrib>Xie, Xiaohong</creatorcontrib><creatorcontrib>He, Linli</creatorcontrib><creatorcontrib>Tian, Daiyin</creatorcontrib><creatorcontrib>Wang, Lijia</creatorcontrib><creatorcontrib>Huang, Ailong</creatorcontrib><creatorcontrib>Zhao, Yao</creatorcontrib><creatorcontrib>Zhao, Xiaodong</creatorcontrib><creatorcontrib>Fu, Zhou</creatorcontrib><creatorcontrib>Tu, Wenwei</creatorcontrib><creatorcontrib>Liu, Enmei</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Archives of virology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Xia, Qiuling</au><au>Zhou, Lili</au><au>Peng, Caijing</au><au>Hao, Rui</au><au>Ni, Ke</au><au>Zang, Na</au><au>Ren, Luo</au><au>Deng, Yu</au><au>Xie, Xiaohong</au><au>He, Linli</au><au>Tian, Daiyin</au><au>Wang, Lijia</au><au>Huang, Ailong</au><au>Zhao, Yao</au><au>Zhao, Xiaodong</au><au>Fu, Zhou</au><au>Tu, Wenwei</au><au>Liu, Enmei</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Detection of respiratory syncytial virus fusion protein variants between 2009 and 2012 in China</atitle><jtitle>Archives of virology</jtitle><stitle>Arch Virol</stitle><addtitle>Arch Virol</addtitle><date>2014-05-01</date><risdate>2014</risdate><volume>159</volume><issue>5</issue><spage>1089</spage><epage>1098</epage><pages>1089-1098</pages><issn>0304-8608</issn><eissn>1432-8798</eissn><abstract>Respiratory syncytial virus (RSV) causes respiratory tract infection, particularly acute lower respiratory tract infection (ALRTI), in early childhood. The RSV fusion protein (F protein) is an important surface protein, and it is the target of both cytotoxic T lymphocytes (CTL) and neutralizing antibodies; thus, it may be useful as a candidate for vaccine research. This study investigated the genetic diversity of the RSV F protein. To this end, a total of 1800 nasopharyngeal aspirates from hospitalized children with ALRTI were collected for virus isolation between June 2009 and March 2012. There were 333 RSV-positive cases (277 cases of RSV A, 55 of RSV B, and 1 with both RSV A and RSV B), accounting for 18.5 % of the total cases. Next, 130 clinical strains (107 of RSV A, 23 of RSV B) were selected for F gene sequencing. Phylogenetic analysis revealed that the F gene sequence is highly conserved, with significant amino acid changes at residues 16, 25, 45, 102, 122, 124, 209, and 447. Mutations in human histocompatibility leukocyte antigen (HLA)-restricted CTL epitopes were also observed. Variations in RSV A F protein at the palivizumab binding site 276 (N→S) increased between 2009 and 2012 and became predominant. Western blot analysis and microneutralization data showed a substitution at residue 276 (N→S) in RSV A that did not cause resistance to palivizumab. In conclusion, the RSV F gene is geographically and temporally conserved, but limited genetic variations were still observed. These data could be helpful for the development of vaccines against RSV infection.</abstract><cop>Vienna</cop><pub>Springer-Verlag</pub><pmid>24297488</pmid><doi>10.1007/s00705-013-1870-9</doi><tpages>10</tpages></addata></record> |
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| subjects | Amino Acid Sequence Antibodies Antigens binding sites Biomedical and Life Sciences Biomedicine Child Child development Child, Preschool childhood children China - epidemiology cytotoxic T-lymphocytes Cytotoxicity Epitopes Female Gene Expression Regulation, Viral genes Genetic diversity genetic variation Hospitals Humans Infant Infections Infectious Diseases Laboratories Leukocytes Male Medical Microbiology Medicine Molecular Sequence Data Mutation neutralizing antibodies nucleotide sequences Original Article Phylogeny Proteins Respiratory syncytial virus Respiratory Syncytial Virus Infections - epidemiology Respiratory Syncytial Virus Infections - virology Respiratory Syncytial Viruses - genetics Respiratory Syncytial Viruses - metabolism respiratory system surface proteins T-Lymphocytes, Cytotoxic Vaccines Viral Fusion Proteins - genetics Viral Fusion Proteins - metabolism Virology viruses Western blotting |
| title | Detection of respiratory syncytial virus fusion protein variants between 2009 and 2012 in China |
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