Mass spectrometry analysis of influenza virus reassortant clones does not reveal an influence of other viral proteins on S-acylation of hemagglutinin
Hemagglutinin (HA) of influenza virus is S-acylated with stearate at a transmembrane cysteine and with palmitate at two cytoplasmic cysteines. The amount of stearate varies from 35 (in avian strains) to 12% (in human strains), although the acylation region exhibits only minor or even no amino acid d...
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| Veröffentlicht in: | Archives of virology 2013-02, Vol.158 (2), p.467-472 |
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| container_title | Archives of virology |
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| creator | Serebryakova, Marina V. Kordyukova, Larisa V. Rudneva, Irina A. Kropotkina, Ekaterina A. Veit, Michael Baratova, Lyudmila A. |
| description | Hemagglutinin (HA) of influenza virus is S-acylated with stearate at a transmembrane cysteine and with palmitate at two cytoplasmic cysteines. The amount of stearate varies from 35 (in avian strains) to 12% (in human strains), although the acylation region exhibits only minor or even no amino acid differences between HAs. To address whether matrix proteins and neuraminidase affect stearoylation of HA, we used mass spectrometry to analyze laboratory reassortants containing avian virus HA and the internal proteins from a human virus. Only minor fluctuations in the amount of stearate were observed, implying that other viral proteins do not affect acylation of HA. |
| doi_str_mv | 10.1007/s00705-012-1510-9 |
| format | Article |
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The amount of stearate varies from 35 (in avian strains) to 12% (in human strains), although the acylation region exhibits only minor or even no amino acid differences between HAs. To address whether matrix proteins and neuraminidase affect stearoylation of HA, we used mass spectrometry to analyze laboratory reassortants containing avian virus HA and the internal proteins from a human virus. Only minor fluctuations in the amount of stearate were observed, implying that other viral proteins do not affect acylation of HA.</description><identifier>ISSN: 0304-8608</identifier><identifier>EISSN: 1432-8798</identifier><identifier>DOI: 10.1007/s00705-012-1510-9</identifier><identifier>PMID: 23065113</identifier><language>eng</language><publisher>Vienna: Springer Vienna</publisher><subject>Acylation ; Amino acids ; Avian flu ; Biomedical and Life Sciences ; Biomedicine ; Brief Report ; Cloning ; Fatty acids ; Glycoproteins ; Hemagglutinin Glycoproteins, Influenza Virus - chemistry ; Hemagglutinin Glycoproteins, Influenza Virus - metabolism ; Humans ; Infectious Diseases ; Influenza virus ; Mass Spectrometry ; Medical Microbiology ; Membranes ; Orthomyxoviridae - chemistry ; Palmitates - analysis ; Protein Processing, Post-Translational ; Proteins ; Reassortant Viruses - chemistry ; Scientific imaging ; Stearates - analysis ; Virology ; Viruses</subject><ispartof>Archives of virology, 2013-02, Vol.158 (2), p.467-472</ispartof><rights>Springer-Verlag Wien 2012</rights><rights>Springer-Verlag Wien 2013</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c405t-e55857a6c8b647f760d2960507273e59784e50e4a8d6e9f66ac841a23a6b20f23</citedby><cites>FETCH-LOGICAL-c405t-e55857a6c8b647f760d2960507273e59784e50e4a8d6e9f66ac841a23a6b20f23</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/s00705-012-1510-9$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00705-012-1510-9$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23065113$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Serebryakova, Marina V.</creatorcontrib><creatorcontrib>Kordyukova, Larisa V.</creatorcontrib><creatorcontrib>Rudneva, Irina A.</creatorcontrib><creatorcontrib>Kropotkina, Ekaterina A.</creatorcontrib><creatorcontrib>Veit, Michael</creatorcontrib><creatorcontrib>Baratova, Lyudmila A.</creatorcontrib><title>Mass spectrometry analysis of influenza virus reassortant clones does not reveal an influence of other viral proteins on S-acylation of hemagglutinin</title><title>Archives of virology</title><addtitle>Arch Virol</addtitle><addtitle>Arch Virol</addtitle><description>Hemagglutinin (HA) of influenza virus is S-acylated with stearate at a transmembrane cysteine and with palmitate at two cytoplasmic cysteines. The amount of stearate varies from 35 (in avian strains) to 12% (in human strains), although the acylation region exhibits only minor or even no amino acid differences between HAs. To address whether matrix proteins and neuraminidase affect stearoylation of HA, we used mass spectrometry to analyze laboratory reassortants containing avian virus HA and the internal proteins from a human virus. Only minor fluctuations in the amount of stearate were observed, implying that other viral proteins do not affect acylation of HA.</description><subject>Acylation</subject><subject>Amino acids</subject><subject>Avian flu</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Brief Report</subject><subject>Cloning</subject><subject>Fatty acids</subject><subject>Glycoproteins</subject><subject>Hemagglutinin Glycoproteins, Influenza Virus - chemistry</subject><subject>Hemagglutinin Glycoproteins, Influenza Virus - metabolism</subject><subject>Humans</subject><subject>Infectious Diseases</subject><subject>Influenza virus</subject><subject>Mass Spectrometry</subject><subject>Medical Microbiology</subject><subject>Membranes</subject><subject>Orthomyxoviridae - chemistry</subject><subject>Palmitates - analysis</subject><subject>Protein Processing, Post-Translational</subject><subject>Proteins</subject><subject>Reassortant Viruses - chemistry</subject><subject>Scientific imaging</subject><subject>Stearates - 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chemistry</topic><topic>Hemagglutinin Glycoproteins, Influenza Virus - metabolism</topic><topic>Humans</topic><topic>Infectious Diseases</topic><topic>Influenza virus</topic><topic>Mass Spectrometry</topic><topic>Medical Microbiology</topic><topic>Membranes</topic><topic>Orthomyxoviridae - chemistry</topic><topic>Palmitates - analysis</topic><topic>Protein Processing, Post-Translational</topic><topic>Proteins</topic><topic>Reassortant Viruses - chemistry</topic><topic>Scientific imaging</topic><topic>Stearates - analysis</topic><topic>Virology</topic><topic>Viruses</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Serebryakova, Marina V.</creatorcontrib><creatorcontrib>Kordyukova, Larisa V.</creatorcontrib><creatorcontrib>Rudneva, Irina A.</creatorcontrib><creatorcontrib>Kropotkina, Ekaterina A.</creatorcontrib><creatorcontrib>Veit, Michael</creatorcontrib><creatorcontrib>Baratova, Lyudmila A.</creatorcontrib><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>Serebryakova, Marina V.</au><au>Kordyukova, Larisa V.</au><au>Rudneva, Irina A.</au><au>Kropotkina, Ekaterina A.</au><au>Veit, Michael</au><au>Baratova, Lyudmila A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Mass spectrometry analysis of influenza virus reassortant clones does not reveal an influence of other viral proteins on S-acylation of hemagglutinin</atitle><jtitle>Archives of virology</jtitle><stitle>Arch Virol</stitle><addtitle>Arch Virol</addtitle><date>2013-02-01</date><risdate>2013</risdate><volume>158</volume><issue>2</issue><spage>467</spage><epage>472</epage><pages>467-472</pages><issn>0304-8608</issn><eissn>1432-8798</eissn><abstract>Hemagglutinin (HA) of influenza virus is S-acylated with stearate at a transmembrane cysteine and with palmitate at two cytoplasmic cysteines. The amount of stearate varies from 35 (in avian strains) to 12% (in human strains), although the acylation region exhibits only minor or even no amino acid differences between HAs. To address whether matrix proteins and neuraminidase affect stearoylation of HA, we used mass spectrometry to analyze laboratory reassortants containing avian virus HA and the internal proteins from a human virus. Only minor fluctuations in the amount of stearate were observed, implying that other viral proteins do not affect acylation of HA.</abstract><cop>Vienna</cop><pub>Springer Vienna</pub><pmid>23065113</pmid><doi>10.1007/s00705-012-1510-9</doi><tpages>6</tpages></addata></record> |
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| ispartof | Archives of virology, 2013-02, Vol.158 (2), p.467-472 |
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| subjects | Acylation Amino acids Avian flu Biomedical and Life Sciences Biomedicine Brief Report Cloning Fatty acids Glycoproteins Hemagglutinin Glycoproteins, Influenza Virus - chemistry Hemagglutinin Glycoproteins, Influenza Virus - metabolism Humans Infectious Diseases Influenza virus Mass Spectrometry Medical Microbiology Membranes Orthomyxoviridae - chemistry Palmitates - analysis Protein Processing, Post-Translational Proteins Reassortant Viruses - chemistry Scientific imaging Stearates - analysis Virology Viruses |
| title | Mass spectrometry analysis of influenza virus reassortant clones does not reveal an influence of other viral proteins on S-acylation of hemagglutinin |
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