Neuraminidase Stalk Length and Additional Glycosylation of the Hemagglutinin Influence the Virulence of Influenza H5N1 Viruses for Mice
Following circulation of avian influenza H5 and H7 viruses in poultry, the hemagglutinin (HA) can acquire additional glycosylation sites, and the neuraminidase (NA) stalk becomes shorter. We investigated whether these features play a role in the pathogenesis of infection in mammalian hosts. From 199...
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| Veröffentlicht in: | Journal of Virology 2009-05, Vol.83 (9), p.4704-4708 |
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| creator | Matsuoka, Yumiko Swayne, David E Thomas, Colleen Rameix-Welti, Marie-Anne Naffakh, Nadia Warnes, Christine Altholtz, Melanie Donis, Ruben Subbarao, Kanta |
| description | Following circulation of avian influenza H5 and H7 viruses in poultry, the hemagglutinin (HA) can acquire additional glycosylation sites, and the neuraminidase (NA) stalk becomes shorter. We investigated whether these features play a role in the pathogenesis of infection in mammalian hosts. From 1996 to 2007, H5N1 viruses with a short NA stalk have become widespread in several avian species. Compared to viruses with a long-stalk NA, viruses with a short-stalk NA showed a decreased capacity to elute from red blood cells and an increased virulence in mice, but not in chickens. The presence of additional HA glycosylation sites had less of an effect on virulence than did NA stalk length. The short-stalk NA of H5N1 viruses circulating in Asia may contribute to virulence in humans. |
| doi_str_mv | 10.1128/jvi.01987-08 |
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We investigated whether these features play a role in the pathogenesis of infection in mammalian hosts. From 1996 to 2007, H5N1 viruses with a short NA stalk have become widespread in several avian species. Compared to viruses with a long-stalk NA, viruses with a short-stalk NA showed a decreased capacity to elute from red blood cells and an increased virulence in mice, but not in chickens. The presence of additional HA glycosylation sites had less of an effect on virulence than did NA stalk length. The short-stalk NA of H5N1 viruses circulating in Asia may contribute to virulence in humans.</description><identifier>ISSN: 1098-5514</identifier><identifier>ISSN: 0022-538X</identifier><identifier>EISSN: 1098-5514</identifier><identifier>DOI: 10.1128/jvi.01987-08</identifier><identifier>PMID: 19225004</identifier><language>eng</language><publisher>Washington, DC: American Society for Microbiology</publisher><subject>Animals ; avian influenza ; Biological and medical sciences ; Chickens ; enzyme activity ; Erythrocytes - metabolism ; Fundamental and applied biological sciences. Psychology ; Glycosylation ; Hemagglutinin Glycoproteins, Influenza Virus - chemistry ; Hemagglutinin Glycoproteins, Influenza Virus - metabolism ; hemagglutinins ; Influenza A virus ; Influenza A Virus, H5N1 Subtype - classification ; Influenza A Virus, H5N1 Subtype - enzymology ; Influenza A Virus, H5N1 Subtype - genetics ; Influenza A Virus, H5N1 Subtype - pathogenicity ; mice ; Mice - virology ; Microbiology ; Miscellaneous ; Mutation - genetics ; Neuraminidase - chemistry ; Neuraminidase - genetics ; Neuraminidase - metabolism ; Orthomyxoviridae Infections ; Pathogenesis and Immunity ; poultry ; poultry diseases ; protein structure ; sialidase ; strains ; Time Factors ; viral diseases of animals and humans ; Virology ; Virulence ; waterfowl ; wild birds</subject><ispartof>Journal of Virology, 2009-05, Vol.83 (9), p.4704-4708</ispartof><rights>2009 INIST-CNRS</rights><rights>Copyright © 2009, American Society for Microbiology</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c528t-1368dc99e0930ba026364196f0d4ccf04e4e656cb242525d759a632235914ff93</citedby><cites>FETCH-LOGICAL-c528t-1368dc99e0930ba026364196f0d4ccf04e4e656cb242525d759a632235914ff93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2668507/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2668507/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,315,728,781,785,886,27929,27930,53796,53798</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=21374923$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19225004$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Matsuoka, Yumiko</creatorcontrib><creatorcontrib>Swayne, David E</creatorcontrib><creatorcontrib>Thomas, Colleen</creatorcontrib><creatorcontrib>Rameix-Welti, Marie-Anne</creatorcontrib><creatorcontrib>Naffakh, Nadia</creatorcontrib><creatorcontrib>Warnes, Christine</creatorcontrib><creatorcontrib>Altholtz, Melanie</creatorcontrib><creatorcontrib>Donis, Ruben</creatorcontrib><creatorcontrib>Subbarao, Kanta</creatorcontrib><title>Neuraminidase Stalk Length and Additional Glycosylation of the Hemagglutinin Influence the Virulence of Influenza H5N1 Viruses for Mice</title><title>Journal of Virology</title><addtitle>J Virol</addtitle><description>Following circulation of avian influenza H5 and H7 viruses in poultry, the hemagglutinin (HA) can acquire additional glycosylation sites, and the neuraminidase (NA) stalk becomes shorter. We investigated whether these features play a role in the pathogenesis of infection in mammalian hosts. From 1996 to 2007, H5N1 viruses with a short NA stalk have become widespread in several avian species. Compared to viruses with a long-stalk NA, viruses with a short-stalk NA showed a decreased capacity to elute from red blood cells and an increased virulence in mice, but not in chickens. The presence of additional HA glycosylation sites had less of an effect on virulence than did NA stalk length. The short-stalk NA of H5N1 viruses circulating in Asia may contribute to virulence in humans.</description><subject>Animals</subject><subject>avian influenza</subject><subject>Biological and medical sciences</subject><subject>Chickens</subject><subject>enzyme activity</subject><subject>Erythrocytes - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glycosylation</subject><subject>Hemagglutinin Glycoproteins, Influenza Virus - chemistry</subject><subject>Hemagglutinin Glycoproteins, Influenza Virus - metabolism</subject><subject>hemagglutinins</subject><subject>Influenza A virus</subject><subject>Influenza A Virus, H5N1 Subtype - classification</subject><subject>Influenza A Virus, H5N1 Subtype - enzymology</subject><subject>Influenza A Virus, H5N1 Subtype - genetics</subject><subject>Influenza A Virus, H5N1 Subtype - pathogenicity</subject><subject>mice</subject><subject>Mice - virology</subject><subject>Microbiology</subject><subject>Miscellaneous</subject><subject>Mutation - genetics</subject><subject>Neuraminidase - chemistry</subject><subject>Neuraminidase - genetics</subject><subject>Neuraminidase - metabolism</subject><subject>Orthomyxoviridae Infections</subject><subject>Pathogenesis and Immunity</subject><subject>poultry</subject><subject>poultry diseases</subject><subject>protein structure</subject><subject>sialidase</subject><subject>strains</subject><subject>Time Factors</subject><subject>viral diseases of animals and humans</subject><subject>Virology</subject><subject>Virulence</subject><subject>waterfowl</subject><subject>wild birds</subject><issn>1098-5514</issn><issn>0022-538X</issn><issn>1098-5514</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVks1uEzEURkcIREthxxrMAlak-H_sDVJVQRMUyqK0W-vGY09cPJ5izxSFF-C1mSZRKSv76js6vtLnqnpJ8DEhVH24vg3HmGhVz7B6VB0SrNVMCMIfP7gfVM9KucaYcC750-qAaEoFxvyw-nPuxgxdSKGB4tDFAPEHWrrUDmsEqUEnTROG0CeI6CxubF82Ee5m1Hs0rB2auw7aNo7DZEhokXwcXbJum12FPMbtNMH76DeguTgn26y4gnyf0ddg3fPqiYdY3Iv9eVRdfv70_XQ-W347W5yeLGdWUDXMCJOqsVo7rBleAaaSSU609Ljh1nrMHXdSSLuinAoqmlpokIxSJjTh3mt2VH3ceW_GVeca69KQIZqbHDrIG9NDMP8nKaxN298aKqUSuJ4E7_aC3P8cXRlMF4p1MUJy_ViMrAkRSogJfL8Dbe5Lyc7fP0KwuWvOfLlamG1zBqsJf_VwsX_wvqoJeLsHoFiIPkOyodxzlLCaa8om7s2OW4d2_StkZ6B0ZvolRjGjDa-3rtc7xkNvoM2T5_KCYsIwUTXnhLO_Y6O2_g</recordid><startdate>20090501</startdate><enddate>20090501</enddate><creator>Matsuoka, Yumiko</creator><creator>Swayne, David E</creator><creator>Thomas, Colleen</creator><creator>Rameix-Welti, Marie-Anne</creator><creator>Naffakh, Nadia</creator><creator>Warnes, Christine</creator><creator>Altholtz, Melanie</creator><creator>Donis, Ruben</creator><creator>Subbarao, Kanta</creator><general>American Society for Microbiology</general><general>American Society for Microbiology (ASM)</general><scope>FBQ</scope><scope>IQODW</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>7X8</scope><scope>5PM</scope></search><sort><creationdate>20090501</creationdate><title>Neuraminidase Stalk Length and Additional Glycosylation of the Hemagglutinin Influence the Virulence of Influenza H5N1 Viruses for Mice</title><author>Matsuoka, Yumiko ; Swayne, David E ; Thomas, Colleen ; Rameix-Welti, Marie-Anne ; Naffakh, Nadia ; Warnes, Christine ; Altholtz, Melanie ; Donis, Ruben ; Subbarao, Kanta</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c528t-1368dc99e0930ba026364196f0d4ccf04e4e656cb242525d759a632235914ff93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Animals</topic><topic>avian influenza</topic><topic>Biological and medical sciences</topic><topic>Chickens</topic><topic>enzyme activity</topic><topic>Erythrocytes - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glycosylation</topic><topic>Hemagglutinin Glycoproteins, Influenza Virus - chemistry</topic><topic>Hemagglutinin Glycoproteins, Influenza Virus - metabolism</topic><topic>hemagglutinins</topic><topic>Influenza A virus</topic><topic>Influenza A Virus, H5N1 Subtype - classification</topic><topic>Influenza A Virus, H5N1 Subtype - enzymology</topic><topic>Influenza A Virus, H5N1 Subtype - genetics</topic><topic>Influenza A Virus, H5N1 Subtype - pathogenicity</topic><topic>mice</topic><topic>Mice - virology</topic><topic>Microbiology</topic><topic>Miscellaneous</topic><topic>Mutation - genetics</topic><topic>Neuraminidase - chemistry</topic><topic>Neuraminidase - genetics</topic><topic>Neuraminidase - metabolism</topic><topic>Orthomyxoviridae Infections</topic><topic>Pathogenesis and Immunity</topic><topic>poultry</topic><topic>poultry diseases</topic><topic>protein structure</topic><topic>sialidase</topic><topic>strains</topic><topic>Time Factors</topic><topic>viral diseases of animals and humans</topic><topic>Virology</topic><topic>Virulence</topic><topic>waterfowl</topic><topic>wild birds</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Matsuoka, Yumiko</creatorcontrib><creatorcontrib>Swayne, David E</creatorcontrib><creatorcontrib>Thomas, Colleen</creatorcontrib><creatorcontrib>Rameix-Welti, Marie-Anne</creatorcontrib><creatorcontrib>Naffakh, Nadia</creatorcontrib><creatorcontrib>Warnes, Christine</creatorcontrib><creatorcontrib>Altholtz, Melanie</creatorcontrib><creatorcontrib>Donis, Ruben</creatorcontrib><creatorcontrib>Subbarao, Kanta</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Journal of Virology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Matsuoka, Yumiko</au><au>Swayne, David E</au><au>Thomas, Colleen</au><au>Rameix-Welti, Marie-Anne</au><au>Naffakh, Nadia</au><au>Warnes, Christine</au><au>Altholtz, Melanie</au><au>Donis, Ruben</au><au>Subbarao, Kanta</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Neuraminidase Stalk Length and Additional Glycosylation of the Hemagglutinin Influence the Virulence of Influenza H5N1 Viruses for Mice</atitle><jtitle>Journal of Virology</jtitle><addtitle>J Virol</addtitle><date>2009-05-01</date><risdate>2009</risdate><volume>83</volume><issue>9</issue><spage>4704</spage><epage>4708</epage><pages>4704-4708</pages><issn>1098-5514</issn><issn>0022-538X</issn><eissn>1098-5514</eissn><abstract>Following circulation of avian influenza H5 and H7 viruses in poultry, the hemagglutinin (HA) can acquire additional glycosylation sites, and the neuraminidase (NA) stalk becomes shorter. We investigated whether these features play a role in the pathogenesis of infection in mammalian hosts. From 1996 to 2007, H5N1 viruses with a short NA stalk have become widespread in several avian species. Compared to viruses with a long-stalk NA, viruses with a short-stalk NA showed a decreased capacity to elute from red blood cells and an increased virulence in mice, but not in chickens. The presence of additional HA glycosylation sites had less of an effect on virulence than did NA stalk length. The short-stalk NA of H5N1 viruses circulating in Asia may contribute to virulence in humans.</abstract><cop>Washington, DC</cop><pub>American Society for Microbiology</pub><pmid>19225004</pmid><doi>10.1128/jvi.01987-08</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Animals avian influenza Biological and medical sciences Chickens enzyme activity Erythrocytes - metabolism Fundamental and applied biological sciences. Psychology Glycosylation Hemagglutinin Glycoproteins, Influenza Virus - chemistry Hemagglutinin Glycoproteins, Influenza Virus - metabolism hemagglutinins Influenza A virus Influenza A Virus, H5N1 Subtype - classification Influenza A Virus, H5N1 Subtype - enzymology Influenza A Virus, H5N1 Subtype - genetics Influenza A Virus, H5N1 Subtype - pathogenicity mice Mice - virology Microbiology Miscellaneous Mutation - genetics Neuraminidase - chemistry Neuraminidase - genetics Neuraminidase - metabolism Orthomyxoviridae Infections Pathogenesis and Immunity poultry poultry diseases protein structure sialidase strains Time Factors viral diseases of animals and humans Virology Virulence waterfowl wild birds |
| title | Neuraminidase Stalk Length and Additional Glycosylation of the Hemagglutinin Influence the Virulence of Influenza H5N1 Viruses for Mice |
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