Functional significance of the hemadsorption activity of influenza virus neuraminidase and its alteration in pandemic viruses
Identifieur interne : 000013 ( Istex/Corpus ); précédent : 000012; suivant : 000014Functional significance of the hemadsorption activity of influenza virus neuraminidase and its alteration in pandemic viruses
Auteurs : Jennifer Uhlendorff ; Tatyana Matrosovich ; Hans-Dieter Klenk ; Mikhail MatrosovichSource :
- Archives of Virology [ 0304-8608 ] ; 2009-06-01.
Abstract
Abstract: Human influenza viruses derive their genes from avian viruses. The neuraminidase (NA) of the avian viruses has, in addition to the catalytic site, a separate sialic acid binding site (hemadsorption site) that is not present in human viruses. The biological significance of the NA hemadsorption activity in avian influenza viruses remained elusive. A sequence database analysis revealed that the NAs of the majority of human H2N2 viruses isolated during the influenza pandemic of 1957 differ from their putative avian precursor by amino acid substitutions in the hemadsorption site. We found that the NA of a representative pandemic virus A/Singapore/1/57 (H2N2) lacks hemadsorption activity and that a single reversion to the avian-virus-like sequence (N367S) restores hemadsorption. Using this hemadsorption-positive NA, we generated three NA variants with substitutions S370L, N400S and W403R that have been found in the hemadsorption site of human H2N2 viruses. Each substitution abolished hemadsorption activity. Although, there was no correlation between hemadsorption activity of the NA variants and their enzymatic activity with respect to monovalent substrates, all four hemadsorption-negative NAs desialylated macromolecular substrates significantly slower than did the hemadsorption-positive counterpart. The NA of the 1918 pandemic virus A/Brevig Mission/1/18 (H1N1) also differed from avian N1 NAs by reduced hemadsorption activity and less efficient hydrolysis of macromolecular substrates. Our data indicate that the hemadsorption site serves to enhance the catalytic efficiency of NA and they suggest that, in addition to changes in the receptor-binding specificity of the hemagglutinin, alterations of the NA are needed for the emergence of pandemic influenza viruses.
Url:
DOI: 10.1007/s00705-009-0393-x
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The neuraminidase (NA) of the avian viruses has, in addition to the catalytic site, a separate sialic acid binding site (hemadsorption site) that is not present in human viruses. The biological significance of the NA hemadsorption activity in avian influenza viruses remained elusive. A sequence database analysis revealed that the NAs of the majority of human H2N2 viruses isolated during the influenza pandemic of 1957 differ from their putative avian precursor by amino acid substitutions in the hemadsorption site. We found that the NA of a representative pandemic virus A/Singapore/1/57 (H2N2) lacks hemadsorption activity and that a single reversion to the avian-virus-like sequence (N367S) restores hemadsorption. Using this hemadsorption-positive NA, we generated three NA variants with substitutions S370L, N400S and W403R that have been found in the hemadsorption site of human H2N2 viruses. Each substitution abolished hemadsorption activity. Although, there was no correlation between hemadsorption activity of the NA variants and their enzymatic activity with respect to monovalent substrates, all four hemadsorption-negative NAs desialylated macromolecular substrates significantly slower than did the hemadsorption-positive counterpart. The NA of the 1918 pandemic virus A/Brevig Mission/1/18 (H1N1) also differed from avian N1 NAs by reduced hemadsorption activity and less efficient hydrolysis of macromolecular substrates. Our data indicate that the hemadsorption site serves to enhance the catalytic efficiency of NA and they suggest that, in addition to changes in the receptor-binding specificity of the hemagglutinin, alterations of the NA are needed for the emergence of pandemic influenza viruses.</div></front></TEI><istex><corpusName>springer-journals</corpusName><author><json:item><name>Jennifer Uhlendorff</name><affiliations><json:string>Institute of Virology, Philipps University, Hans-Meerwein-Str.2, 35043, Marburg, Germany</json:string></affiliations></json:item><json:item><name>Tatyana Matrosovich</name><affiliations><json:string>Institute of Virology, Philipps University, Hans-Meerwein-Str.2, 35043, Marburg, Germany</json:string></affiliations></json:item><json:item><name>Hans-Dieter Klenk</name><affiliations><json:string>Institute of Virology, Philipps University, Hans-Meerwein-Str.2, 35043, Marburg, Germany</json:string></affiliations></json:item><json:item><name>Mikhail Matrosovich</name><affiliations><json:string>Institute of Virology, Philipps University, Hans-Meerwein-Str.2, 35043, Marburg, Germany</json:string><json:string>E-mail: M.Matrosovich@gmail.com</json:string></affiliations></json:item></author><articleId><json:string>393</json:string><json:string>s00705-009-0393-x</json:string></articleId><arkIstex>ark:/67375/VQC-Q7CWW1GT-8</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>OriginalPaper</json:string></originalGenre><abstract>Abstract: Human influenza viruses derive their genes from avian viruses. The neuraminidase (NA) of the avian viruses has, in addition to the catalytic site, a separate sialic acid binding site (hemadsorption site) that is not present in human viruses. The biological significance of the NA hemadsorption activity in avian influenza viruses remained elusive. A sequence database analysis revealed that the NAs of the majority of human H2N2 viruses isolated during the influenza pandemic of 1957 differ from their putative avian precursor by amino acid substitutions in the hemadsorption site. We found that the NA of a representative pandemic virus A/Singapore/1/57 (H2N2) lacks hemadsorption activity and that a single reversion to the avian-virus-like sequence (N367S) restores hemadsorption. Using this hemadsorption-positive NA, we generated three NA variants with substitutions S370L, N400S and W403R that have been found in the hemadsorption site of human H2N2 viruses. Each substitution abolished hemadsorption activity. Although, there was no correlation between hemadsorption activity of the NA variants and their enzymatic activity with respect to monovalent substrates, all four hemadsorption-negative NAs desialylated macromolecular substrates significantly slower than did the hemadsorption-positive counterpart. The NA of the 1918 pandemic virus A/Brevig Mission/1/18 (H1N1) also differed from avian N1 NAs by reduced hemadsorption activity and less efficient hydrolysis of macromolecular substrates. 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The neuraminidase (NA) of the avian viruses has, in addition to the catalytic site, a separate sialic acid binding site (hemadsorption site) that is not present in human viruses. The biological significance of the NA hemadsorption activity in avian influenza viruses remained elusive. A sequence database analysis revealed that the NAs of the majority of human H2N2 viruses isolated during the influenza pandemic of 1957 differ from their putative avian precursor by amino acid substitutions in the hemadsorption site. We found that the NA of a representative pandemic virus A/Singapore/1/57 (H2N2) lacks hemadsorption activity and that a single reversion to the avian-virus-like sequence (N367S) restores hemadsorption. Using this hemadsorption-positive NA, we generated three NA variants with substitutions S370L, N400S and W403R that have been found in the hemadsorption site of human H2N2 viruses. Each substitution abolished hemadsorption activity. Although, there was no correlation between hemadsorption activity of the NA variants and their enzymatic activity with respect to monovalent substrates, all four hemadsorption-negative NAs desialylated macromolecular substrates significantly slower than did the hemadsorption-positive counterpart. The NA of the 1918 pandemic virus A/Brevig Mission/1/18 (H1N1) also differed from avian N1 NAs by reduced hemadsorption activity and less efficient hydrolysis of macromolecular substrates. Our data indicate that the hemadsorption site serves to enhance the catalytic efficiency of NA and they suggest that, in addition to changes in the receptor-binding specificity of the hemagglutinin, alterations of the NA are needed for the emergence of pandemic influenza viruses.</p></abstract><textClass><keywords scheme="Journal Subject"><list><head>Biomedicine</head><item><term>Infectious Diseases</term></item><item><term>Medical Microbiology</term></item><item><term>Virology</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="2009-03-12">Created</change><change when="2009-06-01">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/VQC-Q7CWW1GT-8/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="corpus springer-journals not found" wicri:toSee="no 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Author(s)</CopyrightHolderName><CopyrightYear>2009</CopyrightYear></ArticleCopyright><ArticleGrants Type="OpenChoice"><MetadataGrant Grant="OpenAccess"></MetadataGrant><AbstractGrant Grant="OpenAccess"></AbstractGrant><BodyPDFGrant Grant="OpenAccess"></BodyPDFGrant><BodyHTMLGrant Grant="OpenAccess"></BodyHTMLGrant><BibliographyGrant Grant="OpenAccess"></BibliographyGrant><ESMGrant Grant="OpenAccess"></ESMGrant></ArticleGrants></ArticleInfo><ArticleHeader><AuthorGroup><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Jennifer</GivenName><FamilyName>Uhlendorff</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Tatyana</GivenName><FamilyName>Matrosovich</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Hans-Dieter</GivenName><FamilyName>Klenk</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1" CorrespondingAffiliationID="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Mikhail</GivenName><FamilyName>Matrosovich</FamilyName></AuthorName><Contact><Phone>+49-6421-2865166</Phone><Fax>+49-6421-2868962</Fax><Email>M.Matrosovich@gmail.com</Email></Contact></Author><Affiliation ID="Aff1"><OrgDivision>Institute of Virology</OrgDivision><OrgName>Philipps University</OrgName><OrgAddress><Street>Hans-Meerwein-Str.2</Street><Postcode>35043</Postcode><City>Marburg</City><Country Code="DE">Germany</Country></OrgAddress></Affiliation></AuthorGroup><Abstract ID="Abs1" Language="En" OutputMedium="All"><Heading>Abstract</Heading><Para>Human influenza viruses derive their genes from avian viruses. The neuraminidase (NA) of the avian viruses has, in addition to the catalytic site, a separate sialic acid binding site (hemadsorption site) that is not present in human viruses. The biological significance of the NA hemadsorption activity in avian influenza viruses remained elusive. A sequence database analysis revealed that the NAs of the majority of human H2N2 viruses isolated during the influenza pandemic of 1957 differ from their putative avian precursor by amino acid substitutions in the hemadsorption site. We found that the NA of a representative pandemic virus A/Singapore/1/57 (H2N2) lacks hemadsorption activity and that a single reversion to the avian-virus-like sequence (N367S) restores hemadsorption. Using this hemadsorption-positive NA, we generated three NA variants with substitutions S370L, N400S and W403R that have been found in the hemadsorption site of human H2N2 viruses. Each substitution abolished hemadsorption activity. Although, there was no correlation between hemadsorption activity of the NA variants and their enzymatic activity with respect to monovalent substrates, all four hemadsorption-negative NAs desialylated macromolecular substrates significantly slower than did the hemadsorption-positive counterpart. The NA of the 1918 pandemic virus A/Brevig Mission/1/18 (H1N1) also differed from avian N1 NAs by reduced hemadsorption activity and less efficient hydrolysis of macromolecular substrates. Our data indicate that the hemadsorption site serves to enhance the catalytic efficiency of NA and they suggest that, in addition to changes in the receptor-binding specificity of the hemagglutinin, alterations of the NA are needed for the emergence of pandemic influenza viruses.</Para></Abstract></ArticleHeader><NoBody></NoBody></Article></Issue></Volume></Journal></Publisher></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Functional significance of the hemadsorption activity of influenza virus neuraminidase and its alteration in pandemic viruses</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Functional significance of the hemadsorption activity of influenza virus neuraminidase and its alteration in pandemic viruses</title></titleInfo><name type="personal"><namePart type="given">Jennifer</namePart><namePart type="family">Uhlendorff</namePart><affiliation>Institute of Virology, Philipps University, Hans-Meerwein-Str.2, 35043, Marburg, Germany</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Tatyana</namePart><namePart type="family">Matrosovich</namePart><affiliation>Institute of Virology, Philipps University, Hans-Meerwein-Str.2, 35043, Marburg, Germany</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Hans-Dieter</namePart><namePart type="family">Klenk</namePart><affiliation>Institute of Virology, Philipps University, Hans-Meerwein-Str.2, 35043, Marburg, Germany</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal" displayLabel="corresp"><namePart type="given">Mikhail</namePart><namePart type="family">Matrosovich</namePart><affiliation>Institute of Virology, Philipps University, Hans-Meerwein-Str.2, 35043, Marburg, Germany</affiliation><affiliation>E-mail: M.Matrosovich@gmail.com</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="OriginalPaper" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>Springer Vienna</publisher><place><placeTerm type="text">Vienna</placeTerm></place><dateCreated encoding="w3cdtf">2009-03-12</dateCreated><dateIssued encoding="w3cdtf">2009-06-01</dateIssued><copyrightDate encoding="w3cdtf">2009</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><abstract lang="en">Abstract: Human influenza viruses derive their genes from avian viruses. The neuraminidase (NA) of the avian viruses has, in addition to the catalytic site, a separate sialic acid binding site (hemadsorption site) that is not present in human viruses. The biological significance of the NA hemadsorption activity in avian influenza viruses remained elusive. A sequence database analysis revealed that the NAs of the majority of human H2N2 viruses isolated during the influenza pandemic of 1957 differ from their putative avian precursor by amino acid substitutions in the hemadsorption site. We found that the NA of a representative pandemic virus A/Singapore/1/57 (H2N2) lacks hemadsorption activity and that a single reversion to the avian-virus-like sequence (N367S) restores hemadsorption. Using this hemadsorption-positive NA, we generated three NA variants with substitutions S370L, N400S and W403R that have been found in the hemadsorption site of human H2N2 viruses. Each substitution abolished hemadsorption activity. Although, there was no correlation between hemadsorption activity of the NA variants and their enzymatic activity with respect to monovalent substrates, all four hemadsorption-negative NAs desialylated macromolecular substrates significantly slower than did the hemadsorption-positive counterpart. The NA of the 1918 pandemic virus A/Brevig Mission/1/18 (H1N1) also differed from avian N1 NAs by reduced hemadsorption activity and less efficient hydrolysis of macromolecular substrates. Our data indicate that the hemadsorption site serves to enhance the catalytic efficiency of NA and they suggest that, in addition to changes in the receptor-binding specificity of the hemagglutinin, alterations of the NA are needed for the emergence of pandemic influenza viruses.</abstract><note>Original Article</note><relatedItem type="host"><titleInfo><title>Archives of Virology</title><subTitle>Official Journal of the Virology Division of the International Union of Microbiological Societies</subTitle></titleInfo><titleInfo type="abbreviated"><title>Arch Virol</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>Springer</publisher><dateIssued encoding="w3cdtf">2009-06-05</dateIssued><copyrightDate encoding="w3cdtf">2009</copyrightDate></originInfo><subject><genre>Biomedicine</genre><topic>Infectious Diseases</topic><topic>Medical Microbiology</topic><topic>Virology</topic></subject><identifier type="ISSN">0304-8608</identifier><identifier type="eISSN">1432-8798</identifier><identifier type="JournalID">705</identifier><identifier type="IssueArticleCount">15</identifier><identifier type="VolumeIssueCount">12</identifier><part><date>2009</date><detail type="volume"><number>154</number><caption>vol.</caption></detail><detail type="issue"><number>6</number><caption>no.</caption></detail><extent unit="pages"><start>945</start><end>957</end></extent></part><recordInfo><recordOrigin>Springer-Verlag, 2009</recordOrigin></recordInfo></relatedItem><identifier type="istex">D581EDCB9D9E9EE8B977AB9777561F2F7B853367</identifier><identifier type="ark">ark:/67375/VQC-Q7CWW1GT-8</identifier><identifier type="DOI">10.1007/s00705-009-0393-x</identifier><identifier type="ArticleID">393</identifier><identifier type="ArticleID">s00705-009-0393-x</identifier><accessCondition type="use and reproduction" contentType="copyright">The Author(s), 2009</accessCondition><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-3XSW68JL-F">springer</recordContentSource><recordOrigin>The Author(s), 2009</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/VQC-Q7CWW1GT-8/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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