Galectins promote the interaction of influenza virus with its target cell
Identifieur interne : 000279 ( Istex/Corpus ); précédent : 000278; suivant : 000280Galectins promote the interaction of influenza virus with its target cell
Auteurs : E. S. Chernyy ; E. M. Rapoport ; S. Andre ; H. Kaltner ; H. J. Gabius ; N. V. BovinSource :
- Biochemistry (Moscow) [ 0006-2979 ] ; 2011-08-01.
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Abstract
Abstract: Influenza virus is known to bind sialoglycans located on the surface of the host cell. In addition, recent data suggest the involvement of other molecular targets in viral reception. Of note, a high density of terminal galactose residues is created on the surface of virions because of the influenza virus’ own neuraminidase activity. Thus, we suggested the possibility for an interaction of the influenza virus with galactose-binding proteins — galectins. In the present work we studied the influence of several galectins on the adhesion and further internalization of virus into the cell; six virus strains and three cell lines were studied. Chicken galectins CG-1A and -2 as well as human galectins HGal-1 and -8 promote virus binding in dose dependent manner, but they do not influence the internalization stage. Also, galectins are able to restore the ability of influenza virus to infect desialylated cells up to the level of native cells. When CG-1A in physiological concentrations was loaded onto viruses, the adhesion level was higher than in the case of on-cell loading. The effect of adhesion increase depends on the glycan structure of target-cell as well as of virus. The aggregated data suggest a promotional effect of galectins during the stage of influenza virus binding with the surface of target-cell.
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DOI: 10.1134/S0006297911080128
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Andre</name><affiliation><mods:affiliation>Institute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig Maximilians University, Veterinar str. 13, 80539, Munich, Germany</mods:affiliation></affiliation></author><author><name sortKey="Kaltner, H" sort="Kaltner, H" uniqKey="Kaltner H" first="H." last="Kaltner">H. Kaltner</name><affiliation><mods:affiliation>Institute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig Maximilians University, Veterinar str. 13, 80539, Munich, Germany</mods:affiliation></affiliation></author><author><name sortKey="Gabius, H J" sort="Gabius, H J" uniqKey="Gabius H" first="H. J." last="Gabius">H. J. Gabius</name><affiliation><mods:affiliation>Institute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig Maximilians University, Veterinar str. 13, 80539, Munich, Germany</mods:affiliation></affiliation></author><author><name sortKey="Bovin, N V" sort="Bovin, N V" uniqKey="Bovin N" first="N. V." last="Bovin">N. V. 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In addition, recent data suggest the involvement of other molecular targets in viral reception. Of note, a high density of terminal galactose residues is created on the surface of virions because of the influenza virus’ own neuraminidase activity. Thus, we suggested the possibility for an interaction of the influenza virus with galactose-binding proteins — galectins. In the present work we studied the influence of several galectins on the adhesion and further internalization of virus into the cell; six virus strains and three cell lines were studied. Chicken galectins CG-1A and -2 as well as human galectins HGal-1 and -8 promote virus binding in dose dependent manner, but they do not influence the internalization stage. Also, galectins are able to restore the ability of influenza virus to infect desialylated cells up to the level of native cells. When CG-1A in physiological concentrations was loaded onto viruses, the adhesion level was higher than in the case of on-cell loading. The effect of adhesion increase depends on the glycan structure of target-cell as well as of virus. The aggregated data suggest a promotional effect of galectins during the stage of influenza virus binding with the surface of target-cell.</div></front></TEI><istex><corpusName>springer-journals</corpusName><author><json:item><name>E. S. Chernyy</name><affiliations><json:string>Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, 117997, Moscow, Russia</json:string></affiliations></json:item><json:item><name>E. M. Rapoport</name><affiliations><json:string>Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, 117997, Moscow, Russia</json:string></affiliations></json:item><json:item><name>S. Andre</name><affiliations><json:string>Institute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig Maximilians University, Veterinar str. 13, 80539, Munich, Germany</json:string></affiliations></json:item><json:item><name>H. Kaltner</name><affiliations><json:string>Institute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig Maximilians University, Veterinar str. 13, 80539, Munich, Germany</json:string></affiliations></json:item><json:item><name>H. -J. Gabius</name><affiliations><json:string>Institute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig Maximilians University, Veterinar str. 13, 80539, Munich, Germany</json:string></affiliations></json:item><json:item><name>N. V. Bovin</name><affiliations><json:string>Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, 117997, Moscow, Russia</json:string><json:string>E-mail: bovin@carb.ibch.ru</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>influenza virus</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>galectins</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>glycans</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>BSA : bovine serum albumin</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>C-virus : virus passaged in chicken embryos</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>CG : chicken galectins</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>FITC : fluorescein isothiocyanate</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>HA : hemagglutinin</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>HGal : human galectins</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>M-virus : virus passaged in MDCK (Madin-Darby Canine Kidney) cells</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>NA : neuraminidase</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Neu5Ac : N-acetyl-neuraminic acid</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>PBA : phosphate buffered saline containing 0.2% BSA</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>PBS : phosphate buffered saline</value></json:item></subject><articleId><json:string>9465</json:string><json:string>S0006297911080128</json:string></articleId><arkIstex>ark:/67375/VQC-CLKC4HP9-Z</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>OriginalPaper</json:string></originalGenre><abstract>Abstract: Influenza virus is known to bind sialoglycans located on the surface of the host cell. In addition, recent data suggest the involvement of other molecular targets in viral reception. Of note, a high density of terminal galactose residues is created on the surface of virions because of the influenza virus’ own neuraminidase activity. Thus, we suggested the possibility for an interaction of the influenza virus with galactose-binding proteins — galectins. In the present work we studied the influence of several galectins on the adhesion and further internalization of virus into the cell; six virus strains and three cell lines were studied. Chicken galectins CG-1A and -2 as well as human galectins HGal-1 and -8 promote virus binding in dose dependent manner, but they do not influence the internalization stage. Also, galectins are able to restore the ability of influenza virus to infect desialylated cells up to the level of native cells. When CG-1A in physiological concentrations was loaded onto viruses, the adhesion level was higher than in the case of on-cell loading. The effect of adhesion increase depends on the glycan structure of target-cell as well as of virus. 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In addition, recent data suggest the involvement of other molecular targets in viral reception. Of note, a high density of terminal galactose residues is created on the surface of virions because of the influenza virus’ own neuraminidase activity. Thus, we suggested the possibility for an interaction of the influenza virus with galactose-binding proteins — galectins. In the present work we studied the influence of several galectins on the adhesion and further internalization of virus into the cell; six virus strains and three cell lines were studied. Chicken galectins CG-1A and -2 as well as human galectins HGal-1 and -8 promote virus binding in dose dependent manner, but they do not influence the internalization stage. Also, galectins are able to restore the ability of influenza virus to infect desialylated cells up to the level of native cells. When CG-1A in physiological concentrations was loaded onto viruses, the adhesion level was higher than in the case of on-cell loading. The effect of adhesion increase depends on the glycan structure of target-cell as well as of virus. The aggregated data suggest a promotional effect of galectins during the stage of influenza virus binding with the surface of target-cell.</p></abstract><textClass xml:lang="en"><keywords scheme="keyword"><list><head>Key words</head><item><term>influenza virus</term></item><item><term>galectins</term></item><item><term>glycans</term></item></list></keywords></textClass><textClass><keywords scheme="keyword"><list><head>Abbreviations</head><item><term>BSA</term><term>bovine serum albumin</term></item><item><term>C-virus</term><term>virus passaged in chicken embryos</term></item><item><term>CG</term><term>chicken galectins</term></item><item><term>FITC</term><term>fluorescein isothiocyanate</term></item><item><term>HA</term><term>hemagglutinin</term></item><item><term>HGal</term><term>human galectins</term></item><item><term>M-virus</term><term>virus passaged in MDCK (Madin-Darby Canine Kidney) cells</term></item><item><term>NA</term><term>neuraminidase</term></item><item><term>Neu5Ac</term><term>N-acetyl-neuraminic acid</term></item><item><term>PBA</term><term>phosphate buffered saline containing 0.2% BSA</term></item><item><term>PBS</term><term>phosphate buffered saline</term></item></list></keywords></textClass><textClass><keywords scheme="Journal Subject"><list><head>Life Sciences</head><item><term>Biomedicine general</term></item><item><term>Microbiology</term></item><item><term>Bioorganic Chemistry</term></item><item><term>Biochemistry, general</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="2011-01-31">Created</change><change when="2011-08-01">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-CLKC4HP9-Z/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml 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Grant="OpenAccess"></MetadataGrant><AbstractGrant Grant="OpenAccess"></AbstractGrant><BodyPDFGrant Grant="Restricted"></BodyPDFGrant><BodyHTMLGrant Grant="Restricted"></BodyHTMLGrant><BibliographyGrant Grant="Restricted"></BibliographyGrant><ESMGrant Grant="Restricted"></ESMGrant></ArticleGrants></ArticleInfo><ArticleHeader><AuthorGroup><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>E.</GivenName><GivenName>S.</GivenName><FamilyName>Chernyy</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>E.</GivenName><GivenName>M.</GivenName><FamilyName>Rapoport</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff2"><AuthorName DisplayOrder="Western"><GivenName>S.</GivenName><FamilyName>Andre</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff2"><AuthorName DisplayOrder="Western"><GivenName>H.</GivenName><FamilyName>Kaltner</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff2"><AuthorName DisplayOrder="Western"><GivenName>H.</GivenName><GivenName>-J.</GivenName><FamilyName>Gabius</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1" CorrespondingAffiliationID="Aff1"><AuthorName DisplayOrder="Western"><GivenName>N.</GivenName><GivenName>V.</GivenName><FamilyName>Bovin</FamilyName></AuthorName><Contact><Fax>(495) 330-5592</Fax><Email>bovin@carb.ibch.ru</Email></Contact></Author><Affiliation ID="Aff1"><OrgDivision>Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry</OrgDivision><OrgName>Russian Academy of Sciences</OrgName><OrgAddress><Street>ul. Miklukho-Maklaya 16/10</Street><Postcode>117997</Postcode><City>Moscow</City><Country Code="RU">Russia</Country></OrgAddress></Affiliation><Affiliation ID="Aff2"><OrgDivision>Institute of Physiological Chemistry, Faculty of Veterinary Medicine</OrgDivision><OrgName>Ludwig Maximilians University</OrgName><OrgAddress><Street>Veterinar str. 13</Street><Postcode>80539</Postcode><City>Munich</City><Country Code="DE">Germany</Country></OrgAddress></Affiliation></AuthorGroup><Abstract ID="Abs1" Language="En"><Heading>Abstract</Heading><Para TextBreak="No">Influenza virus is known to bind sialoglycans located on the surface of the host cell. In addition, recent data suggest the involvement of other molecular targets in viral reception. Of note, a high density of terminal galactose residues is created on the surface of virions because of the influenza virus’ own neuraminidase activity. Thus, we suggested the possibility for an interaction of the influenza virus with galactose-binding proteins — galectins. In the present work we studied the influence of several galectins on the adhesion and further internalization of virus into the cell; six virus strains and three cell lines were studied. Chicken galectins CG-1A and -2 as well as human galectins HGal-1 and -8 promote virus binding in dose dependent manner, but they do not influence the internalization stage. Also, galectins are able to restore the ability of influenza virus to infect desialylated cells up to the level of native cells. When CG-1A in physiological concentrations was loaded onto viruses, the adhesion level was higher than in the case of on-cell loading. The effect of adhesion increase depends on the glycan structure of target-cell as well as of virus. The aggregated data suggest a promotional effect of galectins during the stage of influenza virus binding with the surface of target-cell.</Para></Abstract><KeywordGroup Language="En"><Heading>Key words</Heading><Keyword>influenza virus</Keyword><Keyword>galectins</Keyword><Keyword>glycans</Keyword></KeywordGroup><AbbreviationGroup><Heading>Abbreviations</Heading><DefinitionList><DefinitionListEntry><Term>BSA</Term><Description><Para TextBreak="No">bovine serum albumin</Para></Description></DefinitionListEntry><DefinitionListEntry><Term>C-virus</Term><Description><Para TextBreak="No">virus passaged in chicken embryos</Para></Description></DefinitionListEntry><DefinitionListEntry><Term>CG</Term><Description><Para TextBreak="No">chicken galectins</Para></Description></DefinitionListEntry><DefinitionListEntry><Term>FITC</Term><Description><Para TextBreak="No">fluorescein isothiocyanate</Para></Description></DefinitionListEntry><DefinitionListEntry><Term>HA</Term><Description><Para TextBreak="No">hemagglutinin</Para></Description></DefinitionListEntry><DefinitionListEntry><Term>HGal</Term><Description><Para TextBreak="No">human galectins</Para></Description></DefinitionListEntry><DefinitionListEntry><Term>M-virus</Term><Description><Para TextBreak="No">virus passaged in MDCK (Madin-Darby Canine Kidney) cells</Para></Description></DefinitionListEntry><DefinitionListEntry><Term>NA</Term><Description><Para TextBreak="No">neuraminidase</Para></Description></DefinitionListEntry><DefinitionListEntry><Term>Neu5Ac</Term><Description><Para TextBreak="No">N-acetyl-neuraminic acid</Para></Description></DefinitionListEntry><DefinitionListEntry><Term>PBA</Term><Description><Para TextBreak="No">phosphate buffered saline containing 0.2% BSA</Para></Description></DefinitionListEntry><DefinitionListEntry><Term>PBS</Term><Description><Para TextBreak="No">phosphate buffered saline</Para></Description></DefinitionListEntry></DefinitionList></AbbreviationGroup><ArticleNote Type="Misc"><SimplePara>Published in Russian in Biokhimiya, 2011, Vol. 76, No. 8, pp. 1173–1184.</SimplePara><SimplePara>Originally published in Biochemistry (Moscow) On-Line Papers in Press, as Manuscript BM11-041, April 24, 2011.</SimplePara></ArticleNote></ArticleHeader><NoBody></NoBody></Article></Issue></Volume></Journal></Publisher></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Galectins promote the interaction of influenza virus with its target cell</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Galectins promote the interaction of influenza virus with its target cell</title></titleInfo><name type="personal"><namePart type="given">E.</namePart><namePart type="given">S.</namePart><namePart type="family">Chernyy</namePart><affiliation>Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, 117997, Moscow, Russia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">E.</namePart><namePart type="given">M.</namePart><namePart type="family">Rapoport</namePart><affiliation>Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, 117997, Moscow, Russia</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">S.</namePart><namePart type="family">Andre</namePart><affiliation>Institute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig Maximilians University, Veterinar str. 13, 80539, Munich, Germany</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">H.</namePart><namePart type="family">Kaltner</namePart><affiliation>Institute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig Maximilians University, Veterinar str. 13, 80539, Munich, Germany</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">H.</namePart><namePart type="given">-J.</namePart><namePart type="family">Gabius</namePart><affiliation>Institute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig Maximilians University, Veterinar str. 13, 80539, Munich, Germany</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal" displayLabel="corresp"><namePart type="given">N.</namePart><namePart type="given">V.</namePart><namePart type="family">Bovin</namePart><affiliation>Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, 117997, Moscow, Russia</affiliation><affiliation>E-mail: bovin@carb.ibch.ru</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>SP MAIK Nauka/Interperiodica</publisher><place><placeTerm type="text">Dordrecht</placeTerm></place><dateCreated encoding="w3cdtf">2011-01-31</dateCreated><dateIssued encoding="w3cdtf">2011-08-01</dateIssued><copyrightDate encoding="w3cdtf">2011</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><abstract lang="en">Abstract: Influenza virus is known to bind sialoglycans located on the surface of the host cell. In addition, recent data suggest the involvement of other molecular targets in viral reception. Of note, a high density of terminal galactose residues is created on the surface of virions because of the influenza virus’ own neuraminidase activity. Thus, we suggested the possibility for an interaction of the influenza virus with galactose-binding proteins — galectins. In the present work we studied the influence of several galectins on the adhesion and further internalization of virus into the cell; six virus strains and three cell lines were studied. Chicken galectins CG-1A and -2 as well as human galectins HGal-1 and -8 promote virus binding in dose dependent manner, but they do not influence the internalization stage. Also, galectins are able to restore the ability of influenza virus to infect desialylated cells up to the level of native cells. When CG-1A in physiological concentrations was loaded onto viruses, the adhesion level was higher than in the case of on-cell loading. The effect of adhesion increase depends on the glycan structure of target-cell as well as of virus. The aggregated data suggest a promotional effect of galectins during the stage of influenza virus binding with the surface of target-cell.</abstract><subject lang="en"><genre>Key words</genre><topic>influenza virus</topic><topic>galectins</topic><topic>glycans</topic></subject><subject><genre>Abbreviations</genre><topic>BSA : bovine serum albumin</topic><topic>C-virus : virus passaged in chicken embryos</topic><topic>CG : chicken galectins</topic><topic>FITC : fluorescein isothiocyanate</topic><topic>HA : hemagglutinin</topic><topic>HGal : human galectins</topic><topic>M-virus : virus passaged in MDCK (Madin-Darby Canine Kidney) cells</topic><topic>NA : neuraminidase</topic><topic>Neu5Ac : N-acetyl-neuraminic acid</topic><topic>PBA : phosphate buffered saline containing 0.2% BSA</topic><topic>PBS : phosphate buffered saline</topic></subject><relatedItem type="host"><titleInfo><title>Biochemistry (Moscow)</title></titleInfo><titleInfo type="abbreviated"><title>Biochemistry Moscow</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">2011-08-16</dateIssued><copyrightDate encoding="w3cdtf">2011</copyrightDate></originInfo><subject><genre>Life Sciences</genre><topic>Biomedicine general</topic><topic>Microbiology</topic><topic>Bioorganic Chemistry</topic><topic>Biochemistry, general</topic></subject><identifier type="ISSN">0006-2979</identifier><identifier type="eISSN">1608-3040</identifier><identifier type="JournalID">10541</identifier><identifier type="IssueArticleCount">14</identifier><identifier type="VolumeIssueCount">13</identifier><part><date>2011</date><detail type="volume"><number>76</number><caption>vol.</caption></detail><detail type="issue"><number>8</number><caption>no.</caption></detail><extent unit="pages"><start>958</start><end>967</end></extent></part><recordInfo><recordOrigin>Pleiades Publishing, Ltd., 2011</recordOrigin></recordInfo></relatedItem><identifier type="istex">D0AAE286A5E112CFAD3CA8066328E383BF0A469E</identifier><identifier type="ark">ark:/67375/VQC-CLKC4HP9-Z</identifier><identifier type="DOI">10.1134/S0006297911080128</identifier><identifier type="ArticleID">9465</identifier><identifier type="ArticleID">S0006297911080128</identifier><accessCondition type="use and reproduction" contentType="copyright">Pleiades Publishing, Ltd., 2011</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>Pleiades Publishing, Ltd., 2011</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/VQC-CLKC4HP9-Z/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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