Beyond the classical: Influenza virus and the elucidation of alternative MHC class II-restricted antigen processing pathways
Identifieur interne : 001876 ( Istex/Corpus ); précédent : 001875; suivant : 001877Beyond the classical: Influenza virus and the elucidation of alternative MHC class II-restricted antigen processing pathways
Auteurs : Laurence C. Eisenlohr ; Nancy Luckashenak ; Sebastien Apcher ; Michael A. Miller ; Gomathinayagam SinnathambySource :
- Immunologic Research [ 0257-277X ] ; 2011-12-01.
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Abstract
Abstract: CD4+ T cells (TCD4+) are activated by peptides, generally 13–17 amino acids in length, presented at the cell surface in combination with highly polymorphic MHC class II molecules. According to the classical model, these peptides are generated by endosomal digestion of internalized antigen and loaded onto MHC class II molecules in the late endosome. Historically, this “exogenous” pathway has been defined through the extensive use of purified proteins. However, the relatively recent use of clinically relevant antigens, those of influenza virus in our case, has revealed several additional pathways of peptide production, including some that are truly “endogenous”, entailing synthesis of the protein within the infected cell. Indeed, some peptides appear to be created only via endogenous processing. The cell biology that underlies these alternative pathways remains poorly understood as do their relative contributions to defence against infectious agents and cancer, and the triggering of autoimmune diseases.
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DOI: 10.1007/s12026-011-8257-3
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Eisenlohr</name><affiliation><mods:affiliation>Department of Microbiology and Immunology, Kimmel Cancer Center, Thomas Jefferson University, Philadelphia, PA, USA</mods:affiliation></affiliation><affiliation><mods:affiliation>BLSB, Room 730, 233 South 10th Street, 19107, Philadelphia, PA, USA</mods:affiliation></affiliation><affiliation><mods:affiliation>E-mail: Laurence.Eisenlohr@jefferson.edu</mods:affiliation></affiliation></author><author><name sortKey="Luckashenak, Nancy" sort="Luckashenak, Nancy" uniqKey="Luckashenak N" first="Nancy" last="Luckashenak">Nancy Luckashenak</name><affiliation><mods:affiliation>Department of Microbiology and Immunology, Kimmel Cancer Center, Thomas Jefferson University, Philadelphia, PA, USA</mods:affiliation></affiliation></author><author><name sortKey="Apcher, Sebastien" sort="Apcher, Sebastien" uniqKey="Apcher S" first="Sebastien" last="Apcher">Sebastien Apcher</name><affiliation><mods:affiliation>Department of Microbiology and Immunology, Kimmel Cancer Center, Thomas Jefferson University, Philadelphia, PA, USA</mods:affiliation></affiliation></author><author><name sortKey="Miller, Michael A" sort="Miller, Michael A" uniqKey="Miller M" first="Michael A." last="Miller">Michael A. 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According to the classical model, these peptides are generated by endosomal digestion of internalized antigen and loaded onto MHC class II molecules in the late endosome. Historically, this “exogenous” pathway has been defined through the extensive use of purified proteins. However, the relatively recent use of clinically relevant antigens, those of influenza virus in our case, has revealed several additional pathways of peptide production, including some that are truly “endogenous”, entailing synthesis of the protein within the infected cell. Indeed, some peptides appear to be created only via endogenous processing. The cell biology that underlies these alternative pathways remains poorly understood as do their relative contributions to defence against infectious agents and cancer, and the triggering of autoimmune diseases.</div></front></TEI><istex><corpusName>springer-journals</corpusName><author><json:item><name>Laurence C. 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According to the classical model, these peptides are generated by endosomal digestion of internalized antigen and loaded onto MHC class II molecules in the late endosome. Historically, this “exogenous” pathway has been defined through the extensive use of purified proteins. However, the relatively recent use of clinically relevant antigens, those of influenza virus in our case, has revealed several additional pathways of peptide production, including some that are truly “endogenous”, entailing synthesis of the protein within the infected cell. Indeed, some peptides appear to be created only via endogenous processing. The cell biology that underlies these alternative pathways remains poorly understood as do their relative contributions to defence against infectious agents and cancer, and the triggering of autoimmune diseases.</p></abstract><textClass xml:lang="en"><keywords scheme="keyword"><list><head>Keywords</head><item><term>Antigen processing</term></item><item><term>Antigen presentation</term></item><item><term>Influenza</term></item><item><term>Major histocompatibility class II</term></item><item><term>Endogenous</term></item><item><term>Exogenous</term></item></list></keywords></textClass><textClass><keywords scheme="Journal Subject"><list><head>Medicine & Public Health</head><item><term>Medicine/Public Health, general</term></item><item><term>Immunology</term></item><item><term>Allergology</term></item><item><term>Internal Medicine</term></item></list></keywords></textClass></profileDesc><revisionDesc><change 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Grant="Restricted"></BodyPDFGrant><BodyHTMLGrant Grant="Restricted"></BodyHTMLGrant><BibliographyGrant Grant="Restricted"></BibliographyGrant><ESMGrant Grant="Restricted"></ESMGrant></ArticleGrants></ArticleInfo><ArticleHeader><AuthorGroup><Author AffiliationIDS="Aff1 Aff2" CorrespondingAffiliationID="Aff2"><AuthorName DisplayOrder="Western"><GivenName>Laurence</GivenName><GivenName>C.</GivenName><FamilyName>Eisenlohr</FamilyName></AuthorName><Contact><Phone>215 503-4540</Phone><Fax>215 923-4153</Fax><Email>Laurence.Eisenlohr@jefferson.edu</Email></Contact><Biography><FormalPara RenderingStyle="Style1"><Heading>Laurence C. Eisenlohr</Heading><Para><Figure Category="Standard" Float="No" ID="Figa"><MediaObject ID="MO100"><ImageObject Color="Color" Format="JPEG" Rendition="HTML" Type="Halftone" FileRef="MediaObjects/12026_2011_8257_Figa_HTML.jpg"></ImageObject></MediaObject></Figure></Para></FormalPara></Biography></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Nancy</GivenName><FamilyName>Luckashenak</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Sebastien</GivenName><FamilyName>Apcher</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Michael</GivenName><GivenName>A.</GivenName><FamilyName>Miller</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Gomathinayagam</GivenName><FamilyName>Sinnathamby</FamilyName></AuthorName></Author><Affiliation ID="Aff1"><OrgDivision>Department of Microbiology and Immunology, Kimmel Cancer Center</OrgDivision><OrgName>Thomas Jefferson University</OrgName><OrgAddress><City>Philadelphia</City><State>PA</State><Country Code="US">USA</Country></OrgAddress></Affiliation><Affiliation ID="Aff2"><OrgName>BLSB</OrgName><OrgAddress><Street>Room 730, 233 South 10th Street</Street><City>Philadelphia</City><State>PA</State><Postcode>19107</Postcode><Country Code="US">USA</Country></OrgAddress></Affiliation></AuthorGroup><Abstract ID="Abs1" Language="En" OutputMedium="All"><Heading>Abstract</Heading><Para>CD4+ T cells (T<Subscript>CD4+</Subscript>) are activated by peptides, generally 13–17 amino acids in length, presented at the cell surface in combination with highly polymorphic MHC class II molecules. According to the classical model, these peptides are generated by endosomal digestion of internalized antigen and loaded onto MHC class II molecules in the late endosome. Historically, this “exogenous” pathway has been defined through the extensive use of purified proteins. However, the relatively recent use of clinically relevant antigens, those of influenza virus in our case, has revealed several additional pathways of peptide production, including some that are truly “endogenous”, entailing synthesis of the protein within the infected cell. Indeed, some peptides appear to be created only via endogenous processing. The cell biology that underlies these alternative pathways remains poorly understood as do their relative contributions to defence against infectious agents and cancer, and the triggering of autoimmune diseases.</Para></Abstract><KeywordGroup Language="En" OutputMedium="All"><Heading>Keywords</Heading><Keyword>Antigen processing</Keyword><Keyword>Antigen presentation</Keyword><Keyword>Influenza</Keyword><Keyword>Major histocompatibility class II</Keyword><Keyword>Endogenous</Keyword><Keyword>Exogenous</Keyword></KeywordGroup></ArticleHeader><NoBody></NoBody></Article></Issue></Volume></Journal></Publisher></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Beyond the classical: Influenza virus and the elucidation of alternative MHC class II-restricted antigen processing pathways</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Beyond the classical: Influenza virus and the elucidation of alternative MHC class II-restricted antigen processing pathways</title></titleInfo><name type="personal" displayLabel="corresp"><namePart type="given">Laurence</namePart><namePart type="given">C.</namePart><namePart type="family">Eisenlohr</namePart><affiliation>Department of Microbiology and Immunology, Kimmel Cancer Center, Thomas Jefferson University, Philadelphia, PA, USA</affiliation><affiliation>BLSB, Room 730, 233 South 10th Street, 19107, Philadelphia, PA, USA</affiliation><affiliation>E-mail: Laurence.Eisenlohr@jefferson.edu</affiliation><role><roleTerm type="text">author</roleTerm></role><description>Laurence C. Eisenlohr</description></name><name type="personal"><namePart type="given">Nancy</namePart><namePart type="family">Luckashenak</namePart><affiliation>Department of Microbiology and Immunology, Kimmel Cancer Center, Thomas Jefferson University, Philadelphia, PA, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Sebastien</namePart><namePart type="family">Apcher</namePart><affiliation>Department of Microbiology and Immunology, Kimmel Cancer Center, Thomas Jefferson University, Philadelphia, PA, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Michael</namePart><namePart type="given">A.</namePart><namePart type="family">Miller</namePart><affiliation>Department of Microbiology and Immunology, Kimmel Cancer Center, Thomas Jefferson University, Philadelphia, PA, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Gomathinayagam</namePart><namePart type="family">Sinnathamby</namePart><affiliation>Department of Microbiology and Immunology, Kimmel Cancer Center, Thomas Jefferson University, Philadelphia, PA, USA</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>Humana Press Inc</publisher><place><placeTerm type="text">New York</placeTerm></place><dateIssued encoding="w3cdtf">2011-12-01</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: CD4+ T cells (TCD4+) are activated by peptides, generally 13–17 amino acids in length, presented at the cell surface in combination with highly polymorphic MHC class II molecules. According to the classical model, these peptides are generated by endosomal digestion of internalized antigen and loaded onto MHC class II molecules in the late endosome. Historically, this “exogenous” pathway has been defined through the extensive use of purified proteins. However, the relatively recent use of clinically relevant antigens, those of influenza virus in our case, has revealed several additional pathways of peptide production, including some that are truly “endogenous”, entailing synthesis of the protein within the infected cell. Indeed, some peptides appear to be created only via endogenous processing. The cell biology that underlies these alternative pathways remains poorly understood as do their relative contributions to defence against infectious agents and cancer, and the triggering of autoimmune diseases.</abstract><note>Current Immunology Research at Jefferson</note><subject lang="en"><genre>Keywords</genre><topic>Antigen processing</topic><topic>Antigen presentation</topic><topic>Influenza</topic><topic>Major histocompatibility class II</topic><topic>Endogenous</topic><topic>Exogenous</topic></subject><relatedItem type="host"><titleInfo><title>Immunologic Research</title></titleInfo><titleInfo type="abbreviated"><title>Immunol Res</title></titleInfo><name type="personal"><namePart type="given">Tim L</namePart><namePart type="family">Manser</namePart><role><roleTerm type="text">editor</roleTerm></role></name><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">2011-12-21</dateIssued><copyrightDate encoding="w3cdtf">2011</copyrightDate></originInfo><subject><genre>Medicine & Public Health</genre><topic>Medicine/Public Health, general</topic><topic>Immunology</topic><topic>Allergology</topic><topic>Internal Medicine</topic></subject><identifier type="ISSN">0257-277X</identifier><identifier type="eISSN">1559-0755</identifier><identifier type="JournalID">12026</identifier><identifier type="IssueArticleCount">15</identifier><identifier type="VolumeIssueCount">3</identifier><part><date>2011</date><detail type="issue"><title>Special Issue: Thomas Jefferson University</title></detail><detail type="volume"><number>51</number><caption>vol.</caption></detail><detail type="issue"><number>2-3</number><caption>no.</caption></detail><extent unit="pages"><start>237</start><end>248</end></extent></part><recordInfo><recordOrigin>Springer Science+Business Media, LLC, 2011</recordOrigin></recordInfo></relatedItem><identifier type="istex">1FF7537E0AE17E362A250E5B87DD70432A34295F</identifier><identifier type="ark">ark:/67375/VQC-FBZJ0Z86-0</identifier><identifier type="DOI">10.1007/s12026-011-8257-3</identifier><identifier type="ArticleID">8257</identifier><identifier type="ArticleID">s12026-011-8257-3</identifier><accessCondition type="use and reproduction" contentType="copyright">Springer Science+Business Media, LLC, 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>Springer Science+Business Media, LLC, 2011</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/VQC-FBZJ0Z86-0/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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