HLA-A2 molecules in an antigen-processing mutant cell contain signal sequence-derived peptides.
Identifieur interne : 002960 ( PubMed/Corpus ); précédent : 002959; suivant : 002961HLA-A2 molecules in an antigen-processing mutant cell contain signal sequence-derived peptides.
Auteurs : M L Wei ; P. CresswellSource :
- Nature [ 0028-0836 ] ; 1992.
English descriptors
- KwdEn :
- Alleles, Amino Acid Sequence, Cell Line, Cell Membrane (immunology), Genes, MHC Class I, HLA Antigens, HLA-A Antigens (genetics), HLA-A Antigens (isolation & purification), HLA-A2 Antigen (genetics), HLA-B Antigens (genetics), HLA-B Antigens (isolation & purification), Humans, Major Histocompatibility Complex, Molecular Sequence Data, Mutation, Transfection.
- MESH :
- chemical , genetics : HLA-A Antigens, HLA-A2 Antigen, HLA-B Antigens.
- chemical , isolation & purification : HLA-A Antigens, HLA-B Antigens.
- chemical : HLA Antigens.
- immunology : Cell Membrane.
- Alleles, Amino Acid Sequence, Cell Line, Genes, MHC Class I, Humans, Major Histocompatibility Complex, Molecular Sequence Data, Mutation, Transfection.
Abstract
The mutant human cell line T2 is defective in antigen presentation in the context of class I major histocompatibility complex (MHC) molecules, and also in that transfected T2 cells show poor surface expression of exogenous human class I (HLA) alleles. Both defects are thought to lie in the transport of antigenic peptides derived from cytosolic proteins into the endoplasmic reticulum (ER), as peptide-deficient class I molecules might be expected to be either unstable or retained in the ER. The products of several mouse class I (H-2) genes, and the endogenous gene HLA-A2 do, however, reach the surface of T2 cells at reasonable levels although they are non-functional. We report here that, as expected, poorly surface-expressed HLA molecules do not significantly bind endogenous peptides. Surprisingly, H-2 molecules expressed in T2 also lack associated peptides, arguing that 'empty' complexes of mouse class I glycoproteins with human beta 2-microglobulin are neither retained in the ER nor unstable. HLA-A2 molecules, however, do bind high levels of a limited set of endogenous peptides. We have sequenced three of these peptides and find that two, a 9-mer and an 11-mer, are derived from a putative signal sequence (of IP-30, an interferon-gamma-inducible protein), whereas a third, a 13-mer, is of unknown origin. The unusual length of two of the peptides argues that the 9-mers normally associated with HLA-A2 molecules may be generated before their transport from the cytosol rather than in a pre-Golgi compartment. To our knowledge, this is the first report of the isolation of a fragment of a eukaryotic signal peptide generated in vivo.
DOI: 10.1038/356443a0
PubMed: 1557127
Links to Exploration step
pubmed:1557127Le document en format XML
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Cresswell</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1992">1992</date><idno type="RBID">pubmed:1557127</idno><idno type="pmid">1557127</idno><idno type="doi">10.1038/356443a0</idno><idno type="wicri:Area/PubMed/Corpus">002960</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002960</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">HLA-A2 molecules in an antigen-processing mutant cell contain signal sequence-derived peptides.</title><author><name sortKey="Wei, M L" sort="Wei, M L" uniqKey="Wei M" first="M L" last="Wei">M L Wei</name><affiliation><nlm:affiliation>Department of Microbiology and Immunology, Duke University Medical Center, Durham, North Carolina 27710.</nlm:affiliation></affiliation></author><author><name sortKey="Cresswell, P" sort="Cresswell, P" uniqKey="Cresswell P" first="P" last="Cresswell">P. Cresswell</name></author></analytic><series><title level="j">Nature</title><idno type="ISSN">0028-0836</idno><imprint><date when="1992" type="published">1992</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Alleles</term><term>Amino Acid Sequence</term><term>Cell Line</term><term>Cell Membrane (immunology)</term><term>Genes, MHC Class I</term><term>HLA Antigens</term><term>HLA-A Antigens (genetics)</term><term>HLA-A Antigens (isolation & purification)</term><term>HLA-A2 Antigen (genetics)</term><term>HLA-B Antigens (genetics)</term><term>HLA-B Antigens (isolation & purification)</term><term>Humans</term><term>Major Histocompatibility Complex</term><term>Molecular Sequence Data</term><term>Mutation</term><term>Transfection</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>HLA-A Antigens</term><term>HLA-A2 Antigen</term><term>HLA-B Antigens</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>HLA-A Antigens</term><term>HLA-B Antigens</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>HLA Antigens</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Cell Membrane</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Alleles</term><term>Amino Acid Sequence</term><term>Cell Line</term><term>Genes, MHC Class I</term><term>Humans</term><term>Major Histocompatibility Complex</term><term>Molecular Sequence Data</term><term>Mutation</term><term>Transfection</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The mutant human cell line T2 is defective in antigen presentation in the context of class I major histocompatibility complex (MHC) molecules, and also in that transfected T2 cells show poor surface expression of exogenous human class I (HLA) alleles. Both defects are thought to lie in the transport of antigenic peptides derived from cytosolic proteins into the endoplasmic reticulum (ER), as peptide-deficient class I molecules might be expected to be either unstable or retained in the ER. The products of several mouse class I (H-2) genes, and the endogenous gene HLA-A2 do, however, reach the surface of T2 cells at reasonable levels although they are non-functional. We report here that, as expected, poorly surface-expressed HLA molecules do not significantly bind endogenous peptides. Surprisingly, H-2 molecules expressed in T2 also lack associated peptides, arguing that 'empty' complexes of mouse class I glycoproteins with human beta 2-microglobulin are neither retained in the ER nor unstable. HLA-A2 molecules, however, do bind high levels of a limited set of endogenous peptides. We have sequenced three of these peptides and find that two, a 9-mer and an 11-mer, are derived from a putative signal sequence (of IP-30, an interferon-gamma-inducible protein), whereas a third, a 13-mer, is of unknown origin. The unusual length of two of the peptides argues that the 9-mers normally associated with HLA-A2 molecules may be generated before their transport from the cytosol rather than in a pre-Golgi compartment. To our knowledge, this is the first report of the isolation of a fragment of a eukaryotic signal peptide generated in vivo.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">1557127</PMID><DateCompleted><Year>1992</Year><Month>05</Month><Day>06</Day></DateCompleted><DateRevised><Year>2006</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0028-0836</ISSN><JournalIssue CitedMedium="Print"><Volume>356</Volume><Issue>6368</Issue><PubDate><Year>1992</Year><Month>Apr</Month><Day>02</Day></PubDate></JournalIssue><Title>Nature</Title><ISOAbbreviation>Nature</ISOAbbreviation></Journal><ArticleTitle>HLA-A2 molecules in an antigen-processing mutant cell contain signal sequence-derived peptides.</ArticleTitle><Pagination><MedlinePgn>443-6</MedlinePgn></Pagination><Abstract><AbstractText>The mutant human cell line T2 is defective in antigen presentation in the context of class I major histocompatibility complex (MHC) molecules, and also in that transfected T2 cells show poor surface expression of exogenous human class I (HLA) alleles. Both defects are thought to lie in the transport of antigenic peptides derived from cytosolic proteins into the endoplasmic reticulum (ER), as peptide-deficient class I molecules might be expected to be either unstable or retained in the ER. The products of several mouse class I (H-2) genes, and the endogenous gene HLA-A2 do, however, reach the surface of T2 cells at reasonable levels although they are non-functional. We report here that, as expected, poorly surface-expressed HLA molecules do not significantly bind endogenous peptides. Surprisingly, H-2 molecules expressed in T2 also lack associated peptides, arguing that 'empty' complexes of mouse class I glycoproteins with human beta 2-microglobulin are neither retained in the ER nor unstable. HLA-A2 molecules, however, do bind high levels of a limited set of endogenous peptides. We have sequenced three of these peptides and find that two, a 9-mer and an 11-mer, are derived from a putative signal sequence (of IP-30, an interferon-gamma-inducible protein), whereas a third, a 13-mer, is of unknown origin. The unusual length of two of the peptides argues that the 9-mers normally associated with HLA-A2 molecules may be generated before their transport from the cytosol rather than in a pre-Golgi compartment. To our knowledge, this is the first report of the isolation of a fragment of a eukaryotic signal peptide generated in vivo.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Wei</LastName><ForeName>M L</ForeName><Initials>ML</Initials><AffiliationInfo><Affiliation>Department of Microbiology and Immunology, Duke University Medical Center, Durham, North Carolina 27710.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cresswell</LastName><ForeName>P</ForeName><Initials>P</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Nature</MedlineTA><NlmUniqueID>0410462</NlmUniqueID><ISSNLinking>0028-0836</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D006680">HLA Antigens</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D015234">HLA-A Antigens</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D015789">HLA-A2 Antigen</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D015235">HLA-B Antigens</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="CommentIn"><RefSource>Nature. 1992 Jul 16;358(6383):198</RefSource><PMID Version="1">1321345</PMID></CommentsCorrections><CommentsCorrections RefType="CommentIn"><RefSource>Nature. 1992 Apr 2;356(6368):386-7</RefSource><PMID Version="1">1557115</PMID></CommentsCorrections></CommentsCorrectionsList><MeshHeadingList><MeshHeading><DescriptorName UI="D000483" MajorTopicYN="N">Alleles</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002460" MajorTopicYN="N">Cell Line</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002462" MajorTopicYN="N">Cell Membrane</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005805" MajorTopicYN="Y">Genes, MHC Class I</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006680" MajorTopicYN="Y">HLA Antigens</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015234" MajorTopicYN="N">HLA-A Antigens</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015789" MajorTopicYN="N">HLA-A2 Antigen</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015235" MajorTopicYN="N">HLA-B Antigens</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008285" MajorTopicYN="Y">Major Histocompatibility Complex</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014162" MajorTopicYN="N">Transfection</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1992</Year><Month>4</Month><Day>2</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1992</Year><Month>4</Month><Day>2</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1992</Year><Month>4</Month><Day>2</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">1557127</ArticleId><ArticleId IdType="doi">10.1038/356443a0</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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