HLA-A2 molecules in an antigen-processing mutant cell contain signal sequence-derived peptides.
Identifieur interne : 004728 ( Main/Exploration ); précédent : 004727; suivant : 004729HLA-A2 molecules in an antigen-processing mutant cell contain signal sequence-derived peptides.
Auteurs : M L Wei [États-Unis] ; P. CresswellSource :
- Nature [ 0028-0836 ] ; 1992.
Descripteurs français
- KwdFr :
- Allèles, Antigène HLA-A2 (génétique), Antigènes HLA, Antigènes HLA-A (génétique), Antigènes HLA-A (isolement et purification), Antigènes HLA-B (génétique), Antigènes HLA-B (isolement et purification), Complexe majeur d'histocompatibilité, Données de séquences moléculaires, Gènes MHC de classe I, Humains, Lignée cellulaire, Membrane cellulaire (immunologie), Mutation, Séquence d'acides aminés, Transfection.
- MESH :
- génétique : Antigène HLA-A2, Antigènes HLA-A, Antigènes HLA-B.
- immunologie : Membrane cellulaire.
- isolement et purification : Antigènes HLA-A, Antigènes HLA-B.
- Allèles, Antigènes HLA, Complexe majeur d'histocompatibilité, Données de séquences moléculaires, Gènes MHC de classe I, Humains, Lignée cellulaire, Mutation, Séquence d'acides aminés, Transfection.
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
Affiliations:
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Le document en format XML
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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="KwdFr" xml:lang="fr"><term>Allèles</term><term>Antigène HLA-A2 (génétique)</term><term>Antigènes HLA</term><term>Antigènes HLA-A (génétique)</term><term>Antigènes HLA-A (isolement et purification)</term><term>Antigènes HLA-B (génétique)</term><term>Antigènes HLA-B (isolement et purification)</term><term>Complexe majeur d'histocompatibilité</term><term>Données de séquences moléculaires</term><term>Gènes MHC de classe I</term><term>Humains</term><term>Lignée cellulaire</term><term>Membrane cellulaire (immunologie)</term><term>Mutation</term><term>Séquence d'acides aminés</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="génétique" xml:lang="fr"><term>Antigène HLA-A2</term><term>Antigènes HLA-A</term><term>Antigènes HLA-B</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Membrane cellulaire</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Cell Membrane</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Antigènes HLA-A</term><term>Antigènes HLA-B</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><keywords scheme="MESH" xml:lang="fr"><term>Allèles</term><term>Antigènes HLA</term><term>Complexe majeur d'histocompatibilité</term><term>Données de séquences moléculaires</term><term>Gènes MHC de classe I</term><term>Humains</term><term>Lignée cellulaire</term><term>Mutation</term><term>Séquence d'acides aminés</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><affiliations><list><country><li>États-Unis</li></country><region><li>Caroline du Nord</li></region></list><tree><noCountry><name sortKey="Cresswell, P" sort="Cresswell, P" uniqKey="Cresswell P" first="P" last="Cresswell">P. Cresswell</name></noCountry><country name="États-Unis"><region name="Caroline du Nord"><name sortKey="Wei, M L" sort="Wei, M L" uniqKey="Wei M" first="M L" last="Wei">M L Wei</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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