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The Rat cim Effect: TAP Allele-Dependent Changes in a Class I MHC Anchor Motif and Evidence Against C-Terminal Trimming of Peptides in the ER

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The Rat cim Effect: TAP Allele-Dependent Changes in a Class I MHC Anchor Motif and Evidence Against C-Terminal Trimming of Peptides in the ER

Auteurs : Simon J. Powis [Royaume-Uni] ; Lesley L. Young [Royaume-Uni] ; Etienne Joly [Royaume-Uni] ; Patrick J. Barker [Royaume-Uni] ; Louise Richardson [Royaume-Uni] ; Remco P. Brandt [Pays-Bas] ; Cornelis J. Melief [Pays-Bas] ; Jonathan C. Howard [Royaume-Uni, Allemagne] ; Geoffrey W. Butcher [Royaume-Uni]

Source :

Immunity [ 1074-7613 ] ; 1996.

RBID : ISTEX:0196865F642CFDB2B72296B1999F7C8EB451E180

English descriptors

Teeft :
- Affinity matrix, Allele, Alloreactive cytotoxic, Amino, Amino acid, Amino acids, Anchor residues, Anhydrotrypsin, Antigen processing, Assay, Bind peptides, Binding buffer, Binding motif, Binding peptides, Binding pocket, Cima cells, Cimb, Cimb cells, Classical class, Edman degradation, Endogenous class, Endoplasmic reticulum, Flow cytometry, Heavy chain, Heemels, Histocompatibility, Hydrophobic residues, Joly, Kingdom biotechnology, Lysis buffer, Major histocompatibility, Molecule, Mutant, Negative charge, Other residues, Peptide, Peptide binding, Peptide binding pocket, Peptide motifs, Peptide pool, Peptide pools, Peptide residue, Peptide translocation, Peptide transporter, Ploegh, Polymorphism, Powis, Protease activity, Residue, Retention phenotype, Separate experiments, Sequencing, Signal peptide, Stabilization assay, Strong preference, Synthetic peptides, Tap2a, Tap2a cells, Tap2b, Tap2b cells, Tap2b rats, Tap2b spleens, Terminus, Transporter, Vacuum centrifugation.

Abstract

Abstract: Functional polymorphism in the rat peptide transporter associated with antigen processing (TAP) changes the peptide pool available for binding and presentation by a class I MHC allele, RT1.Aa. The peptide binding motif for RT1.Aa, determined by stabilization with synthetic peptides, included a strong preference for arginine at the peptide C terminus. Analysis of natural peptides bound to RT1.Aa by both pool sequencing and anhydrotrypsin chromatography revealed that TAP polymorphism determined the presence or absence of arginine as the peptide C-terminal residue. This result highlights the in vivo impact of TAP–peptide selectivity, and provides evidence against a high rate of generation of new C termini by protease activity in the endoplasmic reticulum.

Url:

https://api.istex.fr/ark:/67375/6H6-6S6484V6-5/fulltext.pdf

DOI: 10.1016/S1074-7613(00)80680-9

Affiliations:

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Le document en format XML

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<affiliation wicri:level="1"><country xml:lang="fr">Allemagne</country>
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<wicri:noRegion>Cologne</wicri:noRegion>
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<profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Affinity matrix</term>
<term>Allele</term>
<term>Alloreactive cytotoxic</term>
<term>Amino</term>
<term>Amino acid</term>
<term>Amino acids</term>
<term>Anchor residues</term>
<term>Anhydrotrypsin</term>
<term>Antigen processing</term>
<term>Assay</term>
<term>Bind peptides</term>
<term>Binding buffer</term>
<term>Binding motif</term>
<term>Binding peptides</term>
<term>Binding pocket</term>
<term>Cima cells</term>
<term>Cimb</term>
<term>Cimb cells</term>
<term>Classical class</term>
<term>Edman degradation</term>
<term>Endogenous class</term>
<term>Endoplasmic reticulum</term>
<term>Flow cytometry</term>
<term>Heavy chain</term>
<term>Heemels</term>
<term>Histocompatibility</term>
<term>Hydrophobic residues</term>
<term>Joly</term>
<term>Kingdom biotechnology</term>
<term>Lysis buffer</term>
<term>Major histocompatibility</term>
<term>Molecule</term>
<term>Mutant</term>
<term>Negative charge</term>
<term>Other residues</term>
<term>Peptide</term>
<term>Peptide binding</term>
<term>Peptide binding pocket</term>
<term>Peptide motifs</term>
<term>Peptide pool</term>
<term>Peptide pools</term>
<term>Peptide residue</term>
<term>Peptide translocation</term>
<term>Peptide transporter</term>
<term>Ploegh</term>
<term>Polymorphism</term>
<term>Powis</term>
<term>Protease activity</term>
<term>Residue</term>
<term>Retention phenotype</term>
<term>Separate experiments</term>
<term>Sequencing</term>
<term>Signal peptide</term>
<term>Stabilization assay</term>
<term>Strong preference</term>
<term>Synthetic peptides</term>
<term>Tap2a</term>
<term>Tap2a cells</term>
<term>Tap2b</term>
<term>Tap2b cells</term>
<term>Tap2b rats</term>
<term>Tap2b spleens</term>
<term>Terminus</term>
<term>Transporter</term>
<term>Vacuum centrifugation</term>
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<front><div type="abstract" xml:lang="en">Abstract: Functional polymorphism in the rat peptide transporter associated with antigen processing (TAP) changes the peptide pool available for binding and presentation by a class I MHC allele, RT1.Aa. The peptide binding motif for RT1.Aa, determined by stabilization with synthetic peptides, included a strong preference for arginine at the peptide C terminus. Analysis of natural peptides bound to RT1.Aa by both pool sequencing and anhydrotrypsin chromatography revealed that TAP polymorphism determined the presence or absence of arginine as the peptide C-terminal residue. This result highlights the in vivo impact of TAP–peptide selectivity, and provides evidence against a high rate of generation of new C termini by protease activity in the endoplasmic reticulum.</div>
</front>
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<affiliations><list><country><li>Allemagne</li>
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<name sortKey="Young, Lesley L" sort="Young, Lesley L" uniqKey="Young L" first="Lesley L" last="Young">Lesley L. Young</name>
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<country name="Pays-Bas"><region name="Hollande-Méridionale"><name sortKey="Brandt, Remco P" sort="Brandt, Remco P" uniqKey="Brandt R" first="Remco P" last="Brandt">Remco P. Brandt</name>
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<name sortKey="Melief, Cornelis J" sort="Melief, Cornelis J" uniqKey="Melief C" first="Cornelis J" last="Melief">Cornelis J. Melief</name>
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The Rat cim Effect: TAP Allele-Dependent Changes in a Class I MHC Anchor Motif and Evidence Against C-Terminal Trimming of Peptides in the ER

The Rat cim Effect: TAP Allele-Dependent Changes in a Class I MHC Anchor Motif and Evidence Against C-Terminal Trimming of Peptides in the ER

Source :

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

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