Evidence of widespread binding of HLA class I molecules to peptides.
We have tested the binding of HLA class I proteins to peptides using a solid-phase binding assay. We tested 102 peptides, mostly derived from the HIV gag and HIV pol sequences. Most peptides did not bind to any class I protein tested. The pattern of binding among the three class I proteins tested, H...
Autori principali: | , , , , |
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Natura: | Journal article |
Lingua: | English |
Pubblicazione: |
1990
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_version_ | 1826297826323202048 |
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author | Frelinger, J Gotch, F Zweerink, H Wain, E Mcmichael, A |
author_facet | Frelinger, J Gotch, F Zweerink, H Wain, E Mcmichael, A |
author_sort | Frelinger, J |
collection | OXFORD |
description | We have tested the binding of HLA class I proteins to peptides using a solid-phase binding assay. We tested 102 peptides, mostly derived from the HIV gag and HIV pol sequences. Most peptides did not bind to any class I protein tested. The pattern of binding among the three class I proteins tested, HLA-A2, -B27, and -B8, was approximately 85% concordant. Further, all five of the known HIV-1 gag T cell epitopes detected by human CTL bound at least one class I protein. Binding of class I to the peptides could be detected either by directly iodinated class I proteins, or indirectly using monoclonal antibodies specific for class I. The binding to the plates could be blocked with MA2.1, which binds in the alpha 1 region of A2, but not by W6/32, which binds elsewhere. The data presented here show that binding of class I to peptides is specific, but that many peptides bind to more than a single class I protein. |
first_indexed | 2024-03-07T04:37:33Z |
format | Journal article |
id | oxford-uuid:d07af58b-e38b-4663-9739-36046b658adf |
institution | University of Oxford |
language | English |
last_indexed | 2024-03-07T04:37:33Z |
publishDate | 1990 |
record_format | dspace |
spelling | oxford-uuid:d07af58b-e38b-4663-9739-36046b658adf2022-03-27T07:50:13ZEvidence of widespread binding of HLA class I molecules to peptides.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:d07af58b-e38b-4663-9739-36046b658adfEnglishSymplectic Elements at Oxford1990Frelinger, JGotch, FZweerink, HWain, EMcmichael, AWe have tested the binding of HLA class I proteins to peptides using a solid-phase binding assay. We tested 102 peptides, mostly derived from the HIV gag and HIV pol sequences. Most peptides did not bind to any class I protein tested. The pattern of binding among the three class I proteins tested, HLA-A2, -B27, and -B8, was approximately 85% concordant. Further, all five of the known HIV-1 gag T cell epitopes detected by human CTL bound at least one class I protein. Binding of class I to the peptides could be detected either by directly iodinated class I proteins, or indirectly using monoclonal antibodies specific for class I. The binding to the plates could be blocked with MA2.1, which binds in the alpha 1 region of A2, but not by W6/32, which binds elsewhere. The data presented here show that binding of class I to peptides is specific, but that many peptides bind to more than a single class I protein. |
spellingShingle | Frelinger, J Gotch, F Zweerink, H Wain, E Mcmichael, A Evidence of widespread binding of HLA class I molecules to peptides. |
title | Evidence of widespread binding of HLA class I molecules to peptides. |
title_full | Evidence of widespread binding of HLA class I molecules to peptides. |
title_fullStr | Evidence of widespread binding of HLA class I molecules to peptides. |
title_full_unstemmed | Evidence of widespread binding of HLA class I molecules to peptides. |
title_short | Evidence of widespread binding of HLA class I molecules to peptides. |
title_sort | evidence of widespread binding of hla class i molecules to peptides |
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