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PMID: 2433598 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Inhibition of alloreactive cytotoxic T lymphocytes by peptides from the alpha 2 domain of HLA-A2.

Nature ·Vol. 325 ·No. 6105 ·1987-00-00 ·Pages 625-8

Parham P, Clayberger C, Zorn SL, Ludwig DS, Schoolnik GK, Krensky AM

Abstract

Class I major histocompatibility complex (MHC) molecules function in the recognition of antigens by cytotoxic T lymphocytes (CTL). Although this biological role is firmly established and much has been learnt about their structure and polymorphic variation, little is known of the regions of class I molecules that are involved in functional interactions with components of the T-cell surface. Here we show that peptides derived from residues 98-113 of the alpha 2 domain of HLA-A2 specifically inhibit the recognition of target cells by many HLA-A2-specific CTL. In addition to identifying a region that is probably involved in binding the T-cell receptor these results raise the possibility that alloreactive CTL may recognize degraded fragments of class I histocompatibility antigens.

MeSH Terms
Amino Acid Sequence Chymotrypsin/pharmacology Endopeptidase K Endopeptidases/pharmacology Epitopes/immunology HLA Antigens/analysis HLA-A2 Antigen Peptides/analysis T-Lymphocytes, Cytotoxic/immunology
Chemicals
Epitopes HLA Antigens HLA-A2 Antigen Peptides Endopeptidases Chymotrypsin Endopeptidase K
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Parham P
Clayberger C
Zorn S L
Ludwig D S
Schoolnik G K
Krensky A M
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1987-00-00
Pages
625-8
Language
English
Region
England
NLM ID
0410462
Subset
IM
Grants
NIAID NIH HHS · AI22039 · United States
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