The existence of two completely distinct antigenic sites within a decapeptide.

Abstract:

:A decapeptide (1182-1191) derived from the bovine interphotoreceptor retinoid-binding protein (IRBP) was found to contain two completely distinct antigenic sites when tested in Lewis rats. One site, localized in sequence 1182-1191, is the core of the immunodominant and highly uveitogenic determinant of IRBP. The second site localizes within sequence 1183-1191 and becomes detectable only when tryptophan at position 1182 is deleted. Lymphocytes sensitized against the first, larger site recognized all longer peptides within sequence 1169-1191, as well as whole IRBP. In contrast, lymphocytes sensitized against the second, short epitope recognized only two peptides, 1184-1191 and (to a lesser degree) 1183-1191. The responses to both sites were restricted by the same major histocompatibility complex (MHC) product (I-A), as shown by monoclonal antibody blocking and by the finding that the lymphocyte response to 1184-1191 was competitively inhibited by peptide 1181-1191. The unique finding of two completely distinct antigenic sites within a decapeptide could be explained by the hypothesis that peptides of the two sites combine with the MHC molecule on antigen-presenting cells by different configurations, thus forming two distinct antigenicities.

journal_name

Cell Immunol

journal_title

Cellular immunology

authors

Kotake S,Sasamoto Y,Kawano Y,Sanui H,Wiggert B,Chader GJ,Gery I

doi

10.1016/0008-8749(92)90181-n

subject

Has Abstract

pub_date

1992-03-01 00:00:00

pages

123-9

issue

1

eissn

0008-8749

issn

1090-2163

pii

0008-8749(92)90181-N

journal_volume

140

pub_type

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