Identification of heat shock proteins binding to an immunodominant uveitopathogenic peptide of IRBP.

Abstract:

:Intracellular binding proteins have been identified and isolated from B cells by their ability to bind to the synthetic peptide (1169-1191), the major immunodominant epitope of bovine interphotoreceptor retinoid-binding protein (IRBP) coupled to cyanogen bromide activated Sepharose 4B. After SDS-PAGE, two discrete protein bands of approximately 72 and 74 kDa, were found to be present in B cells of naive Lewis rats as well as in EBV transformed B cells from a human patient with ocular Behçet's disease. Enhanced expression of these peptide-binding proteins was achieved by incubating the cells with Lipopolysaccharide (LPS) from S. typhimurium. The approximately 72 and 74 kDa peptide-binding proteins reacted in western blot with monoclonal antibodies specific for both constitutively expressed and inducible 72/74 kDa hsp 70 proteins. The demonstration that these proteins bind to the immunodominant epitope of IRBP indicates that they may play a role in the processing and presentation of antigens by antigen-presenting cell (APC).

journal_name

Curr Eye Res

journal_title

Current eye research

authors

Rengarajan K,de Smet MD,Chader GJ,Wiggert B

doi

10.3109/02713689408995790

subject

Has Abstract

pub_date

1994-04-01 00:00:00

pages

289-96

issue

4

eissn

0271-3683

issn

1460-2202

journal_volume

13

pub_type

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