Recognition of HLA class II molecules by antipeptide antibodies elicited by synthetic peptides selected from regions of HLA-DP antigens Article

Chersi, A, Morganti, MC, Muratti, E et al. (1987). Recognition of HLA class II molecules by antipeptide antibodies elicited by synthetic peptides selected from regions of HLA-DP antigens . 42(11-12), 1313-1318. 10.1515/znc-1987-11-1227

cited authors

  • Chersi, A; Morganti, MC; Muratti, E; Houghten, RA

authors

abstract

  • Repeated immunizations of rabbits with chemically synthesized peptides from selected regions of HLA-DP histocompatibility antigens resulted in the production of specific antibodies that were then isolated from the immune sera by chromatography on Sepharose-peptide immunoadsorbents. The purified antibodies, when tested with an enzyme-linked immunosorbant assay, specifically bound to the inciting fragments; moreover, two of them recognized glycoproteins extracted by nonionic detergents from human chronic lymphocytic leukemia cells, as revealed by binding assays. The results suggest thatamino acid stretches 51-61 of the alpha chain and 80—90 of the beta chain of HLA-DP histocompatibility antigens are likely exposed on the surface of the protein molecule. The specific recognition of DP regions is strongly suggested by thedifference in the binding of those antibodies to soluble membrane proteins, as compared to the binding of monomorphic anti-Class II monoclonal antibodies to the same antigens. © 1987, Walter de Gruyter. All rights reserved.

publication date

  • December 1, 1987

Digital Object Identifier (DOI)

start page

  • 1313

end page

  • 1318

volume

  • 42

issue

  • 11-12