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Serological and structural analysis of HLA class I molecules: beta 2-microglobulin interacts with the two external domains of the HLA class I heavy chain.

Authors
  • Ferrier, P
  • Kahn-Perles, B
  • Layet, C
  • Pontarotti, P
  • Sire, J
  • Hakem, R
  • Le Bouteiller, P
  • Toubert, A
  • Perarnau, B
  • Roudier, J
Type
Published Article
Journal
Annales de l'Institut Pasteur. Immunology
Publication Date
Jan 01, 1987
Volume
138
Issue
1
Pages
19–35
Identifiers
PMID: 2437937
Source
Medline
License
Unknown

Abstract

The serological reactivities of HLA class I molecules were studied in relation to structural modifications of these molecules, including shuffling of external exons and exchange of human beta 2-microglobulin for beta 2-microglobulin from different species. Two major clusters (I and II) of monomorphic and polymorphic antigenic determinants could be delineated. beta 2-Microglobulin participates in the formation of the two clusters, indicating that the light chain interacts tightly with the two external domains of the HLA class I heavy chain. However, external molecules can modify these interactions and alter the antigenic structure of the overall molecule. Thus, fixation on HLA class I molecules of the Fab fragment of a monoclonal antibody directed at antigenic determinants associated with cluster II resulted in enhanced fixation of a monoclonal antibody (B10.6) related to cluster I. The structural and functional implications of these results are discussed.

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