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The tetraspanin protein CD82 associates with both free HLA class I heavy chain and heterodimeric beta 2-microglobulin

C Lagaudrière-Gesbert1, S Lebel-Binay, E Wiertz

  • 1Immunomodulation and Autoimmunity Laboratory, National Institute of Health and Medical Research, Paris, France.

Journal of Immunology (Baltimore, Md. : 1950)
|March 15, 1997
PubMed

CD82 is a tetraspan transmembrane protein on NK/LAK-susceptible targets. A single highly glycosylated protein of heterogeneous molecular mass (50-90 kDa) was immunoprecipitated by anti-CD82 from Nonidet P-40 lysates of various B cell lines, Raji, Daudi, 721, and 721.134. Using the milder detergent 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate (CHAPS), additional proteins were coprecipitated with CD82 from surface iodinated B cell lines, including a major band at 45 kDa, identified as the HLA class I heavy chain by sequential immunoprecipitations and sequential immunoprecipitation-Western blot analysis. Cocapping experiments confirmed the molecular association of CD82 and HLA class I at the cell surface of these B cell lines. CD82 could be coprecipitated with both mature and beta 2-microglobulin (beta 2m)-free heavy chains of MHC-I from CHAPS extracts. No association between MHC-I and CD82 was found in the beta 2m-deficient Daudi cell line or after co-in vitro translation of CD82, MHC heavy chain, and beta 2m mRNA. The most likely source of free class I heavy chains at the cell surface is by dissociation of beta 2m-associated class I molecules. These results suggest that association of CD82-MHC-I takes place at the cell surface and could interfere with the capacity of the MHC-I complex to protect targets from NK-mediated cytotoxicity.

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