Processed antigen binds to newly synthesized mhc class II molecules in antigen-specific B lymphocytes

Howard W. Davidson, Pamela A. Reid, Antonio Lanzavecchia, Colin Watts

    Research output: Contribution to journalArticlepeer-review

    186 Citations (Scopus)


    We describe the direct detection of radiolabeled antigen fragments bound to class II MHC molecules following immunoglobulin-mediated endocytosis and processing of native antigen in B lymphoblastoid cells. Tris-Tricine SDS gels revealed six distinct iodinated processing products that could be detected on class II MHC 1 hr after antigen endocytosis and persisted for at least 20 hr. These physiological processed antigen-class II complexes were remarkably stable, as judged by the fact that class II a(3 dimers, which remain associated in SDS, became labeled with the same set of processed peptides. Using a lectin-binding assay, we show that these physiological processing products bind to the newly maturing population of MHC molecules rather than binding to the preexisting cell surface population; in contrast, an exogenous peptide binds predominantly to the latter population. A direct T cell-independent assay for processed peptide-MHC complex formation should facilitate additional studies on the exogenous antigen processing pathway.

    Original languageEnglish
    Pages (from-to)105-116
    Number of pages12
    Issue number1
    Publication statusPublished - 4 Oct 1991

    ASJC Scopus subject areas

    • General Biochemistry,Genetics and Molecular Biology


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