Cathepsin B cleavage of Ii from class II MHC α- and β-chains

Victor E. Reyes, Shan Lu, Robert E. Humphreys

Research output: Contribution to journalArticlepeer-review

76 Scopus citations


Class II MHC-associated invariant chain (Ii) might regulate binding of digested peptides to the Ag binding site (desetope) of class II MHC proteins by directly or allosterically blocking that site until cleavage and release of Ii from MHC α- and β-chains at the time of peptide charging. We examined the cleavage and release of Ii from class II MHC α/β/Ii trimers by cathepsin B, which has been shown by others to colocalize with class II MHC molecules in intracellular compartments and to generate antigenic peptide fragments. Cathepsin B at pH 5.0 cleaved and released Ii from class II MHC α- and β-chains. Cathepsin B digested Ii from α- and β-chains in a dose-dependent fashion, yielding 23-, 21-, and 10-kDa fragments. Blockage of cathepsin B activity with leupeptin restored the 2D(nonequilibrium pH gradient gel electrophoresis/SDS) PAGE patterns of Ii and sialic acid-derivatized forms of Ii seen without the protease. The fragmentation pattern of cathepsin D treatment was different from that of cathepsin B, yielding 25-kDa intermediates.

Original languageEnglish (US)
Pages (from-to)3877-3880
Number of pages4
JournalJournal of Immunology
Issue number11
StatePublished - Jun 1 1991
Externally publishedYes

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology


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