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Participation of cathepsin B in processing of antigen presentation to MHC class II
Author(s) -
Matsunaga Youichi,
Saibara Toshiji,
Kido Hiroshi,
Katunuma Nobuhiko
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80144-j
Subject(s) - antigen processing , cathepsin o , cathepsin s , cathepsin b , antigen , cathepsin a , antigen presentation , mhc class i , cathepsin h , mhc class ii , major histocompatibility complex , biology , chemistry , microbiology and biotechnology , transporter associated with antigen processing , biochemistry , immune system , immunology , enzyme , t cell
Cellular and humoral immune responses to vaccines of hepatitis B type and rabies were inhibited by specific inhibitors of cathepsin B, specific synthetic substrates of cathepsin B and anti‐cathepsin B antibody. Therefore the lysosomal cathepsin B of antigen presenting cells plays an essential role in processing of these antigens for presentation to MHC class II. One of the active sites of cathepsin B, VN 217–222 shares highly homologous sequences with a part of the desetope, a binding domain of antigenic peptides, VN 57–62 of MHC class II, β‐chain. This evidence suggests that the peptides processed by the substrate specificity of cathepsin B exhibit a common affinity to bind with the desetope of MHC class II, β‐chain.