Matsunaga Y, Saibara T, Kido H, Katunuma N
Department of The Third Internal Medicine, School of Medicine, University of Tokushima, Japan.
FEBS Lett. 1993 Jun 21;324(3):325-30. doi: 10.1016/0014-5793(93)80144-j.
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, VN217-222 shares highly homologous sequences with a part of the desetope, a binding domain of antigenic peptides, VN57-62 of MHC class II, beta-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, beta-chain.
组织蛋白酶B的特异性抑制剂、组织蛋白酶B的特异性合成底物和抗组织蛋白酶B抗体可抑制针对乙型肝炎和狂犬病疫苗的细胞免疫和体液免疫反应。因此，抗原呈递细胞的溶酶体组织蛋白酶B在处理这些抗原以呈递给MHC II类分子的过程中起重要作用。组织蛋白酶B的一个活性位点VN217 - 222与MHC II类分子β链的desetope（抗原肽结合域VN57 - 62）的一部分具有高度同源序列。这一证据表明，由组织蛋白酶B的底物特异性加工的肽对与MHC II类分子β链的desetope结合表现出共同亲和力。
