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Specificity of human cathepsin S determined by processing of peptide substrates and MHC class II-associated invariant chain

机译：人类组织蛋白酶S的特异性由肽底物和与MHC II类相关的恒定链的加工确定

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摘要

Cathepsin S (CatS) is a lysosomal cysteine protease of the papain family, the members of which possess relatively broad substrate specificities. It has distinct roles in major histocompatibility complex (MHC) class II-associated peptide loading and in antigen processing in both the MHC class I and class II pathways. It may therefore represent a target for interference with antigen presentation, which could be of value in the therapy of (auto) immune diseases. To obtain more detailed information on the specificity of CatS, we mapped its cleavage site preferences at subsites S3-S1' by in vitro processing of a peptide library. Only five amino acid residues at the substrate's P2 position allowed for cleavage by CatS under time-limited conditions. Preferences for groups of amino acid residues were also observed at positions P3, P1 and P1'. Based on these results, we developed highly CatS-sensitive peptides. After processing of MHC class II-associated invariant chain (Ii), a natural protein substrate of CatS, we identified CatS cleavage sites in Ii of which a majority matched the amino acid residue preference data obtained with peptides. These observed cleavage sites in Ii might be of relevance for its in vivo processing by CatS.
机译：组织蛋白酶S（CatS）是木瓜蛋白酶家族的溶酶体半胱氨酸蛋白酶，其成员具有相对广泛的底物特异性。它在主要组织相容性复合体（MHC）II类相关肽负载以及在MHC I类和II类途径中的抗原加工中均具有独特的作用。因此，它可以代表干扰抗原呈递的靶标，这在（自身）免疫疾病的治疗中可能是有价值的。为了获得有关CatS特异性的更多详细信息，我们通过体外处理肽库将其切割位点的偏好性定位在亚位点S3-S1'。在限时条件下，CatS只能切割底物P2位的五个氨基酸残基。在位置P3，P1和P1'处也观察到氨基酸残基组的偏好。基于这些结果，我们开发了高度对CatS敏感的肽。经过处理MHC II类相关的恒定链（Ii），是CatS的天然蛋白质底物，我们鉴定了Cati的切割位点，其中大部分与用肽获得的氨基酸残基偏好数据相匹配。这些在Ii中观察到的切割位点可能与其在CatS体内加工有关。

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