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首页> 外文期刊>The FEBS journal >The metalloprotease PrtV from Vibrio cholerae
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The metalloprotease PrtV from Vibrio cholerae

机译：霍乱弧菌的金属蛋白酶PrtV

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摘要

The Vibrio metalloprotease PrtV was purified from the culture supernatant of a Vibrio cholerae derivative that is deficient in several other secreted peptidases, including the otherwise abundant hemagglutinin/protease HapA. The PrtV is synthesized as a 102 kDa protein, but undergoes several N- and C-terminal processing steps during V. cholerae envelope translocation and prolonged incubation. Purified V. cholerae PrtV protease forms of 81 or 73 kDa were stabilized by calcium ions. Removal of calcium resulted in further rapid autoproteolysis. The two major products of autoproteolysis of the PrtV protease were approximately 37 and 18 kDa and could not be separated under non-denaturing conditions, indicating they are interacting domains. In an assay using cultured cells of the human intestinal cell line HCT8, the PrtV protein showed a cytotoxic effect leading to cell death. Using human blood plasma as a source of potential substrates of mammalian origin for the PrtV protease, we found that the extracellular matrix components fibronectin and fibrinogen were degraded by the enzyme. Additional tests with individual protein substrates revealed that plasminogen was also a possible target for the PrtV protease.
机译：从霍乱弧菌衍生物的培养上清液中纯化了弧菌金属蛋白酶PrtV，霍乱弧菌衍生物缺乏其他几种分泌的肽酶，包括原本丰富的血凝素/蛋白酶HapA。 PrtV合成为102 kDa的蛋白质，但在霍乱弧菌包膜易位和长时间孵育期间经历了多个N和C末端加工步骤。纯化的霍乱弧菌PrtV蛋白酶形式的81或73 kDa被钙离子稳定。钙的去除导致进一步快速的自蛋白水解。 PrtV蛋白酶自蛋白水解的两个主要产物分别约为37和18 kDa，在非变性条件下无法分离，表明它们是相互作用的域。在使用人类肠道细胞系HCT8的培养细胞进行的测定中，PrtV蛋白显示出细胞毒性作用，导致细胞死亡。使用人类血浆作为PrtV蛋白酶的哺乳动物来源的潜在底物的来源，我们发现该酶降解了细胞外基质成分纤连蛋白和纤维蛋白原。对单个蛋白质底物的其他测试表明，纤溶酶原也是PrtV蛋白酶的可能靶标。

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