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葡萄球菌肠毒素B功能活性片段的鉴定

Identification of functionally active fragments of staphylococcal enterotoxin B.

作者信息

Kolosov M I, Maurer-Fogy I, Sveshnikov P G, Pozdnyakova L P, Shemchukova O B, Severin E S

机构信息

Research Center of Molecular Diagnostics and Therapy, Moscow, Russia.

出版信息

Eur J Biochem. 1992 Nov 1;209(3):823-8. doi: 10.1111/j.1432-1033.1992.tb17353.x.

Abstract

It has been found that staphylococcal enterotoxin B contains a proteolysis-sensitive sequence in the cysteine loop formed by two half-cystines located in the middle of the toxin polypeptide chain. Fragments of the enterotoxin formed as a result of its digestion in this region have been isolated, their N-terminal sequences have been determined and sites of proteolysis have been identified. It has been demonstrated that the N-terminal fragment of staphylococcal enterotoxin B is capable of activating T cell proliferation in the culture of human mononuclear cells practically to the same degree as the intact enterotoxin. The toxin's C-terminal fragment possesses an ability to activate calmodulin-dependent enzymes and is probably the toxicogenic part of the enterotoxin.

摘要

已发现葡萄球菌肠毒素B在毒素多肽链中部由两个半胱氨酸形成的半胱氨酸环中含有一个对蛋白水解敏感的序列。已分离出由于该区域消化而形成的肠毒素片段,测定了它们的N端序列,并确定了蛋白水解位点。已证明葡萄球菌肠毒素B的N端片段在人单核细胞培养物中激活T细胞增殖的能力几乎与完整肠毒素相同。毒素的C端片段具有激活钙调蛋白依赖性酶的能力,可能是肠毒素的毒性部分。

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