THE MYCOPLASMA-ARTHRITIDIS SUPERANTIGEN MAM - PURIFICATION AND IDENTIFICATION OF AN ACTIVE PEPTIDE
THE MYCOPLASMA-ARTHRITIDIS SUPERANTIGEN MAM - PURIFICATION AND IDENTIFICATION OF AN ACTIVE PEPTIDE
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DOI：
10.1128/iai.62.12.5367-5375.1994
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发表时间：
1994-12-01
影响因子：
3.1
通讯作者：
COLE, BC
中科院分区：
文献类型：
--
作者：
ATKIN, CL;WEI, SH;COLE, BC
超抗原MAM是由引起啮齿类动物慢性增生性关节炎的关节炎支原体（Mycoplasma arthritis）产生的细胞外T细胞有丝分裂原。mire MAM表现出先前描述的部分纯化的MAM的所有主要性质，包括在呈递给T细胞时对H-2E分子的偏好、对T细胞活化的V-β T细胞受体特异性、以及在体内抑制T细胞功能但增强B细胞活性（如由超抗原桥介导的）。纯MAM的Edman降解得到54个残基的部分氨基末端序列。根据Edman序列合成的寡肽MAM（15 - 31）-C阻断MAM的促有丝分裂性并支持氨基酸序列的分配。
The prototypical superantigen MAM is an extracellular T-cell mitogen produced by Mycoplasma arthritidis, an organism which causes chronic proliferative arthritis of rodents, We here describe purification of MAM to homogeneity. mire MAM exhibits all of the major properties previously described for partially purified MAM, including preference for H-2E molecules in presention to T cells, V-beta T-cell receptor specificity for T-cell activation, and in vivo inhibition of T-cell functions but enhancement of B-cell activity as mediated by the superantigen bridge. Edman degradation of pure MAM gave a 54-residue partial amino-terminal sequence. The oligopeptide MAM(15-31)-C, synthesized according to the Edman sequence, blocked mitogenicity of MAM and supported assignment of the amino acid sequence.