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关节炎支原体超抗原MAM:一种活性肽的纯化与鉴定

The Mycoplasma arthritidis superantigen MAM: purification and identification of an active peptide.

作者信息

Atkin C L, Wei S, Cole B C

机构信息

Department of Internal Medicine, University of Utah School of Medicine, Salt Lake City 84132.

出版信息

Infect Immun. 1994 Dec;62(12):5367-75. doi: 10.1128/iai.62.12.5367-5375.1994.

Abstract

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. Pure 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 MAM15-31-C, synthesized according to the Edman sequence, blocked mitogenicity of MAM and supported assignment of the amino acid sequence.

摘要

典型的超抗原MAM是由关节炎支原体产生的一种细胞外T细胞丝裂原,该支原体可导致啮齿动物的慢性增殖性关节炎。我们在此描述了将MAM纯化至同质的过程。纯MAM展现出了先前针对部分纯化的MAM所描述的所有主要特性,包括在呈递给T细胞时对H-2E分子的偏好、T细胞受体Vβ对T细胞激活的特异性,以及在体内对T细胞功能的抑制,但通过超抗原桥介导可增强B细胞活性。对纯MAM进行的埃德曼降解得到了一个54个残基的部分氨基末端序列。根据埃德曼序列合成的寡肽MAM15-31-C阻断了MAM的促有丝分裂活性,并支持了氨基酸序列的确定。

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