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葡萄球菌肠毒素微生物超抗原。

Staphylococcal enterotoxin microbial superantigens.

作者信息

Johnson H M, Russell J K, Pontzer C H

机构信息

Department of Microbiology and Cell Science, University of Florida, Gainesville 32611.

出版信息

FASEB J. 1991 Sep;5(12):2706-12. doi: 10.1096/fasebj.5.12.1916093.

DOI:10.1096/fasebj.5.12.1916093
PMID:1916093
Abstract

Staphylococcal enterotoxins are a family of structurally related proteins that are produced by Staphylococcus aureus. In addition to their role in the pathogenicity of food poisoning, these microbial superantigens have profound effects on the immune system, which makes them useful tools for understanding its mechanism of action. These molecules (24-30 kDa) are highly hydrophilic and exhibit low alpha helix and high beta pleated sheet content, suggesting a flexible, accessible structure. Staphylococcal enterotoxins are among the most potent activators of T lymphocytes known. The receptors for staphylococcal enterotoxins on antigen-presenting cells are major histocompatibility complex (MHC) class II molecules. Further, the alpha-helical regions of the class II molecule are essential for function and appear to interact directly with the NH2-terminal region of staphylococcal enterotoxins such as SEA. Recent studies have shown that a complex of staphylococcal enterotoxin and MHC class II molecules is required for binding to the V beta region of the T cell antigen receptor. Staphylococcal enterotoxin mitogenic activity is dependent on induction of interleukin 2, which may be intimately involved in the mechanism of toxicity. The mouse minor lymphocyte stimulating (M1s) "endogenous" self-superantigen has been shown to be a retroviral gene product, so this too is apparently a microbial superantigen. An understanding of the mechanisms of action of these microbial superantigens has implications for normal and pathological immune functions.

摘要

葡萄球菌肠毒素是由金黄色葡萄球菌产生的一族结构相关的蛋白质。除了在食物中毒的致病性中发挥作用外,这些微生物超抗原对免疫系统有深远影响,这使其成为理解免疫系统作用机制的有用工具。这些分子(24 - 30 kDa)具有高度亲水性,α螺旋含量低,β折叠含量高,表明其结构灵活且易于接近。葡萄球菌肠毒素是已知的最有效的T淋巴细胞激活剂之一。抗原呈递细胞上葡萄球菌肠毒素的受体是主要组织相容性复合体(MHC)II类分子。此外,II类分子的α螺旋区域对其功能至关重要,并且似乎直接与葡萄球菌肠毒素(如SEA)的NH2末端区域相互作用。最近的研究表明,葡萄球菌肠毒素与MHC II类分子的复合物是与T细胞抗原受体的Vβ区域结合所必需的。葡萄球菌肠毒素的促有丝分裂活性依赖于白细胞介素2的诱导,白细胞介素2可能密切参与毒性机制。小鼠次要淋巴细胞刺激(M1s)“内源性”自身超抗原已被证明是一种逆转录病毒基因产物,所以这显然也是一种微生物超抗原。了解这些微生物超抗原的作用机制对正常和病理免疫功能都有重要意义。

相似文献

1
Staphylococcal enterotoxin microbial superantigens.葡萄球菌肠毒素微生物超抗原。
FASEB J. 1991 Sep;5(12):2706-12. doi: 10.1096/fasebj.5.12.1916093.
2
Staphylococcal enterotoxin superantigens.葡萄球菌肠毒素超抗原
Proc Soc Exp Biol Med. 1991 Dec;198(3):765-71. doi: 10.3181/00379727-198-43321a.
3
Crystal structure of microbial superantigen staphylococcal enterotoxin B at 1.5 A resolution: implications for superantigen recognition by MHC class II molecules and T-cell receptors.分辨率为1.5埃的微生物超抗原葡萄球菌肠毒素B的晶体结构:对MHC II类分子和T细胞受体识别超抗原的影响
J Mol Biol. 1998 Mar 20;277(1):61-79. doi: 10.1006/jmbi.1997.1577.
4
The crystal structure of staphylococcal enterotoxin H: implications for binding properties to MHC class II and TcR molecules.葡萄球菌肠毒素H的晶体结构:对其与II类主要组织相容性复合体及T细胞受体分子结合特性的影响
J Mol Biol. 2000 Sep 22;302(3):527-37. doi: 10.1006/jmbi.2000.4093.
5
Immunopharmacology of the superantigen staphylococcal enterotoxin A in T-cell receptor V beta 3 transgenic mice.超抗原金黄色葡萄球菌肠毒素A在T细胞受体Vβ3转基因小鼠中的免疫药理学
Immunology. 1993 Aug;79(4):520-7.
6
Superantigenic staphylococcal exotoxins induce T-cell proliferation in the presence of Langerhans cells or class II-bearing keratinocytes and stimulate keratinocytes to produce T-cell-activating cytokines.超抗原性葡萄球菌外毒素在朗格汉斯细胞或表达II类分子的角质形成细胞存在的情况下诱导T细胞增殖,并刺激角质形成细胞产生T细胞激活细胞因子。
J Invest Dermatol. 1994 Jan;102(1):31-8. doi: 10.1111/1523-1747.ep12371727.
7
Superantigens: interaction of staphylococcal enterotoxins with MHC class II molecules.超抗原:葡萄球菌肠毒素与II类主要组织相容性复合体分子的相互作用
Trans Am Clin Climatol Assoc. 1990;101:195-204; discussion 204-6.
8
Structural basis for differential binding of staphylococcal enterotoxin A and toxic shock syndrome toxin 1 to class II major histocompatibility molecules.葡萄球菌肠毒素A和中毒性休克综合征毒素1与II类主要组织相容性分子差异结合的结构基础。
Proc Natl Acad Sci U S A. 1991 Jan 1;88(1):125-8. doi: 10.1073/pnas.88.1.125.
9
Enterotoxin residues determining T-cell receptor V beta binding specificity.决定T细胞受体Vβ结合特异性的肠毒素残基。
Nature. 1992 Oct 29;359(6398):841-3. doi: 10.1038/359841a0.
10
Structural basis of superantigen action inferred from crystal structure of toxic-shock syndrome toxin-1.从中毒性休克综合征毒素-1晶体结构推断超抗原作用的结构基础。
Nature. 1994 Jan 6;367(6458):94-7. doi: 10.1038/367094a0.

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