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化脓性链球菌M+和M-变体对纤维蛋白原摄取的定量特征。

Quantitative character of fibrinogen uptake by M+ and M- variants of Streptococcus pyogenes.

作者信息

Havlícek J, Pokorný J, Havlícková H

机构信息

Institute of Hygiene and Epidemiology, Prague, Czechoslovakia.

出版信息

Zentralbl Bakteriol Mikrobiol Hyg A. 1987 Jun;265(1-2):1-11. doi: 10.1016/s0176-6724(87)80147-5.

DOI:10.1016/s0176-6724(87)80147-5
PMID:3314253
Abstract

Fibrinogen was labelled with 125Iodine by mild chemical oxidation and its binding to Streptococcus pyogenes was subjected to quantitative analysis, inhibition and desorption studies. Fibrinogen was bound both by virulent and avirulent (M protein-positive and M protein-negative) matched strains of several serotypes. In all pairs of strains fibrinogen uptake was much higher by the M-positive variants. The ratio of bound fibrinogen to total fibrinogen was highly dependent both on the concentration of fibrinogen and the concentration of cocci. Equilibrium binding studies showed that the binding was a multifactorial process. Probably not only receptor fibrinogen interactions but also interactions between bound and unbound fibrinogen molecules took place. The uptake of fibrinogen was highly depressed in avirulent strains and practically uninfluenced in virulent strains by the presence of albumin or immunoglobulin. The bond between fibrinogen and streptococci is therefore different in virulent and avirulent variants. The fibrinogen receptors on the cell surface are specific.

摘要

通过温和化学氧化法用125碘标记纤维蛋白原,并对其与化脓性链球菌的结合进行定量分析、抑制和脱附研究。几种血清型的有毒和无毒(M蛋白阳性和M蛋白阴性)匹配菌株均能结合纤维蛋白原。在所有菌株对中,M阳性变体摄取的纤维蛋白原要多得多。结合的纤维蛋白原与总纤维蛋白原的比例高度依赖于纤维蛋白原的浓度和球菌的浓度。平衡结合研究表明,这种结合是一个多因素过程。可能不仅发生了受体与纤维蛋白原的相互作用,还发生了结合与未结合的纤维蛋白原分子之间的相互作用。白蛋白或免疫球蛋白的存在使无毒菌株中纤维蛋白原的摄取高度降低,而对有毒菌株几乎没有影响。因此,纤维蛋白原与链球菌之间的结合在有毒和无毒变体中是不同的。细胞表面的纤维蛋白原受体具有特异性。

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引用本文的文献

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Infect Immun. 1999 Sep;67(9):4326-33. doi: 10.1128/IAI.67.9.4326-4333.1999.
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Ultrastructural localization of the fibrinogen-binding domain of streptococcal M protein.链球菌M蛋白纤维蛋白原结合结构域的超微结构定位
Infect Immun. 1989 Aug;57(8):2397-404. doi: 10.1128/iai.57.8.2397-2404.1989.