A组链球菌纤连蛋白结合的定位与特性：使用蛋白质-金复合物的电子显微镜研究

Localization and characterization of fibronectin-binding to group A streptococci. An electron microscopic study using protein-gold-complexes.

作者信息

Wagner B, Schmidt K H, Wagner M, Wadström T

机构信息

Central Institute of Microbiology and Experimental Therapy, Academy of Sciences of the GDR, Jena.

出版信息

Zentralbl Bakteriol Mikrobiol Hyg A. 1988 Nov;269(4):479-91. doi: 10.1016/s0176-6724(88)80070-1.

DOI:10.1016/s0176-6724(88)80070-1

PMID:3066070

Abstract

The location and nature of the binding sites for fibronectin (Fn) and its N-terminal 29 K fragment (FnF) on group A streptococci were studied by electron microscopy using these proteins labelled with colloidal gold. The investigated strains exhibited a different labelling intensity as well as a different labelling pattern varying from a strong regular distribution to a weak focal binding. Binding of Fn and FnF was inhibited by itself as well as by lipoteichoic acid (LTA), anti-LTA and concanavalin A. Simultaneous labelling of the bacteria with marker complexes of FnF, human serum albumin and fibrinogen revealed separate receptor sites for each protein. Our results confirmed LTA to be mainly responsible for the binding of Fn on group A streptococci.

摘要

利用胶体金标记的纤连蛋白（Fn）及其N端29K片段（FnF），通过电子显微镜研究了A组链球菌上Fn和FnF的结合位点的位置和性质。所研究的菌株表现出不同的标记强度以及不同的标记模式，从强规则分布到弱局灶性结合不等。Fn和FnF的结合可被其自身以及脂磷壁酸（LTA）、抗LTA和伴刀豆球蛋白A抑制。用FnF、人血清白蛋白和纤维蛋白原的标记复合物同时标记细菌，揭示了每种蛋白质的独立受体位点。我们的结果证实LTA是A组链球菌上Fn结合的主要原因。