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

Zentralblatt für Bakteriologie, Mikrobiologie und Hygiene. Series A: Medical Microbiology, Infectious Diseases, Virology, Parasitology Pub Date : 1988-11-01 DOI:10.1016/S0176-6724(88)80070-1

Barbara Wagner , Karl-Hermann Schmidt , Manfred Wagner , Torkel Wadström

{"title":"Localization and characterization of fibronectin-binding to group A streptococci an electron microscopic study using protein-gold-complexes","authors":"Barbara Wagner , Karl-Hermann Schmidt , Manfred Wagner , Torkel Wadström","doi":"10.1016/S0176-6724(88)80070-1","DOIUrl":null,"url":null,"abstract":"<div><p>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.</p></div>","PeriodicalId":101291,"journal":{"name":"Zentralblatt für Bakteriologie, Mikrobiologie und Hygiene. Series A: Medical Microbiology, Infectious Diseases, Virology, Parasitology","volume":"269 4","pages":"Pages 479-491"},"PeriodicalIF":0.0000,"publicationDate":"1988-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0176-6724(88)80070-1","citationCount":"7","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Zentralblatt für Bakteriologie, Mikrobiologie und Hygiene. Series A: Medical Microbiology, Infectious Diseases, Virology, Parasitology","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0176672488800701","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}

引用次数: 7

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.

查看原文

微信好友朋友圈 QQ好友复制链接

本刊更多论文

A群链球菌纤维连接蛋白结合的定位和表征——用蛋白-金配合物的电镜研究

用胶体金标记A组链球菌纤维连接蛋白(Fn)及其n端29k片段(FnF)结合位点的位置和性质进行了电镜研究。所研究的菌株表现出不同的标记强度和不同的标记模式，从强规则分布到弱焦点结合。Fn和FnF的结合既被自身抑制，也被脂质胆酸(LTA)、抗LTA和刀豆蛋白a抑制。同时用FnF、人血清白蛋白和纤维蛋白原标记复合物标记细菌，发现每种蛋白的受体位点不同。我们的结果证实LTA主要负责Fn与A群链球菌的结合。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

求助全文

约1分钟内获得全文去求助

来源期刊

Zentralblatt für Bakteriologie, Mikrobiologie und Hygiene. Series A: Medical Microbiology, Infectious Diseases, Virology, Parasitology

自引率

0.00%

发文量