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致泻性大肠杆菌的细凝聚性菌毛

Thin aggregative fimbriae from diarrheagenic Escherichia coli.

作者信息

Collinson S K, Emödy L, Trust T J, Kay W W

机构信息

Department of Biochemistry and Microbiology, University of Victoria, British Columbia.

出版信息

J Bacteriol. 1992 Jul;174(13):4490-5. doi: 10.1128/jb.174.13.4490-4495.1992.

Abstract

Four strains of diarrheagenic Escherichia coli originally isolated from distinct geographic regions were found to produce unusual thin aggregative fimbriae requiring depolymerization in formic acid prior to analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Immunoelectron microscopy of native fimbriae and Western blot (immunoblot) analysis of the corresponding 18-kDa fimbrins showed that these E. coli fimbriae were serologically cross-reactive with SEF 17 (Salmonella enteritidis fimbriae with a fimbrin molecular mass of 17 kDa). The E. coli and S. enteritidis fimbrins had similar total amino acid compositions and highly conserved N-terminal amino acid sequences. These results indicate that E. coli and S. enteritidis produce biochemically related, aggregative fimbriae which constitute a new type of intergenerically distributed fimbriae for which we propose the descriptive name GVVPQ fimbriae on the basis of the conserved N-terminal amino acid sequence.

摘要

从不同地理区域最初分离出的四株致泻性大肠杆菌被发现能产生异常纤细的凝聚性菌毛,在通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳进行分析之前,需要在甲酸中解聚。对天然菌毛的免疫电子显微镜检查以及对相应18 kDa菌毛蛋白的蛋白质印迹(免疫印迹)分析表明,这些大肠杆菌菌毛与SEF 17(菌毛蛋白分子量为17 kDa的肠炎沙门氏菌菌毛)存在血清学交叉反应。大肠杆菌和肠炎沙门氏菌的菌毛蛋白具有相似的总氨基酸组成和高度保守的N端氨基酸序列。这些结果表明,大肠杆菌和肠炎沙门氏菌产生了生物化学相关的凝聚性菌毛,它们构成了一种新型的跨属分布菌毛,基于保守的N端氨基酸序列,我们提议将其描述性命名为GVVPQ菌毛。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d895/206236/b6c64de7ee9d/jbacter00079-0314-a.jpg

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