Enolases from Gram-positive bacterial pathogens and commensal lactobacilli share functional similarity in virulence-associated traits

被引：103

作者：

Antikainen, Jenni ^{[1
]}

Kuparinen, Veera ^{[1
]}

Laehteenmaeki, Kaarina ^{[1
]}

Korhonen, Timo K. ^{[1
]}

机构：

[1] Univ Helsinki, Fac Biosci, Helsinki, Finland

来源：

FEMS IMMUNOLOGY AND MEDICAL MICROBIOLOGY | 2007年 / 51卷 / 03期

关键词：

enolase; lactobacilli; streptococci; laminin; plasminogen;

D O I：

10.1111/j.1574-695X.2007.00330.x

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

Enolase occurs as a cytoplasmic and a surface-associated protein in bacteria. Enolases of the bacterial pathogens Streptococcus pyogenes, Streptococcus pneumoniae and Staphylococcus aureus, as well as of the commensal lactic acid bacteria, Lactobacillus crispatus and Lactobacillus johnsonii, were purified as His(6)-fusion proteins from recombinant Escherichia coli. The fusion proteins were compared for putative virulence-associated functions, i.e., binding of human plasminogen, enhancement of plasminogen activation by human plasminogen activators, as well as binding to immobilized laminin, fibronectin and collagens. The individual enolases showed varying efficiencies in these functions. In particular, highly and equally effective interactions with plasminogen and laminin were seen with lactobacillar and staphylococcal enolases.

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收藏

页码：526 / 534

页数：9

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