pH-dependent association of enolase and glyceraldehyde-3-phosphate dehydrogenase of Lactobacillus crispatus with the cell wall and lipoteichoic acids

被引：109

作者：

Antikainen, Jenni ^{[1
]}

Kupannen, Veera ^{[1
]}

Lahteenmaki, Kaarina ^{[1
]}

Korhonen, Timo K. ^{[1
]}

机构：

[1] Univ Helsinki, Fac Biosci, FIN-00014 Helsinki, Finland

来源：

JOURNAL OF BACTERIOLOGY | 2007年 / 189卷 / 12期

关键词：

D O I：

10.1128/JB.00378-07

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

The plasminogen-binding proteins enolase and glyceraldehyde-3-phosphate dehydrogenase of Lactobacillus crispatus were localized on the cell surface at pH 5 but released into the medium at an alkaline pH. These proteins bound to lipoteichoic acids at a pH below their isoelectric point. The results indicate that lactobacilli rapidly modify their surface properties in response to changes in pH.

引用

页码：4539 / 4543

页数：5

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