Open AccesspH-Dependent Association of Enolase and Glyceraldehyde-3-Phosphate Dehydrogenase of Lactobacillus crispatus with the Cell Wall and Lipoteichoic Acids
Author(s) -
Jenni Antikainen,
Veera Kuparinen,
Kaarina Lähteenmäki,
Timo Korhonen
Publication year - 2007
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.00378-07
Subject(s) - lipoteichoic acid , biology , lactobacillus crispatus , biochemistry , enolase , isoelectric point , glyceraldehyde , teichoic acid , glyceraldehyde 3 phosphate dehydrogenase , dehydrogenase , cell wall , lactobacillus , enzyme , bacteria , peptidoglycan , immunohistochemistry , fermentation , immunology , genetics , staphylococcus aureus
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.