pH-dependent association of enolase and glyceraldehyde-3-phosphate dehydrogenase of Lactobacillus crispatus with the cell wall and lipoteichoic acids.
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.
Antikainen
Jenni
J
General Microbiology, Faculty of Biosciences, P.O. Box 56, FIN-00014 University of Helsinki, Finland.
Kuparinen
Veera
V
Kupannen
Veera
V
Lähteenmäki
Kaarina
K
Korhonen
Timo K
TK
D002473:Cell Wall / Q000201:enzymology*; D005986:Glyceraldehyde 3-Phosphate; D024581:Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating) / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007778:Lactobacillus / Q000201:enzymology*; D008070:Lipopolysaccharides / Q000378:metabolism; D010751:Phosphopyruvate Hydratase / Q000378:metabolism*; D010958:Plasminogen / Q000378:metabolism; D011485:Protein Binding; D014176:Protein Biosynthesis; D013682:Teichoic Acids / Q000378:metabolism; D014158:Transcription, Genetic
D008070:Lipopolysaccharides; D013682:Teichoic Acids; D005986:Glyceraldehyde 3-Phosphate; C009900:lipoteichoic acid; D010958:Plasminogen; D024581:Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating); D010751:Phosphopyruvate Hydratase