pH-Dependent Association of Enolase and Glyceraldehyde-3-Phosphate Dehydrogenase of<i>Lactobacillus crispatus</i>with the Cell Wall and Lipoteichoic Acids

Abstract

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.