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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Cell Wall / enzymology*
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Glyceraldehyde 3-Phosphate
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Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating) / metabolism*
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Hydrogen-Ion Concentration
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Lactobacillus / enzymology*
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Lipopolysaccharides / metabolism
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Phosphopyruvate Hydratase / metabolism*
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Plasminogen / metabolism
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Protein Binding
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Protein Biosynthesis
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Teichoic Acids / metabolism
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Transcription, Genetic
Substances
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Lipopolysaccharides
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Teichoic Acids
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Glyceraldehyde 3-Phosphate
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lipoteichoic acid
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Plasminogen
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Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)
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Phosphopyruvate Hydratase