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Journal of Bacteriology, June 2007, p. 4539-4543, Vol. 189, No. 12
0021-9193/07/$08.00+0     doi:10.1128/JB.00378-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

pH-Dependent Association of Enolase and Glyceraldehyde-3-Phosphate Dehydrogenase of Lactobacillus crispatus with the Cell Wall and Lipoteichoic Acids{triangledown}

Jenni Antikainen, Veera Kupannen, Kaarina Lähteenmäki, and Timo K. Korhonen*

General Microbiology, Faculty of Biosciences, P.O. Box 56, FIN-00014 University of Helsinki, Finland

Received 14 March 2007/ Accepted 5 April 2007

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.

* Corresponding author. Mailing address: General Microbiology, Faculty of Biosciences, P.O. Box 56, FIN-00014 University of Helsinki, Finland. Phone: 358-9-19159250. Fax: 358-9-19159262. E-mail: timo.korhonen{at}helsinki.fi

{triangledown} Published ahead of print on 20 April 2007.

Journal of Bacteriology, June 2007, p. 4539-4543, Vol. 189, No. 12
0021-9193/07/$08.00+0     doi:10.1128/JB.00378-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



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