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Journal of Bacteriology, October 2000, p. 5919-5921, Vol. 182, No. 20
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

The Streptococcus pneumoniae Beta-Galactosidase Is a Surface Protein

Dorothea Zähner and Regine Hakenbeck*

Department of Microbiology, University of Kaiserslautern, D-67663 Kaiserslautern, Germany

Received 30 May 2000/Accepted 19 July 2000

The beta -galactosidase gene of Streptococcus pneumoniae, bgaA, encodes a putative 2,235-amino-acid protein with the two amino acid motifs characteristic of the glycosyl hydrolase family of proteins. In addition, an N-terminal signal sequence and a C-terminal LPXTG motif typical of surface-associated proteins of gram-positive bacteria are present. Trypsin treatment of cells resulted in solubilization of the enzyme, documenting that it is associated with the cell envelope. In order to obtain defined mutants suitable for lacZ reporter experiments, the bgaA gene was disrupted, resulting in a complete absence of endogenous beta -galactosidase activity. The results are consistent with beta -galactosidase being a surface protein that seems not to be involved in lactose metabolism but that may play a role during pathogenesis.

* Corresponding author. Mailing address: Department of Microbiology, University of Kaiserslautern, Paul Ehrlich Strasse, D-67663 Kaiserslautern, Germany. Phone: 49-631-205-2353. Fax: 49-631-205-3799. E-mail: hakenb{at}rhrk.uni-kl.de.

Journal of Bacteriology, October 2000, p. 5919-5921, Vol. 182, No. 20
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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