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Journal of Bacteriology, July 2007, p. 5183-5192, Vol. 189, No. 14
0021-9193/07/$08.00+0     doi:10.1128/JB.00449-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

CcpA-Dependent and -Independent Control of Beta-Galactosidase Expression in Streptococcus pneumoniae Occurs via Regulation of an Upstream Phosphotransferase System-Encoding Operon{triangledown}

Greer E. Kaufman and Janet Yother*

Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama 35294

Received 26 March 2007/ Accepted 1 May 2007

A spontaneous mutant of Streptococcus pneumoniae strain D39 exhibiting elevated ß-galactosidase activity was identified. We determined that the ß-galactosidase activity was due to BgaA, a surface protein in S. pneumoniae, and that the expression of bgaA was regulated. Transcription analyses demonstrated expression of bgaA in the constitutive ß-galactosidase (BgaAC) mutant, but not in the parent. ß-Galactosidase expression was induced in the parent under specific growth conditions; however, the levels did not reach those of the BgaAC mutant. We localized the mutation resulting in the BgaAC phenotype to a region upstream of bgaA and in the promoter of a phosphoenolpyruvate-dependent phosphotransferase system (PTS) operon. The mutation was in a catabolite-responsive element (cre) and affected the binding of CcpA (catabolite control protein A), a key regulator of many carbon metabolism genes. The pts operon and bgaA were cotranscribed, and their transcription was regulated by CcpA. Deletion of ccpA altered ß-galactosidase activity, leading to a sevenfold increase in the parent but a fivefold decrease in the BgaAC mutant. The resulting ß-galactosidase activities were the same in the two strains, suggesting the presence of a second repressor. The presence of glucose in the growth medium resulted in pts-bgaA repression by both CcpA and the second repressor, with the latter being important in responding to the glucose concentration. Expression of ß-galactosidase is important for S. pneumoniae adherence during colonization of the nasopharynx, a site normally devoid of glucose. CcpA and environmental glucose concentrations thus appear to play important roles in the regulation of a niche-specific virulence factor.

* Corresponding author. Mailing address: Department of Microbiology, 845 19th Street South, BBRB 661/12, Birmingham, AL 35294-2170. Phone: (205) 934-9531. Fax: (205) 975-6715. E-mail: jyother{at}uab.edu

{triangledown} Published ahead of print on 11 May 2007.

Journal of Bacteriology, July 2007, p. 5183-5192, Vol. 189, No. 14
0021-9193/07/$08.00+0     doi:10.1128/JB.00449-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



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