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2 "catabolite control protein A"
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Research Support, Non-U.S. Gov'ts
Catabolite Control Protein A of Streptococcus suis Type 2 Contributes to Sugar Metabolism and Virulence
Yulong Tang , Wei Wu , Xiaoyan Zhang , Zhongyan Lu , Jianshun Chen , Weihuan Fang
J. Microbiol. 2012;50(6):994-1002.   Published online December 30, 2012
DOI: https://doi.org/10.1007/s12275-012-2035-3
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AbstractAbstract
Catabolite control protein A (CcpA) is the major transcriptional regulator in carbon catabolite repression in several Gram-positive bacteria. We attempted to characterize the role of a CcpA homologue of Streptococcus suis type 2 in sugar metabolism and virulence. Addition of glucose or sucrose to the defined medium significantly reduced the activity of raffinose-inducible α-galactosidase, cellobiose-inducible β-glucosidase, and maltose-inducible α-glucosidase of the wildtype strain by about 9, 4, and 2-3 fold, respectively. Deletion of ccpA substantially derepressed the effects of repressing sugars on α-galactosidase or β-glucosidase activity. The ccpA deletion mutant showed reduced expression of virulence genes sly and eno (P<0.05), decreased adhesion to and invasion into endothelial cells (P<0.05), and attenuated virulence to mice with significant reduction of death rate and bacterial burden in organs, as compared to the wild-type strain. Both the in vitro and in vivo defect phenotypes were reversible by ccpA complementation. Thus, this study shows that CcpA of S. suis type 2 plays an important role in carbon catabolite repression and virulence.
Expression of the Lactobacillus plantarum malE Gene Is Regulated by CcpA and a MalR-Like Protein
Lidia Muscariello , Valeria Vastano , Rosa A. Siciliano , Margherita Sacco , Rosangela Marasco
J. Microbiol. 2011;49(6):950-955.   Published online December 28, 2011
DOI: https://doi.org/10.1007/s12275-011-0495-5
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  • 12 Scopus
AbstractAbstract
Lactobacillus plantarum is commonly used in the food industry as a starter in various fermentations, especially in vegetable fermentations, in which starch is a common substrate. This polysaccharide, which is obtained from potatoes or corn and is hydrolysed mainly to maltose and glucose by acids or enzymes, is commercially used for the production of lactate by lactic acid fermentation. In this study, we describe the regulation of malE gene expression in L. plantarum. This gene, located in a 7-gene cluster, probably organized in an operon, encodes a putative maltose/maltodextrin-binding protein. We studied the expression of malE in L. plantarum LM3 (wild type) and in LM3-2 (ccpA1), which carries a null mutation in the ccpA gene, encoding the catabolite control protein A (CcpA). In the presence of glucose, expression of the MalE protein was higher in the mutant strain as compared to that in the wild-type strain. Transcription of the malE gene was induced by maltose and regulated by a CcpA-mediated carbon catabolite repression. Further, we isolated strains carrying mutations in 2 genes, lp_0172 and lp_0173, whose deduced amino acid sequences share significant identity with MalR, a regulator of the maltose operon in several gram-positive bacteria. A double mutant exhibited glucose-insensitive malE transcription, while absence of the functional Lp_0172 open reading frame had no effect on malE expression.

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