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PMID: 2557096 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S. Review

Carbohydrate uptake in the oral pathogen Streptococcus mutans: mechanisms and regulation by protein phosphorylation.

Biochimie ·Vol. 71 ·No. 9-10 ·1989-00-00 ·Pages 997-1004

Jacobson GR, Lodge J, Poy F

Abstract

Streptococcus mutans is the primary etiological agent of dental caries in man and other animals. This organism and other related oral streptococci use carbohydrates almost exclusively as carbon and energy sources, fermenting them primarily to lactic acid which initiates erosion of tooth surfaces. Investigations over the past decade have shown that the major uptake mechanism for most carbohydrates in S. mutans is the phosphoenolpyruvate (PEP)-dependent phosphotransferase system (PTS), although non-PTS systems have also been identified for glucose and sucrose. Regulation of sugar uptake occurs by induction/repression and inducer exclusion mechanisms in S. mutans, but apparently not by inducer expulsion as is found in some other streptococci. In addition, ATP-dependent protein kinases have also been identified in S. mutans and other oral streptococci, and a regulatory function for at least one of these has been postulated. Among a number of proteins that are phosphorylated by these enzymes, the predominant soluble protein substrate is the general phospho-carrier protein of the PTS, HPr, as had previously been observed in a variety of Gram-positive bacteria. Recent results have provided evidence for a role for ATP-dependent phosphorylation of HPr in the coordination of sugar uptake and its catabolism in S. mutans. In this review, these results are summarized, and directions for future research in this area are discussed.

MeSH Terms
Carbohydrates/genetics,pharmacokinetics Dental Caries/genetics,microbiology Phosphorylation Phosphotransferases/genetics,metabolism Repressor Proteins/genetics Streptococcus mutans/genetics,metabolism Transcription Factors/genetics
Chemicals
Carbohydrates Repressor Proteins Transcription Factors Phosphotransferases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Jacobson G R
Department of Biology, Boston University, MA 02215.
Lodge J
Poy F
Article Info
Journal
Biochimie
Abbr.
Biochimie
ISSN
0300-9084
Published
1989-00-00
Pages
997-1004
Language
English
Region
France
NLM ID
1264604
Subset
IM
Grants
NIDCR NIH HHS · DE05966 · United States
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