Research progress on the regulation and mechanism of Hsp100/Clp ATPase on virulence expressions in Streptococcus mutans

doi:10.3877/cma.j.issn.1674-1366.2018.03.010

Abstract

Abstract:

Streptococcus mutans (S.mutans) is the initiating factor of dental caries. Depending on its acid production, acid resistance and biofilm formation ability, S.mutans has been regarded as the predominant bacteria in the oral cariogenic environment. Adenosine triphosphate (ATP) dependent endopeptidase Clp (Clp ATPase) belongs to the heat shock protein 100 (heat shock protein, Hsp100) family. It can affect many biological properties of bacteria via regulating gene expression and controlling key proteins activities. Some of Hsp100/Clp ATPase members can bind to the ATP-dependent serine protease ClpP to form functional complexes that have the ability to activate, remodel, and degrade denatured proteins, thus maintaining protein homeostasis and resistance to hostile oral environment. Specifically targeting Hsp100/Clp ATPase of S.mutans is expected to provide new ideas and methods for the prevention and treatment of dental caries. In terms of the structure and classification of Hsp100/Clp ATPase, this review summarizes systematically Hsp100/Clp ATPase related genes, proteins and biological behavior regulations in S.mutans, as well as the roles of drugs that specifically targeted Hsp100/Clp ATPase. A comprehensive foundation of the relationship between Hsp100/Clp ATPase and S.mutans cariogenicity can provide a promising candidate target of anti-caries drugs.

Key words: ATP-dependent endopeptidase Clp, Streptococcus mutans, Stress response, Cariogenic virulent factors

Fangcao Lei, Yan Yang, Jianying Zhang. Research progress on the regulation and mechanism of Hsp100/Clp ATPase on virulence expressions in Streptococcus mutans[J]. Chinese Journal of Stomatological Research(Electronic Edition), 2018, 12(03): 190-194.

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