权益分类	功能权益	普通用户	{{item.name}}会员
{{category.name}}	{{benefitItem.name}}

Role of Clp proteins in pathophysiology of Streptococcus mutans

Clp 蛋白在变形链球菌病理生理学中的作用

基本信息

批准号：
10209781
负责人：
Indranil Biswas
金额：
$ 3.13万
依托单位：
UNIVERSITY OF KANSAS MEDICAL CENTER
依托单位国家：
美国
项目类别：
财政年份：
2018
资助国家：
美国
起止时间：
2018-05-01 至 2022-04-30
项目状态：
已结题

来源：
https://reporter.nih.gov/project-details/10209781
关键词：
ATP phosphohydrolase Adaptor Signaling Protein Adult Bacteria Bacterial Proteins Biology C-terminal Cell division Child ClpX protein Communities Competence Complex Cost of Illness Dental Plaque Dental caries Developed Countries Development Environment Etiology Firmicutes Functional disorder Genes Goals Gram-Positive Bacteria Growth Heat-Shock Response Human Infective endocarditis Mass Spectrum Analysis Mediating Microbial Biofilms Molecular Molecular Chaperones N-terminal Nutrient Oral cavity Organism Peptide Hydrolases Phosphorylation Play Production Protein Family Proteins Proteolysis Quality Control Regulation Role Serine Protease Signal Transduction Streptococcus Streptococcus mutans Stress Substrate Specificity System Temperature Virulence bacterial community bacteriocin biological adaptation to stress environmental flux misfolded protein novel oral pathogen oral streptococci pathogen polymicrobial biofilm protein degradation response stress tolerance tooth surface

项目摘要

ABSTRACT Streptococcus mutans has been strongly implicated as the principal etiological agent in human dental caries. It is also an important agent of infective endocarditis. S. mutans colonizes the oral cavity through the formation of diverse, multispecies biofilms on the tooth surface, known as dental plaque. S. mutans flourishes in the hostile environment of the oral cavity by responding efficiently to various environmental fluxes, including severe nutrient limitation, fluctuations in pH and temperature. Exposure of bacteria to these adverse environments can induce a stress tolerance response through expression of a wide variety of proteins that provide cross-protection against environmental challenges. The caseinolytic protease (Clp) family proteins, which contain HSP100/Clp chaperones and the ClpP protease, constitute the core of bacterial protein quality control systems involved in thermal and other stress responses. ClpP, a small cytoplasmic serine protease, associates with a partner ATPase chaperone to form a functional complex that specifically targets damaged or mis-folded proteins for degradation (collectively known as regulated proteolysis) during stresses. While ClpP degrades the damaged protein, the ATPase component determines the substrate specificity. Like other Firmicutes, streptococci encode five Clp ATPases and only three of these (ClpC, ClpE, and ClpX) interact with ClpP to form active complexes. ClpP is the primary intracellular protease that is required for stress tolerance response, bacteriocin production, and biofilm formation among others While ClpX/P is the major player, we recently found that ClpE/P is also involved in protein quality control in streptococci. However, the molecular mechanism of substrate recognition and degradation by ClpX/P and ClpE/P are not well understood in these organisms. In fact, very little is known about protein quality control and their role in virulence in streptococci. Our long-term goal is to understand the molecular mechanisms of regulated proteolysis in S. mutans and other oral streptococci.

摘要