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Molecular Analysis of the Chlamydia trachomatis virulence factor Tarp

沙眼衣原体毒力因子 Tarp 的分子分析

基本信息

批准号：
10452569
负责人：
Travis James Jewett
金额：
$ 55.17万
依托单位：
UNIVERSITY OF CENTRAL FLORIDA
依托单位国家：
美国
项目类别：
财政年份：
2019
资助国家：
美国
起止时间：
2019-08-28 至 2024-07-31
项目状态：
已结题

来源：
https://reporter.nih.gov/project-details/10452569
关键词：
Actins Affect Architecture Attenuated Bacteria Binding Biochemical Biology Bundling C3H/HeJ Mouse Cell Shape Cells Cervical Chlamydia Chlamydia trachomatis Clinical Collaborations Collection Complement Cytoskeleton Data Development Epithelial Cells Event F-Actin Fluorescence Foundations G Actin GTP-Binding Protein alpha Subunits, Gs Generations Genes Genetic Goals Human Infection Interruption Invaded Length Measures Mechanics Mediating Microfilaments Modeling Molecular Molecular Analysis Molecular Genetics Morbidity - disease rate Mus Pathogenesis Pathogenicity Persons Phosphorylation Phosphotransferases Play Prevention Proline Protein Tyrosine Kinase Proteins Reporting Research Proposals Resources Role Sexually Transmitted Diseases Signal Transduction Spatial Distribution Technology Tertiary Protein Structure Testing Time Tyrosine Vaccines Virulence Virulence Factors biophysical properties bone genetic approach genetic regulatory protein high reward human tissue in vivo in vivo evaluation innovation insight mechanical properties microorganism microscopic imaging molecular mechanics mutant novel novel therapeutic intervention pathogen polymerization recruit tissue/cell culture tool

项目摘要

SUMMARY: The obligate intracellular bacterium Chlamydia trachomatis causes substantial morbidity in the US and worldwide. A C. trachomatis effector called Tarp for translocated actin recruiting protein is a candidate virulence factor. Tarp is tyrosine phosphorylated by a host cell kinase and is associated with actin recruitment during C. trachomatis entry. All reference and clinical isolates of Chlamydiae species examined to date harbor the tarP gene. We have identified and biochemically characterized four Tarp protein domains including: i) a phosphorylation domain ii) a proline rich oligomerization domain iii) a G-actin binding and nucleating domain, and iv) two F-actin binding and bundling domains. We hypothesize that specific Tarp domains are required for bacterial entry and/or chlamydial development. We will test this hypothesis by: 1) examining the mechanics of Tarp mediated actin bundles, 2) analyzing C. trachomatis tarp mutants and complements that express Tarp domain deletions for chlamydial invasion of host cells and development and 3). Investigate the requirement for tarP in a mouse infection model. Elucidation of the molecular mechanisms employed by C. trachomatis to initiate a successful infection may provide clues that can be applied to novel therapeutic interventions for this prolific pathogen.

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