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Live-Cell Forward Genetic Approach to Identify and Isolate Developmental Mutants in Chlamydia trachomatis

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The Chlamydia type III secretion system C-ring engages a chaperone-effector protein complex.

Kris E Spaeth¹, Yi-Shan Chen, Raphael H Valdivia

¹Department of Molecular Genetics and Microbiology and Center for Microbial Pathogenesis, Duke University Medical Center, Durham, North Carolina, USA.

|September 15, 2009

Summary

Chlamydia bacteria use a novel mechanism involving the injectisome

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Area of Science:

Microbiology
Molecular Biology
Bacterial Pathogenesis

Background:

Type III secretion systems (T3SS) translocate effector proteins into host cells.
Specialized chaperones maintain effector proteins for T3SS translocation.
Mechanisms for T3SS recognition of diverse effector-chaperone complexes remain unclear.

Purpose of the Study:

Investigate effector-chaperone recognition by the Chlamydia injectisome.
Identify novel components and mechanisms involved in Chlamydia T3SS function.

Main Methods:

Yeast two-hybrid analysis to identify protein-protein interactions.
Characterization of Chlamydia-specific protein interactions with the injectisome basal structure.

Main Results:

Identified protein interaction hubs linking effectors to CdsQ, a C-ring component.
Ct260/Mcsc (Multiple cargo secretion chaperone) binds and stabilizes hydrophobic effector proteins Cap1 and Ct618.
Mcsc-effector complexes bind to CdsQ, indicating C-ring mediated recognition.

Conclusions:

The Chlamydia injectisome's C-ring recognizes specific inclusion membrane proteins via chaperone complexes.
This mechanism may coordinate the translocation of effector subsets during infection stages.