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Chlamydia trachomatis inclusion membrane protein CT850 interacts with the dynein light chain DYNLT1 (Tctex1)

Jeffrey Mital1, Erika I Lutter2, Alexandra C Barger2

  • 1Host-Parasite Interactions Section, Laboratory of Intracellular Parasites, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, MT 59840, USA; Quinnipiac University, Hamden, CT 06518, USA.

Biochemical and Biophysical Research Communications
|May 7, 2015
PubMed

Insights

Chlamydia trachomatis uses the bacterial protein CT850 to hijack the host cell's dynein motor via DYNLT1. This interaction ensures the pathogen's vacuole localizes to the Microtubule Organizing Center for development.

Area of Science:

  • Cell Biology
  • Microbiology
  • Infectious Diseases

Background:

  • Chlamydia trachomatis subverts host dynein for intracellular trafficking to the Microtubule Organizing Center (MTOC).
  • Unlike typical dynein cargo, C. trachomatis transport is unaffected by dynactin complex disruption.
  • Chlamydial protein synthesis is required to initiate this unique transport mechanism.

Purpose of the Study:

  • To investigate the mechanism by which C. trachomatis interacts with the host dynein motor.
  • To identify specific chlamydial proteins involved in dynein-mediated transport.
  • To elucidate the role of host dynein light chain DYNLT1 in chlamydial inclusion positioning.

Main Methods:

  • Yeast two-hybrid screening to identify C. trachomatis proteins interacting with host factors.
  • Ectopic expression of chlamydial protein CT850 in HeLa cells.
  • Immunofluorescence microscopy to assess protein localization and cellular interactions.
  • Depletion of DYNLT1 using siRNA to evaluate its role in inclusion positioning.

Main Results:

  • The chlamydial inclusion membrane protein CT850 was identified to interact with the dynein light chain DYNLT1 (Tctex1).
  • This interaction depends on a specific motif within CT850, characteristic of DYNLT1 binding domains.
  • CT850 ectopic expression localized to the MTOC, dependent on the DYNLT1 binding domain, and DYNLT1 localized to CT850-rich regions on the inclusion.
  • DYNLT1 depletion disrupted the association of the chlamydial inclusion with centrosomes.

Conclusions:

  • CT850 utilizes a specific binding domain to interact with DYNLT1, a host dynein light chain.
  • This CT850-DYNLT1 interaction is crucial for recruiting dynein and positioning the chlamydial inclusion at the MTOC.
  • The findings reveal a novel mechanism of pathogen subversion of host intracellular transport machinery.
Keywords:
ChlamydiaDyneinMicrotubulesVesicle trafficking

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