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

Publication ,  Journal Article
Spaeth, KE; Chen, Y-S; Valdivia, RH
Published in: PLoS Pathog
September 2009

In Gram-negative bacterial pathogens, specialized chaperones bind to secreted effector proteins and maintain them in a partially unfolded form competent for translocation by type III secretion systems/injectisomes. How diverse sets of effector-chaperone complexes are recognized by injectisomes is unclear. Here we describe a new mechanism of effector-chaperone recognition by the Chlamydia injectisome, a unique and ancestral line of these evolutionarily conserved secretion systems. By yeast two-hybrid analysis we identified networks of Chlamydia-specific proteins that interacted with the basal structure of the injectisome, including two hubs of protein-protein interactions that linked known secreted effector proteins to CdsQ, the putative cytoplasmic C-ring component of the secretion apparatus. One of these protein-interaction hubs is defined by Ct260/Mcsc (Multiple cargo secretion chaperone). Mcsc binds to and stabilizes at least two secreted hydrophobic proteins, Cap1 and Ct618, that localize to the membrane of the pathogenic vacuole ("inclusion"). The resulting complexes bind to CdsQ, suggesting that in Chlamydia, the C-ring of the injectisome mediates the recognition of a subset of inclusion membrane proteins in complex with their chaperone. The selective recognition of inclusion membrane proteins by chaperones may provide a mechanism to co-ordinate the translocation of subsets of inclusion membrane proteins at different stages in infection.

Duke Scholars

Published In

PLoS Pathog

DOI

EISSN

1553-7374

Publication Date

September 2009

Volume

5

Issue

9

Start / End Page

e1000579

Location

United States

Related Subject Headings

  • Virology
  • Two-Hybrid System Techniques
  • Secretory Pathway
  • Protein Interaction Mapping
  • Protein Binding
  • Multiprotein Complexes
  • Molecular Sequence Data
  • Molecular Chaperones
  • Models, Biological
  • Membrane Proteins
 

Citation

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Spaeth, K. E., Chen, Y.-S., & Valdivia, R. H. (2009). The Chlamydia type III secretion system C-ring engages a chaperone-effector protein complex. PLoS Pathog, 5(9), e1000579. https://doi.org/10.1371/journal.ppat.1000579
Spaeth, Kris E., Yi-Shan Chen, and Raphael H. Valdivia. “The Chlamydia type III secretion system C-ring engages a chaperone-effector protein complex.PLoS Pathog 5, no. 9 (September 2009): e1000579. https://doi.org/10.1371/journal.ppat.1000579.
Spaeth KE, Chen Y-S, Valdivia RH. The Chlamydia type III secretion system C-ring engages a chaperone-effector protein complex. PLoS Pathog. 2009 Sep;5(9):e1000579.
Spaeth, Kris E., et al. “The Chlamydia type III secretion system C-ring engages a chaperone-effector protein complex.PLoS Pathog, vol. 5, no. 9, Sept. 2009, p. e1000579. Pubmed, doi:10.1371/journal.ppat.1000579.
Spaeth KE, Chen Y-S, Valdivia RH. The Chlamydia type III secretion system C-ring engages a chaperone-effector protein complex. PLoS Pathog. 2009 Sep;5(9):e1000579.

Published In

PLoS Pathog

DOI

EISSN

1553-7374

Publication Date

September 2009

Volume

5

Issue

9

Start / End Page

e1000579

Location

United States

Related Subject Headings

  • Virology
  • Two-Hybrid System Techniques
  • Secretory Pathway
  • Protein Interaction Mapping
  • Protein Binding
  • Multiprotein Complexes
  • Molecular Sequence Data
  • Molecular Chaperones
  • Models, Biological
  • Membrane Proteins