ArticleJournal of bacteriology2011
Disulfide bonding within components of the Chlamydia type III secretion apparatus correlates with development.
Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Review
- Review
- Pathogenicity and virulence ofVirulence · 2025Review
- Altering the redox status ofeLife · 2025Article
- Type III Secretion inMicrobiology and molecular biology reviews : MMBR · 2023Review
- Chronic Inflammatory Diseases at Secondary Sites Ensuing Urogenital or PulmonaryMicroorganisms · 2020Review
- Article
- Sulforaphane promotes chlamydial infection by suppressing mitochondrial protein oxidation and activation of complement C3.Protein science : a publication of the Protein Society · 2019Article
- Comprehensive Flux Modeling ofFrontiers in microbiology · 2019Article
- The extended structure of the periplasmic region of CdsD, a structural protein of the type III secretion system of Chlamydia trachomatis.Protein science : a publication of the Protein Society · 2016Article
- A working model for the type III secretion mechanism in Chlamydia.Microbes and infection · 2016Review
- Article
- Crystallization and preliminary X-ray diffraction studies of the C-terminal domain of Chlamydia trachomatis CdsD.Acta crystallographica. Section F, Structural biology communications · 2014Article
- New frontiers in type III secretion biology: the Chlamydia perspective.Infection and immunity · 2014Review
- Conserved type III secretion system exerts important roles in Chlamydia trachomatis.International journal of clinical and experimental pathology · 2014Review
- Förster resonance energy transfer (FRET) as a tool for dissecting the molecular mechanisms for maturation of the Shigella type III secretion needle tip complex.International journal of molecular sciences · 2012Review
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Authors and funding
2 authors.
Funding
Abstract
Chlamydia spp. exhibit a unique biphasic developmental cycle whereby infectious elementary bodies (EBs) invade host epithelial cells and differentiate into noninfectious, metabolically active reticulate bodies (RBs). EBs posses a unique outer envelope where rigidity is achieved by disulfide bonding among cysteine-rich envelope-associated proteins. Conversely, these disulfide bonds become reduced in RBs to accommodate vegetative growth, thereby linking the redox status of cysteine-rich envelope proteins with progression of the developmental cycle. We investigated the potential role of disulfide bonding within the chlamydial type III secretion system (T3SS), since activity of this system is also closely linked to development. We focused on structural components of the T3S apparatus that contain an unusually high number of cysteine residues compared to orthologs in other secretion systems. Nonreducing SDS-PAGE revealed that EB-localized apparatus proteins such as CdsF, CdsD, and CdsC form higher-order complexes mediated by disulfide bonding. The most dramatic alterations were detected for the needle protein CdsF. Significantly, disulfide bonding patterns shifted during differentiation of developmental forms and were completely reduced in RBs. Furthermore, at later time points during infection following RB to EB conversion, we found that CdsF is reoxidized into higher-order complexes. Overall, we conclude that the redox status of specific T3SS apparatus proteins is intimately linked to the developmental cycle and constitutes a newly appreciated aspect of functionally significant alterations within proteins of the chlamydial envelope.
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