ArticleJournal of bacteriology2008
Bioinformatic and biochemical evidence for the identification of the type III secretion system needle protein of Chlamydia trachomatis.
Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 57 citations in OpenAlex.
- Type III secretion system chaperones: a helping hand for secretion.Microbiology (Reading, England) · 2026Review
- Anti-Idiotypic Nanobodies Mimicking an Epitope of the Needle Protein of the Chlamydial Type III Secretion System for Targeted Immune Stimulation.International journal of molecular sciences · 2024Article
- Type III Secretion inMicrobiology and molecular biology reviews : MMBR · 2023Review
- Characterization of Chlamydia muridarum TC0668 Protein: Localization, Expression, and Inflammation-Inducing Effects on Host Cell.Current microbiology · 2022Article
- Article
- The multiple functions of the numerousMicrobial cell (Graz, Austria) · 2019Review
- Chaperone-mediated secretion switching from early to middle substrates in the type III secretion system encoded byThe Journal of biological chemistry · 2019Article
- Profiling and validation of individual and patterns of Chlamydia trachomatis-specific antibody responses in trachomatous trichiasis.Parasites & vectors · 2017Article
- Chlamydial Type III Secretion System Needle Protein Induces Protective Immunity againstBioMed research international · 2017Article
- Functional Characterization of EscK (Orf4), a Sorting Platform Component of the Enteropathogenic Escherichia coli Injectisome.Journal of bacteriology · 2017Article
- A working model for the type III secretion mechanism in Chlamydia.Microbes and infection · 2016Review
- Article
- Multipart Chaperone-Effector Recognition in the Type III Secretion System of Chlamydia trachomatis.The Journal of biological chemistry · 2015Article
- Chlamydia psittaci comparative genomics reveals intraspecies variations in the putative outer membrane and type III secretion system genes.Microbiology (Reading, England) · 2015Article
- Pathogen-host reorganization during Chlamydia invasion revealed by cryo-electron tomography.Cellular microbiology · 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
- New players in the same old game: a system level in silico study to predict type III secretion system and effector proteins in bacterial genomes reveals common themes in T3SS mediated pathogenesis.BMC research notes · 2013Article
- Identification of novel type III secretion chaperone-substrate complexes of Chlamydia trachomatis.PloS one · 2013Article
- Chlamydiae assemble a pathogen synapse to hijack the host endoplasmic reticulum.Traffic (Copenhagen, Denmark) · 2012Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Chlamydia spp. express a functional type III secretion system (T3SS) necessary for pathogenesis and intracellular growth. However, certain essential components of the secretion apparatus have diverged to such a degree as to preclude their identification by standard homology searches of primary protein sequences. One example is the needle subunit protein. Electron micrographs indicate that chlamydiae possess needle filaments, and yet database searches fail to identify a SctF homologue. We used a bioinformatics approach to identify a likely needle subunit protein for Chlamydia. Experimental evidence indicates that this protein, designated CdsF, has properties consistent with it being the major needle subunit protein. CdsF is concentrated in the outer membrane of elementary bodies and is surface exposed as a component of an extracellular needle-like projection. During infection CdsF is detectable by indirect immunofluorescence in the inclusion membrane with a punctuate distribution adjacent to membrane-associated reticulate bodies. Biochemical cross-linking studies revealed that, like other SctF proteins, CdsF is able to polymerize into multisubunit complexes. Furthermore, we identified two chaperones for CdsF, termed CdsE and CdsG, which have many characteristics of the Pseudomonas spp. needle chaperones PscE and PscG, respectively. In aggregate, our data are consistent with CdsF representing at least one component of the extended Chlamydia T3SS injectisome. The identification of this secretion system component is essential for studies involving ectopic reconstitution of the Chlamydia T3SS. Moreover, we anticipate that CdsF could serve as an efficacious target for anti-Chlamydia neutralizing antibodies.
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