ArticleBiochemistry2009
Biophysical characterization of Chlamydia trachomatis CT584 supports its potential role as a type III secretion needle tip protein.
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- CT584 Is Not a Protective Vaccine Antigen against Respiratory Chlamydial Challenge in Mice.Vaccines · 2024Article
- Evaluation in mice of cell-free produced CT584 as a Chlamydia vaccine antigen.bioRxiv : the preprint server for biology · 2024Article
- Type III Secretion inMicrobiology and molecular biology reviews : MMBR · 2023Review
- Article
- Robust Heat Shock Response inFrontiers in microbiology · 2021Article
- A working model for the type III secretion mechanism in Chlamydia.Microbes and infection · 2016Review
- Architecture and host interface of environmental chlamydiae revealed by electron cryotomography.Environmental microbiology · 2014Article
- Conserved type III secretion system exerts important roles in Chlamydia trachomatis.International journal of clinical and experimental pathology · 2014Review
- New frontiers in type III secretion biology: the Chlamydia perspective.Infection and immunity · 2014Review
- Modulation of host signaling and cellular responses by Chlamydia.Cell communication and signaling : CCS · 2013Review
- Structure of CT584 from Chlamydia trachomatis refined to 3.05 Å resolution.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- Oligomeric states of the Shigella translocator protein IpaB provide structural insights into formation of the type III secretion translocon.Protein science : a publication of the Protein Society · 2013Article
- Identification of novel type III secretion chaperone-substrate complexes of Chlamydia trachomatis.PloS one · 2013Article
- 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
- The non-flagellar type III secretion system evolved from the bacterial flagellum and diversified into host-cell adapted systems.PLoS genetics · 2012Article
- Structural characterization of a novel Chlamydia pneumoniae type III secretion-associated protein, Cpn0803.PloS one · 2012Article
- Quantitative proteomics reveals metabolic and pathogenic properties of Chlamydia trachomatis developmental forms.Molecular microbiology · 2011Article
- Biochemical and localization analyses of putative type III secretion translocator proteins CopB and CopB2 of Chlamydia trachomatis reveal significant distinctions.Infection and immunity · 2011Article
- Multi-Functional Characteristics of the Pseudomonas aeruginosa Type III Needle-Tip Protein, PcrV; Comparison to Orthologs in other Gram-negative Bacteria.Frontiers in microbiology · 2011Article
- Chlamydia Pneumoniae CdsL Regulates CdsN ATPase Activity, and Disruption with a Peptide Mimetic Prevents Bacterial Invasion.Frontiers in microbiology · 2011Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Chlamydia are obligate intracellular bacterial pathogens that cause a variety of diseases. Like many Gram-negative bacteria, they employ type III secretion systems (T3SS) for invasion, establishing and maintaining their unique intracellular niche, and possibly cellular exit. Computational structure prediction indicated that ORF CT584 is homologous to other T3SS needle tip proteins. Tip proteins have been shown to be localized to the extracellular end of the T3SS needle and play a key role in controlling secretion of effector proteins. We have previously demonstrated that T3SS needle tip proteins from different bacteria share many biophysical characteristics. To support the hypothesis that CT584 is a T3SS needle tip protein, biophysical properties of CT584 were explored as a function of pH and temperature, using spectroscopic techniques. Far-UV circular dichroism, Fourier transform infrared spectroscopy, UV absorbance spectroscopy, ANS extrinsic fluorescence, turbidity, right angle static light scattering, and analytical ultracentrifugation were all employed to monitor the secondary, tertiary, quaternary, and aggregation behavior of this protein. An empirical phase diagram approach is also employed to facilitate such comparisons. These analyses demonstrate that CT584 shares many biophysical characteristics with other T3SS needle tip proteins. These data support the hypothesis that CT584 is a member of the same functional family, although future biologic analyses are required.
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