ArticleJournal of bacteriology2013
Chlamydia trachomatis outer membrane complex protein B (OmcB) is processed by the protease CPAF.
Article in Journal of bacteriology, 2013. 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, 26 citations in OpenAlex.
- Plasmid-encoded Pgp3 protein enhances the infectivity ofZhong nan da xue xue bao. Yi xue ban = Journal of Central South University. Medical sciences · 2026Article
- 3-O Sulfated Heparan Sulfate (G2) Peptide Ligand Impairs the Infectivity ofBiomolecules · 2025Article
- Tail-specific protease is an essentialInfection and immunity · 2024Article
- Preclinical screen for protection efficacy of chlamydial antigens that are immunogenic in humans.Infection and immunity · 2023Article
- TargeTron Inactivation of Chlamydia trachomatisInfection and immunity · 2023Article
- Virulence Protein Pgp3 Is Insufficient To Mediate Plasmid-Dependent Infectivity of Chlamydia trachomatis.Infection and immunity · 2023Article
- The multiple functions of the numerousMicrobial cell (Graz, Austria) · 2019Review
- N-terminomics identifies widespread endoproteolysis and novel methionine excision in a genome-reduced bacterial pathogen.Scientific reports · 2017Article
- Elongation factor Tu is a multifunctional and processed moonlighting protein.Scientific reports · 2017Article
- Article
- Characterization of CPAF critical residues and secretion during Chlamydia trachomatis infection.Infection and immunity · 2015Article
- Chlamydia trachomatis In Vivo to In Vitro Transition Reveals Mechanisms of Phase Variation and Down-Regulation of Virulence Factors.PloS one · 2015Article
- Chlamydia infection depends on a functional MDM2-p53 axis.Nature communications · 2014Article
- The Chlamydia protease CPAF: caution, precautions and function.Pathogens and disease · 2014Article
- Reassessing the role of the secreted protease CPAF in Chlamydia trachomatis infection through genetic approaches.Pathogens and disease · 2014Article
- A path forward for the chlamydial virulence factor CPAF.Microbes and infection · 2013Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
Abstract
We previously reported that the Chlamydia trachomatis outer membrane complex protein B (OmcB) was partially processed in Chlamydia-infected cells. We have now confirmed that the OmcB processing occurred inside live cells during chlamydial infection and was not due to proteolysis during sample harvesting. OmcB processing was preceded by the generation of active CPAF, a serine protease known to be able to cross the inner membrane via a Sec-dependent pathway, suggesting that active CPAF is available for processing OmcB in the periplasm. In a cell-free system, CPAF activity is both necessary and sufficient for processing OmcB. Both depletion of CPAF from Chlamydia-infected cell lysates with a CPAF-specific antibody and blocking CPAF activity with a CPAF-specific inhibitory peptide removed the OmcB processing ability of the lysates. A highly purified wild-type CPAF but not a catalytic residue-substituted mutant CPAF was sufficient for processing OmcB. Most importantly, in chlamydial culture, inhibition of CPAF with a specific inhibitory peptide blocked OmcB processing and reduced the recovery of infectious organisms. Thus, we have identified OmcB as a novel authentic target for the putative chlamydial virulence factor CPAF, which should facilitate our understanding of the roles of CPAF in chlamydial biology and pathogenesis.
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