ArticleArchives of biochemistry and biophysics2009
Identifying catalytic residues in CPAF, a Chlamydia-secreted protease.
Article in Archives of biochemistry and biophysics, 2009. 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.
- A TriAdj-AdjuvantedVaccines · 2024Article
- Insights into the Autoproteolytic Processing and Catalytic Mechanism of theBiochemistry · 2019Article
- Peptidase Inhibitor 15 (PI15) Regulates Chlamydial CPAF Activity.Frontiers in cellular and infection microbiology · 2018Article
- The Chlamydia-Secreted Protease CPAF Promotes Chlamydial Survival in the Mouse Lower Genital Tract.Infection and immunity · 2016Article
- Characterization of CPAF critical residues and secretion during Chlamydia trachomatis infection.Infection and immunity · 2015Article
- Article
- A path forward for the chlamydial virulence factor CPAF.Microbes and infection · 2013Review
- Chlamydia trachomatis outer membrane complex protein B (OmcB) is processed by the protease CPAF.Journal of bacteriology · 2013Article
- Article
- CPAF: a Chlamydial protease in search of an authentic substrate.PLoS pathogens · 2012Article
- Localization of Chlamydia trachomatis hypothetical protein CT311 in host cell cytoplasm.Microbial pathogenesis · 2011Article
- Chlamydia trachomatis secretion of an immunodominant hypothetical protein (CT795) into host cell cytoplasm.Journal of bacteriology · 2011Article
- The chlamydial periplasmic stress response serine protease cHtrA is secreted into host cell cytosol.BMC microbiology · 2011Article
- Chlamydia trachomatis secretion of hypothetical protein CT622 into host cell cytoplasm via a secretion pathway that can be inhibited by the type III secretion system inhibitor compound 1.Microbiology (Reading, England) · 2011Article
- Chlamydia trachomatis secretion of proteases for manipulating host signaling pathways.Frontiers in microbiology · 2011Article
- Pathogenic Bacterial Proteins and their Anti-Inflammatory Effects in the Eukaryotic Host.Anti-inflammatory & anti-allergy agents in medicinal chemistry · 2009Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
A secreted chlamydial protease designated CPAF (Chlamydial Protease/proteasome-like Activity Factor) degrades host proteins, enabling Chlamydia to evade host defenses and replicate. The mechanistic details of CPAF action, however, remain obscure. We used a computational approach to search the protein databank for structures that are compatible with the CPAF amino acid sequence. The results reveal that CPAF possesses a fold similar to that of the catalytic domains of the tricorn protease from Thermoplasma acidophilum,and that CPAF residues H105, S499, and E558 are structurally analogous to the tricorn protease catalytic triad residues H746, S965, and D1023. Substitution of these putative CPAF catalytic residues blocked CPAF from degrading substrates in vitro, while the wild type and a noncatalytic control mutant of CPAF remained cleavage-competent. Substrate cleavage is also correlated with processing of CPAF into N-terminal (CPAFn) and C-terminal (CPAFc) fragments, suggesting that these putative catalytic residues may also be required for CPAF maturation.
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