Journal
BIOCHEMISTRY
Volume 50, Issue 35, Pages 7441-7443Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi201098r
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Funding
- Duke University
- National Institutes of Health [AI081694, AI46611]
- Burroughs Wellcome Trust
- C. R. Hauser Fellowship
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During infection of epithelial cells, the obligate intracellular pathogen Chlamydia trachomatis secretes the serine protease Chlamydia protease-like activity factor (CPAF) into the host cytosol to regulate a range of host cellular processes through targeted proteolysis. Here we report the development of an in vitro assay for the enzyme and the discovery of a cell-permeable CPAF zymogen-based peptide inhibitor with nanomolar inhibitory affinity. Treating C. trachomatis-infected He La cells with this inhibitor prevented CPAF cleavage of the intermediate filament vimentin and led to the loss of vimentin cage surrounding the intracellular vacuole. Because Chlamydia is a genetically intractable organism, this inhibitor may serve as a tool for understanding the role of CPAF in pathogenesis.
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