Chlamydia-secreted protease CPAF degrades host antimicrobial peptides |
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| Institution: | 1. Department of Microbiology and Immunology, University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Drive, San Antonio, TX 78229, USA;2. Department of Clinic Diagnosis, Second Xiangya Hospital, Central South University, Changsha, Hunan, China;3. Department of Obstetrics and Gynecology, Second Xiangya Hospital, Central South University, Changsha, Hunan, China;4. Department of Endocrinology, Second Xiangya Hospital, Central South University, Changsha, Hunan, China;5. Department of Immunology, Xiangya School of Medicine, Central South University, Changsha, Hunan, China;1. Department of Pediatrics, University of Pittsburgh Medical Center, Pittsburgh, PA 15224, USA;2. Department of Epidemiology, Graduate School of Public Health, University of Pittsburgh, Pittsburgh, PA 15261, USA;1. Host-Parasite Interactions Section, Laboratory of Intracellular Parasites, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, MT 59840, USA;2. Microscopy Unit, Research Technologies Branch, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, MT 59840, USA;1. Department of Health Science and Technology, Aalborg University, Fredrik Bajers Vej 3b, 9220, Aalborg Ø, Denmark;2. Department of Biomedicine, Aarhus University, Wilhelms Meyers Allé 4, 8000, Aarhus, Denmark;3. Unit for Thrombosis Research, Institute of Public Health, University of Southern Denmark, Esbjerg, Denmark;1. Department of Obstetrics and Gynecology, Taizhou First People’s Hospital, Taizhou, Zhejiang 318020, PR China;2. First Affiliated Hospital, Wengzhou Medical University, Wengzhou, Zhejiang 325035, PR China;3. Department of Microbiology and Immunology, Wengzhou Medical University, Wengzhou, Zhejiang 325035, PR China;1. Department of Microbiology and Immunology, University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Drive, San Antonio, TX 78229, USA |
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| Abstract: | Chlamydia trachomatis infection in the lower genital tract, if untreated, can ascend to the upper genital tract, potentially leading to complications such as tubal factor infertility. The ascension involves cell-to-cell spreading, which may require C. trachomatis organisms to overcome mucosal extracellular effectors such as antimicrobial peptides. We found that among the 8 antimicrobial peptides tested, the cathelicidin LL-37 that is produced by both urogenital epithelial cells and the recruited neutrophils possessed a most potent antichlamydial activity. Interestingly, this antichlamydial activity was completely inhibited by CPAF, a C. trachomatis-secreted serine protease. The inhibition was dependent on CPAF's proteolytic activity. CPAF selectively degraded LL-37 and other antimicrobial peptides with an antichlamydial activity. CPAF is known to secrete into and accumulate in the infected host cell cytoplasm at the late stage of chlamydial intracellular growth and may be released to confront the extracellular antimicrobial peptides before the intra-inclusion organisms are exposed to extracellular environments during host cell lysis and chlamydial spreading. Thus, the finding that CPAF selectively targets host antimicrobial peptides that possess antichlamydial activities for proteolysis suggests that CPAF may contribute to C. trachomatis pathogenicity by aiding in ascending infection. |
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| Keywords: | CPAF Proteolysis of antimicrobial peptides |
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