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Markerless Gene Deletion by Floxed Cassette Allelic Exchange Mutagenesis in Chlamydia trachomatis
Published on: January 30, 2020
Neutralizing antichlamydial activity of complement by chlamydia-secreted protease CPAF
Zhangsheng Yang1, Lingli Tang2, Zhiguang Zhou3
1Department of Microbiology & Immunology, University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Drive, San Antonio, TX 78229, USA.
Abstract:
Ascending infection by sexually transmitted Chlamydia trachomatis is required for chlamydial induction of tubal pathology. To achieve ascension, the C. trachomatis organisms may have to spread from cell to cell, which inevitably exposes the organisms to extracellular mucosal effectors such as complement factors that are known to possess strong antichlamydial activities. Here, we report that the chlamydia-secreted protease CPAF efficiently neutralized complement factor C3-dependent antichlamydial activity. The neutralization was dependent on the proteolytic activity of CPAF and correlated with the CPAF-mediated degradation of complement factor C3 and factor B. As a result, CPAF preferentially inhibited the alternative complement activation pathway. The significance and limitation of these observations were discussed.
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