CPAF sec-dependent.pdfVIP

Microbiology (2010), 156, 3031–3040 DOI 10.1099/mic.0.040527-0 Secretion of the chlamydial virulence factor CPAF requires the Sec-dependent pathway Ding Chen,1 Lei Lei,1 Chunxue Lu,1 Rhonda Flores,1 Matthew P. DeLisa,2 Tucker C. Roberts,3 Floyd E. Romesberg3 and Guangming Zhong1 Correspondence 1Department of Microbiology and Immunology, University of Texas Health Science Center at San Guangming Zhong Antonio, 7703 Floyd Curl Drive, San Antonio, TX 78229, USA Zhongg@ 2 Department of Biomedical Engineering, Cornell University, Ithaca, NY 14853, USA 3Department of Chemistry, The Scripps Research Institute, 10550 N. Torrey Pines Rd, La Jolla, CA 92037, USA The chlamydial protease/proteasome-like activity factor (CPAF) is secreted into the host cytosol to degrade various host factors that benefit chlamydial intracellular survival. Although the full- length CPAF is predicted to contain a putative signal peptide at its N terminus, the secretion pathway of CPAF is still unknown. Here, we have provided experimental evidence that the N- terminal sequence covering the M1–G31 region was cleaved from CPAF during chlamydial infection. The CPAF N-terminal sequence, when expressed in a phoA gene fusion construct, was able to direct the export of the m