Characterization of CPAF critical residues and secretion during Chlamydia trachomatis infection

Infection and Immunity
Zhangsheng YangGuangming Zhong

Abstract

CPAF (chlamydial protease-like activity factor), a Chlamydia serine protease, is activated via proximity-induced intermolecular dimerization that triggers processing and removal of an inhibitory peptide occupying the CPAF substrate-binding groove. An active CPAF is a homodimer of two identical intramolecular heterodimers, each consisting of 29-kDa N-terminal and 35-kDa C-terminal fragments. However, critical residues for CPAF intermolecular dimerization, catalytic activity, and processing were defined in cell-free systems. Complementation of a CPAF-deficient chlamydial organism with a plasmid-encoded CPAF has enabled us to characterize CPAF during infection. The transformants expressing CPAF mutated at intermolecular dimerization, catalytic, or cleavage residues still produced active CPAF, although at a lower efficiency, indicating that CPAF can tolerate more mutations inside Chlamydia-infected cells than in cell-free systems. Only by simultaneously mutating both intermolecular dimerization and catalytic residues was CPAF activation completely blocked during infection, both indicating the importance of the critical residues identified in the cell-free systems and exploring the limit of CPAF's tolerance for mutations in the intr...Continue Reading

References

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Citations

Apr 26, 2016·Nature Reviews. Microbiology·Cherilyn ElwellJoanne Engel
Oct 21, 2016·Microbes and Infection·Zhangsheng YangGuangming Zhong
Feb 24, 2017·Clinical and Vaccine Immunology : CVI·Luis M de la MazaRobert C Brunham
Mar 8, 2017·Infection and Immunity·Nicholas P Cianciotto, Richard C White
Jul 7, 2016·Infection and Immunity·Zhangsheng YangGuangming Zhong
Jun 15, 2018·Frontiers in Cellular and Infection Microbiology·Bhupesh K PrustyThomas Rudel
Mar 9, 2021·Expert Review of Vaccines·Luis M de la MazaSukumar Pal

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