Hijacking and Use of Host Kinases by Chlamydiae

Abstract

Chlamydia species are causative agents of sexually transmitted infections, blinding trachoma, and animal infections with zoonotic potential. Being an obligate intracellular pathogen, Chlamydia relies on the host cell for its survival and development, subverting various host cell processes throughout the infection cycle. A key subset of host proteins utilized by Chlamydia include an assortment of host kinase signaling networks which are vital for many chlamydial processes including entry, nutrient acquisition, and suppression of host cell apoptosis. In this review, we summarize the recent advancements in our understanding of host kinase subversion by Chlamydia.

Keywords: Chlamydia; infection; kinase; phosphorylation; signaling.

Figure 1

Modulation of extrusion by Chlamydia. CT228 and MrcA interact with MYPT1 and ITPR3, respectively, to regulate the phosphorylation state of MLC2. Active phosphorylated MLC2 correlates with extrusion whereas inactive unphosphorylated MLC2 correlates with lysis. ITPR3 along with STIM1 control Ca2+ concentrations to influence relative active levels of MLCK and MYPT1 to regulate extrusion.

Figure 2

Host kinases manipulated by Chlamydia to promote survival. Schematic contains a summary of host kinases manipulated by Chlamydia to inhibit apoptosis. EB binding and entry activate PI3K and ERK1/2 to promote survival. TarP activates Erk1/2. Sequestration of PKC, 14-3-3β, PDPK1, and GSK3β work via different mechanisms to prevent apoptosis.