Artículos
Título:
The Chlamydia trachomatis type III secretion chaperone Slc1 engages multiple early effectors, including TepP, a tyrosine-phosphorylated protein required for the recruitment of CrkI-II to nascent inclusions and innate immune signaling.
Autor/es:
CHEN, YS; BASTIDAS, RJ; SAKA, HA; CARPENTER, VK; RICHARDS, KL; PLANO, GV; VALDIVIA, RH
Editorial:
PUBLIC LIBRARY SCIENCE
Referencias:
Lugar: San Francisco; Año: 2014 p. 1003954 - 1003954
Resumen:
hlamydia trachomatis, the causative agent of trachoma and sexually
transmitted infections, employs a type III secretion (T3S) system to
deliver effector proteins into host epithelial cells to establish a
replicative vacuole. Aside from the phosphoprotein TARP, a Chlamydia
effector that promotes actin re-arrangements, very few factors mediating
bacterial entry and early inclusion establishment have been
characterized. Like many T3S effectors, TARP requires a chaperone (Slc1)
for efficient translocation into host cells. In this study, we defined
proteins that associate with Slc1 in invasive C. trachomatis elementary
bodies (EB) by immunoprecipitation coupled with mass spectrometry. We
identified Ct875, a new Slc1 client protein and T3S effector, which we
renamed TepP (Translocated early phosphoprotein). We provide evidence
that T3S effectors form large molecular weight complexes with Scl1 in
vitro and that Slc1 enhances their T3S-dependent secretion in a
hete