TheChlamydia trachomatisCtad1 invasin exploits the human integrin β1 receptor for host cell entry

• DOI: 10.1111/cmi.12549
• Publication Date: 2015-11-24T03:42:49Z
• Authors: Sonja Stallmann; Johannes H. Hegemann
• Keywords: Internalization

Infection of human cells by the obligate intracellular bacterium Chlamydia trachomatis requires adhesion and internalization infectious elementary body (EB). This highly complex process is poorly understood. Here, we characterize Ctad1 (CT017) as a new adhesin invasin from C. serovar E. Recombinant (rCtad1) binds to via two bacterial SH3 domains located in its N-terminal half. Pre-incubation host with rCtad1 reduces subsequent infectivity bacteria. Interestingly, protein-coated latex beads revealed being an invasin. interacts integrin β1 subunit on epithelial cells, induces clustering integrins at EB attachment sites. Receptor activation ERK1/2 phosphorylation. Accordingly, binding β1-negative significantly impaired, chlamydial infection. Thus interaction mediates signaling processes that promote host-cell invasion.