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The Chlamydia trachomatis Ctad1 invasin exploits the human integrin ß1 receptor for host cell entry.

Stallmann, Sonja; Hegemann, Johannes H.
Cell Microbiol; 18(5): 761-75, 2016 May.
Artigo em Inglês | MEDLINE | ID: mdl-26597572
Infection of human cells by the obligate intracellular bacterium Chlamydia trachomatis requires adhesion and internalization of the infectious elementary body (EB). This highly complex process is poorly understood. Here, we characterize Ctad1 (CT017) as a new adhesin and invasin from C. trachomatis serovar E. Recombinant Ctad1 (rCtad1) binds to human cells via two bacterial SH3 domains located in its N-terminal half. Pre-incubation of host cells with rCtad1 reduces subsequent adhesion and infectivity of bacteria. Interestingly, protein-coated latex beads revealed Ctad1 being an invasin. rCtad1 interacts with the integrin ß1 subunit on human epithelial cells, and induces clustering of integrins at EB attachment sites. Receptor activation induces ERK1/2 phosphorylation. Accordingly, rCtad1 binding to integrin ß1-negative cells is significantly impaired, as is the chlamydial infection. Thus interaction of C. trachomatis Ctad1 with integrin ß1 mediates EB adhesion and induces signaling processes that promote host-cell invasion.
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