The secreted host-cell protein clusterin interacts with PmpD and promotes <i>Chlamydia trachomatis</i> infection.

ABSTRACT: Attachment and uptake into host cells are pivotal steps in the life cycle of the Chlamydiaceae, a family of obligate intracellular pathogens. Chlamydia trachomatis (Ctr) possesses a family of nine polymorphic membrane proteins (Pmps), which have been shown to be crucial for adhesion and internalization. However, the host-cell molecules involved have so far remained unknown. Here, we show that a fragment of Ctr PmpD, which forms high-molecular-weight oligomers in solution and adheres to epithelial cells, also binds to secreted clusterin (sCLU), a chaperone-like protein that is secreted into the extracellular space by the host cell, and forms part of the chaperone- and receptor-mediated extracellular protein degradation (CRED) pathway. Using in vitro assays, we de

SUBMITTER: Kocher F 

PROVIDER: S-EPMC11807975 | biostudies-literature | 2024

REPOSITORIES: biostudies-literature