Abstract
Chlamydia trachomatis and Candida albicans are common inhabitants of the female genital tract. C. albicans can impact viability and pathogenesis of some bacteria. Previously, we investigated physical interactions between C. trachomatis elementary bodies (EB) and C. albicans. This work indicated that EB bind to C. albicans and become noninfectious by 24 hours post binding. Here, we continue our investigation of these interkingdom, polymicrobial interactions. C. albicans adheres to bacteria or host surfaces via agglutinin-like sequence (Als) or heat shock 70 (Ssa) proteins. C. trachomatis EB did not bind C. albicans Ssa2 deficient strains as efficiently as wild type or complemented strains, indicating a role for this protein in chlamydial adherence to Candida. Additionally, C. albicans β-glucans inhibit chlamydial infection when exposure occurs during EB adsorption onto cervical cells. Laminarin (Lam), a β-glucan agonist of the C-type lectin receptor Dectin-1, inhibited chlamydial infection both cervical epithelial cells and mice when exposure occurred prior to, during, or immediately following EB inoculation. Conversely, a Dectin-1 antagonist laminarin (Lam-Ant) did not inhibit infection in vitro, suggesting β-glucan inhibition of C. trachomatis requires CTLR signaling. Overall, our data demonstrate that β-glucans from multiple species, including Candida albicans, inhibits Chlamydia via stimulation of host signaling pathways.
Published Version
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