Campylobacter jejuni cytolethal distending toxin (CDT)

Cytolethal distending toxin (CDT) is a major virulence factor secreted by Campylobacter jejuni and consists of three subunits: CdtA, CdtB, and CdtC. CdtB functions as a DNase, inducing DNA double-strand breaks in the nuclei of host cells, which leads to cell cycle arrest and apoptosis, while CdtA and CdtC facilitate toxin entry by binding to cholesterol-rich regions of host cell membranes[2]. CDT plays a central role in Campylobacter pathogenesis, contributing to mucosal damage, invasion, and immune evasion. Other notable Campylobacter proteins involved in virulence include Campylobacter invasion antigens (Cia), which facilitate bacterial entry into host cells, and proteins involved in glycosylation for host adherence[1]. Campylobacter infections are among the most common causes of bacterial gastroenteritis worldwide, with complications such as Guillain–Barré syndrome and reactive arthritis occurring in some cases[1][2][3][4]. There are currently no drugs that directly target Campylobacter toxins; instead, management focuses on controlling infection via antibiotics, though resistance is an increasing concern.

Other names

cytolethal distending toxinCDTCdtACdtBCdtCCampylobacter toxinsCampylobacter proteins

DNA double-strand break induction by CdtB, leading to cell cycle arrest at the G2/M phase and apoptosis CdtA and CdtC facilitate delivery of CdtB to host cells by binding cholesterol-rich membrane microdomains Cia proteins facilitate host cell invasion, N-linked glycosylation supports adherence and invasion