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. Author manuscript; available in PMC: 2018 Apr 1.
Published in final edited form as: Emerg Top Life Sci. 2017 Apr 21;1(1):75–83. doi: 10.1042/ETLS20160019

Figure 1. CDI-mediated toxin delivery.

Figure 1

CdiA is exported to the cell surface following Sec-dependent secretion across the inner membrane. CdiA binds to outer-membrane protein (OMP) receptors on target bacteria using a centrally located domain. Following receptor recognition, the C-terminal toxin domain is delivered into the periplasm where it presumably interacts with specific integral membrane proteins (IMP) to enter the lipid bilayer (for pore-forming toxins) or cross the membrane to enter the cytosol. Target bacteria are usually inhibited through dissipation of the proton-motive force or degradation of nucleic acids. Toxin domains delivered into sibling cells are neutralized by the direct binding of cognate CdiI immunity proteins. The outer-membrane (OM), peptidoglyan (PG) and cytoplasmic membrane (CM) are indicated.