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. 2022 Apr 26;9:866854. doi: 10.3389/fmolb.2022.866854

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Copyright © 2022 Cuthbert, Hayes and Goulding.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Introduction to CDI proteins and a working model of CDI toxin translocation. (A) Domain architecture of CdiA and organization of the cdi locus. CdiA is colored by domain, including the secretion signal (SS), two partner secretion (TPS) domain, FHA-1, receptor-binding domain (RBD), tyrosine-proline rich domain (YP), FHA-2, pretoxin (PT) domain, VENN motif, and CdiA-CT entry domain and CdiA-CT cytotoxic (Toxic) domain. (B) Schematic of CDI. CdiB (green) presents CdiA (colored by domain as in A) onto the surface of the inhibitor cell. When the CdiA-RBD (orange) recognizes its target-cell receptor (yellow), CdiA secretion continues, and FHA-2 (dark green) translocates CdiA-CT (red) into the target-cell. Once in the target-cell periplasm, the CdiA-CT is cleaved after the PT-motif, the entry domain recognizes a specific inner membrane receptor (purple) and the cytotoxic domain is translocated across the inner membrane into the cytosol. (C) Structure of CdiB. CdiB is an OMP β-barrel. Key components like α-helix H1 (blue) and loop L6 (pink) are highlighted [PDB ID 6WIL (Guerin et al., 2020)].