7SO7

Novel structural insights for a pair of monoclonal antibodies recognizing non-overlapping epitopes of the glucosyltransferase domain of Clostridium difficile toxin B

Summary for 7SO7

• Entry DOI: 10.2210/pdb7so7/pdb
• Related: 7SO5
• Descriptor: Toxin B, Fab B1 HC, FAB B1 LC (3 entities in total)
• Functional Keywords: antibody, toxin, tcdb, epitope, clostridium difficile toxin, toxin-immune system complex, toxin/immune system
• Biological source: Clostridioides difficile (Peptoclostridium difficile); More
• Total number of polymer chains: 6
• Total formula weight: 217537.51

Authors

Liu, J. (deposition date: 2021-10-29, release date: 2022-05-11, Last modification date: 2023-10-18)

Primary citation

Liu, J.,Kothe, M.,Zhang, J.,Oloo, E.,Stegalkina, S.,Mundle, S.T.,Li, L.,Zhang, J.,Cole, L.E.,Barone, L.,Biemann, H.P.,Kleanthous, H.,Anosova, N.G.,Anderson, S.F.
Novel structural insights for a pair of monoclonal antibodies recognizing non-overlapping epitopes of the glucosyltransferase domain of Clostridium difficile toxin B.
Curr Res Struct Biol, 4:96-105, 2022

PubMed Abstract: toxins are the primary causative agents for hospital-acquired diarrhea and pseudomembranous colitis. Numerous monoclonal antibodies (mAbs) targeting different domains of toxin have been reported. Here we report the crystal structures of two mAbs, B1 and B2, in complex with the glycosyltransferase domain (GTD) of the toxin B (TcdB). B2 bound to the N-terminal 4 helix bundle of the GTD, a conserved membrane localization domain (MLD) found in the large clostridial glycosylating toxin family implicated in targeting plasma membrane. B1 bound to a distinct epitope at the hinge region between the MLD and the catalytic subdomain of the GTD. Functional studies revealed the potency of these mAbs and to be synergistic when given in combination.

PubMed: 35469152
DOI: 10.1016/j.crstbi.2022.03.003

Experimental method

X-RAY DIFFRACTION (3.59 Å)