6P4N

Salmonella typhi PltB Homopentamer with Neu5Ac-alpha-2-6-Gal-beta-1-4-GlcNAc Glycans

Summary for 6P4N

• Entry DOI: 10.2210/pdb6p4n/pdb
• Related PRD ID: PRD_900046
• Descriptor: Putative pertussis-like toxin subunit, N-acetyl-alpha-neuraminic acid-(2-6)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: pltb, toxin
• Biological source: Salmonella enterica subsp. enterica serovar Typhi str. CT18
• Total number of polymer chains: 5
• Total formula weight: 83550.82

Authors

Nguyen, T.,Milano, S.K.,Hillpot, E.C.,Yang, Y.A.,Song, J. (deposition date: 2019-05-28, release date: 2020-03-25, Last modification date: 2024-10-30)

Primary citation

Lee, S.,Yang, Y.A.,Milano, S.K.,Nguyen, T.,Ahn, C.,Sim, J.H.,Thompson, A.J.,Hillpot, E.C.,Yoo, G.,Paulson, J.C.,Song, J.
Salmonella Typhoid Toxin PltB Subunit and Its Non-typhoidal Salmonella Ortholog Confer Differential Host Adaptation and Virulence.
Cell Host Microbe, 27:937-949.e6, 2020

PubMed Abstract: Typhoidal and non-typhoidal Salmonelleae (NTS) cause typhoid fever and gastroenteritis, respectively, in humans. Salmonella typhoid toxin contributes to typhoid disease progression and chronic infection, but little is known about the role of its NTS ortholog. We found that typhoid toxin and its NTS ortholog induce different clinical presentations. The PltB subunit of each toxin exhibits different glycan-binding preferences that correlate with glycan expression profiles of host cells targeted by each bacterium at the primary infection or intoxication sites. Through co-crystal structures of PltB subunits bound to specific glycan receptor moieties, we show that they induce markedly different glycan-binding preferences and virulence outcomes. Furthermore, immunization with the NTS S. Javiana or its toxin offers cross-reactive protection against lethal-dose typhoid toxin challenge. Cumulatively, these results offer insights into the evolution of host adaptations in Salmonella AB toxins, their cell and tissue tropisms, and the design for improved typhoid vaccines and therapeutics.

PubMed: 32396840
DOI: 10.1016/j.chom.2020.04.005

Experimental method

X-RAY DIFFRACTION (1.7 Å)