Structural Basis for Sialoglycan Binding by the Streptococcus sanguinis SrpA Adhesin.

The Journal of Biological Chemistry
Barbara A BensingTina M Iverson

Abstract

Streptococcus sanguinisis a leading cause of infective endocarditis, a life-threatening infection of the cardiovascular system. An important interaction in the pathogenesis of infective endocarditis is attachment of the organisms to host platelets.S. sanguinisexpresses a serine-rich repeat adhesin, SrpA, similar in sequence to platelet-binding adhesins associated with increased virulence in this disease. In this study, we determined the first crystal structure of the putative binding region of SrpA (SrpABR) both unliganded and in complex with a synthetic disaccharide ligand at 1.8 and 2.0 Å resolution, respectively. We identified a conserved Thr-Arg motif that orients the sialic acid moiety and is required for binding to platelet monolayers. Furthermore, we propose that sequence insertions in closely related family members contribute to the modulation of structural and functional properties, including the quaternary structure, the tertiary structure, and the ligand-binding site.

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Citations

Dec 21, 2016·Infection and Immunity·Anirudh K SinghSamantha J King
Dec 11, 2019·Proceedings of the National Academy of Sciences of the United States of America·Fiona WhelanJennifer R Potts
May 1, 2019·Gut Microbes·Dimitrios LatousakisNathalie Juge
Mar 7, 2018·Proceedings of the National Academy of Sciences of the United States of America·Saannya SequeiraNathalie Juge
Oct 16, 2020·Nature Communications·David VizarragaDavid Aparicio
Feb 2, 2021·The EMBO Journal·Nina M van SorgeAlex J McCarthy

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