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Updated: Jan 24, 2026
Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain
Published on: December 12, 2017
Structural Basis for how Sialoglycan-binding Viridans Streptococci Accommodate Ligands that Exceed the Characterized
KeAndreya M Morrison1, Kole Martin2, Hai Yu3
1Department of Pharmacology, Meharry Medical College, Nashville, TN, US.
None:
During endocardial infections, viridans group streptococci use proteins containing siglec-like binding regions to engage sialic acid-capped O- GalNAc glycans on platelet glycoprotein GPIbα. Much past work used isolated di-, tri-, or tetrasaccharide partial ligands to interrogate this sialoglycan binding. Here, we report the 1.9 Å resolution crystal structure of the Streptococcus gordonii strain M99 siglec-like binding region bound to an L-serine-linked sialyl T antigen (sTa) trisaccharide. The structure demonstrates how trisaccharide extensions are accommodated, with implications for binding larger sialoglycan ligands.
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