Origins of glycan selectivity in streptococcal Siglec-like adhesins suggest mechanisms of receptor adaptation

Barbara A. Bensing, Haley E. Stubbs, Rupesh Agarwal, Izumi Yamakawa, Kelvin Luong, Kemal Solakyildirim, Hai Yu, Azadeh Hadadianpour, Manuel A. Castro, Kevin P. Fialkowski, KeAndreya M. Morrison, Zdzislaw Wawrzak, Xi Chen, Carlito B. Lebrilla, Jerome Baudry, Jeremy C. Smith, Paul M. Sullam and T. M. Iverson ()
Additional contact information
Barbara A. Bensing: University of California
Haley E. Stubbs: Vanderbilt University
Rupesh Agarwal: University of Tennessee/Oak Ridge National Laboratory, Center for Molecular Biophysics, Biosciences Division, Oak Ridge National Laboratory
Izumi Yamakawa: Vanderbilt University
Kelvin Luong: Vanderbilt University
Kemal Solakyildirim: Erzincan Binali Yildirim University
Hai Yu: University of California
Azadeh Hadadianpour: Vanderbilt University
Manuel A. Castro: Vanderbilt University
Kevin P. Fialkowski: Vanderbilt University
KeAndreya M. Morrison: Meharry Medical College
Zdzislaw Wawrzak: Northwestern University
Xi Chen: University of California
Carlito B. Lebrilla: University of California
Jerome Baudry: The University of Alabama in Huntsville
Jeremy C. Smith: University of Tennessee/Oak Ridge National Laboratory, Center for Molecular Biophysics, Biosciences Division, Oak Ridge National Laboratory
Paul M. Sullam: University of California
T. M. Iverson: Vanderbilt University

Nature Communications, 2022, vol. 13, issue 1, 1-14

Abstract: Abstract Bacterial binding to host receptors underlies both commensalism and pathogenesis. Many streptococci adhere to protein-attached carbohydrates expressed on cell surfaces using Siglec-like binding regions (SLBRs). The precise glycan repertoire recognized may dictate whether the organism is a strict commensal versus a pathogen. However, it is currently not clear what drives receptor selectivity. Here, we use five representative SLBRs and identify regions of the receptor binding site that are hypervariable in sequence and structure. We show that these regions control the identity of the preferred carbohydrate ligand using chimeragenesis and single amino acid substitutions. We further evaluate how the identity of the preferred ligand affects the interaction with glycoprotein receptors in human saliva and plasma samples. As point mutations can change the preferred human receptor, these studies suggest how streptococci may adapt to changes in the environmental glycan repertoire.

Date: 2022
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DOI: 10.1038/s41467-022-30509-y

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