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Molecular and structural recognition of Listeria cell‐wall glycopolymers by bacteriophage‐encoded SH3b domains
Author(s) -
Shen Yang,
Kalograiaki Ioanna,
Prunotto Alessio,
Dunne Matthew,
Sumrall Eric,
Cañada Francisco Javier,
Loessner Martin
Publication year - 2018
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2018.32.1_supplement.544.10
Subject(s) - teichoic acid , biochemistry , structural similarity , lysin , surface plasmon resonance , bacteriophage , binding selectivity , biology , glycan , binding site , glycosylation , computational biology , chemistry , peptidoglycan , cell wall , escherichia coli , gene , glycoprotein , materials science , nanoparticle , nanotechnology
Targeting carbohydrate recognition plays a key role in multiple biological processes across all kingdoms. SH3b (or bacterial Src homology 3) domain is known as a conserved carbohydrate‐binding module that is responsible for carbohydrate recognition. However, the molecular and structural mechanisms underlying SH3b‐carborhydrate interaction remain elusive. Previously, we reported that three phage‐encoded SH3b domains (termed CBD500, CBDP35 and CBD025) exhibit distinct binding patterns that correlate with structural variations in Listeria wall teichoic acids (WTAs, or glycosylated polyribitol phosphate). Here, we use CBD500 to investigate how it recognizes specific carbohydrate ligand displayed on the bacterial surface. We unveil the contribution of glycosylation and O‐acetylation of WTA polymers to the binding by surface plasmon resonance analysis. Saturation Transfer Difference (STD)‐NMR further substantiates that disparity in GlcNAc to ribitol connectivity, O ‐acteyl group, and glycosylated GlcNAc determine the binding specificity. Crystallography, epitope mapping and docking studies identify key residues that form a binding groove (including Phe175, Trp 198, Asn248, and Ser249) mediating CBD500‐WTA interactions, which are validated by site‐directed mutagenesis. This is the first report providing structural insights into the interactions between SH3b and native WTA polymer, thus guiding further studies on structure‐function relationship of SH3b‐carbohydrate complex, as well as support the potential use of endolysins as novel antimicrobials. This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .