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Insights in the recognition of Listeria cell wall teichoic acids by a phage-derived cell wall binding module

AuthorsKalograiaki, Ioanna; Shen, Yang; Menéndez, Margarita ; Prunotto, Alessio; Hernández, Noelia; Dal Peraro, Matteo; Cañada, F. Javier ; Loessner, Martin
Issue Date16-Jul-2019
Citation42rd Congress of the Spanish Biochemical and Molecular Biology Society (2019)
AbstractEndolysins are phage-encoded peptidoglycan hydrolases able to degrade the cell-wall of bacterial hosts from the inside and the outside. Often they are modular enzymes bearing separate recognition and catalytic functions. Susceptibility to lytic activity depends on the selectivity of their cell wall-binding domain (CBD) frequently a carbohydrate-recognition domain. As significant example the CBD of the phage endolysin Ply500 (CBD500) exhibits binding patterns that correlate with structural variations in wall teichoic acids (WTAs) of Listeria spp. their target bacteria [1]. Yet atomic scale insights in this interaction remain challenging to obtain due to the extraordinary heterogeneity of these glycopolymers in terms of length GlcNAc/ribitol connectivity mutable O-acetylation or further hexose substitution of the GlcNAc unit. In this work we employed a multifaceted strategy in order to decipher the CBD500 fine sugar specificity and WTA recognition mechanism from both the ligand and protein perspectives. Saturation Transfer Difference (STD) NMR of CBD500-complexes with a panel of native and mutant WTAs highlighted the importance of GlcNAc 3¿O-acetylation and the relevant contributions of hexose substitutions in binding. ¿Blind¿ molecular docking on the X-ray structure of CBD500 allowed us to propose the WTA binding site and the putative interacting groups further assessed by site-directed mutagenesis. STD NMR-driven molecular dynamic simulations and isothermal titration calorimetry (ITC) aided to model the CBD500 interaction with targeted WTA and analyze the H-bond network as well as hydrophobic interactions established. This pioneer study unveiled the previously unknown recognition mechanism between CBD500 and Listeria native WTA polymers thus guiding further studies aiming to decipher the regulation of endolysin specificity.
DescriptionSEBBM19madrid, Madrid on 16-19th July 2019, G05-13-P7 f. -- https://congresosebbm.madrid2019.es/
Appears in Collections:(CIB) Comunicaciones congresos
(IQFR) Comunicaciones congresos
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