Structural basis for recognition of bacterial cell wall teichoic acid by pseudo-symmetric SH3b-like repeats of a viral peptidoglycan hydrolase

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Structural basis for recognition of bacterial cell wall teichoic acid by pseudo-symmetric SH3b-like repeats of a viral peptidoglycan hydrolase. / Shen, Yang; Kalograiaki, Ioanna; Prunotto, Alessio; Dunne, Matthew; Boulos, Samy; Taylor, Nicholas M.I.; Sumrall, Eric T.; Eugster, Marcel R.; Martin, Rebecca; Julian-Rodero, Alicia; Gerber, Benjamin; Leiman, Petr G.; Menéndez, Margarita; Peraro, Matteo Dal; Cañada, Francisco Javier; Loessner, Martin J.

In: Chemical Science, Vol. 12, No. 2, 2021, p. 576-589.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Shen, Y, Kalograiaki, I, Prunotto, A, Dunne, M, Boulos, S, Taylor, NMI, Sumrall, ET, Eugster, MR, Martin, R, Julian-Rodero, A, Gerber, B, Leiman, PG, Menéndez, M, Peraro, MD, Cañada, FJ & Loessner, MJ 2021, 'Structural basis for recognition of bacterial cell wall teichoic acid by pseudo-symmetric SH3b-like repeats of a viral peptidoglycan hydrolase', Chemical Science, vol. 12, no. 2, pp. 576-589. https://doi.org/10.1039/d0sc04394j

APA

Shen, Y., Kalograiaki, I., Prunotto, A., Dunne, M., Boulos, S., Taylor, N. M. I., Sumrall, E. T., Eugster, M. R., Martin, R., Julian-Rodero, A., Gerber, B., Leiman, P. G., Menéndez, M., Peraro, M. D., Cañada, F. J., & Loessner, M. J. (2021). Structural basis for recognition of bacterial cell wall teichoic acid by pseudo-symmetric SH3b-like repeats of a viral peptidoglycan hydrolase. Chemical Science, 12(2), 576-589. https://doi.org/10.1039/d0sc04394j

Vancouver

Shen Y, Kalograiaki I, Prunotto A, Dunne M, Boulos S, Taylor NMI et al. Structural basis for recognition of bacterial cell wall teichoic acid by pseudo-symmetric SH3b-like repeats of a viral peptidoglycan hydrolase. Chemical Science. 2021;12(2):576-589. https://doi.org/10.1039/d0sc04394j

Author

Shen, Yang ; Kalograiaki, Ioanna ; Prunotto, Alessio ; Dunne, Matthew ; Boulos, Samy ; Taylor, Nicholas M.I. ; Sumrall, Eric T. ; Eugster, Marcel R. ; Martin, Rebecca ; Julian-Rodero, Alicia ; Gerber, Benjamin ; Leiman, Petr G. ; Menéndez, Margarita ; Peraro, Matteo Dal ; Cañada, Francisco Javier ; Loessner, Martin J. / Structural basis for recognition of bacterial cell wall teichoic acid by pseudo-symmetric SH3b-like repeats of a viral peptidoglycan hydrolase. In: Chemical Science. 2021 ; Vol. 12, No. 2. pp. 576-589.

Bibtex

@article{a73f7ff185f042c8bb832c11de8e0b4e,
title = "Structural basis for recognition of bacterial cell wall teichoic acid by pseudo-symmetric SH3b-like repeats of a viral peptidoglycan hydrolase",
abstract = "Endolysins are bacteriophage-encoded peptidoglycan hydrolases targeting the cell wall of host bacteria via their cell wall-binding domains (CBDs). The molecular basis for selective recognition of surface carbohydrate ligands by CBDs remains elusive. Here, we describe, in atomic detail, the interaction between the Listeria phage endolysin domain CBD500 and its cell wall teichoic acid (WTA) ligands. We show that 3′O-acetylated GlcNAc residues integrated into the WTA polymer chain are the key epitope recognized by a CBD binding cavity located at the interface of tandem copies of beta-barrel, pseudo-symmetric SH3b-like repeats. This cavity consists of multiple aromatic residues making extensive interactions with two GlcNAc acetyl groups via hydrogen bonds and van der Waals contacts, while permitting the docking of the diastereomorphic ligands. Our multidisciplinary approach tackled an extremely challenging protein-glycopolymer complex and delineated a previously unknown recognition mechanism by which a phage endolysin specifically recognizes and targets WTA, suggesting an adaptable model for regulation of endolysin specificity. This journal is ",
author = "Yang Shen and Ioanna Kalograiaki and Alessio Prunotto and Matthew Dunne and Samy Boulos and Taylor, {Nicholas M.I.} and Sumrall, {Eric T.} and Eugster, {Marcel R.} and Rebecca Martin and Alicia Julian-Rodero and Benjamin Gerber and Leiman, {Petr G.} and Margarita Men{\'e}ndez and Peraro, {Matteo Dal} and Ca{\~n}ada, {Francisco Javier} and Loessner, {Martin J.}",
year = "2021",
doi = "10.1039/d0sc04394j",
language = "English",
volume = "12",
pages = "576--589",
journal = "Chemical Science",
issn = "2041-6520",
publisher = "Royal Society of Chemistry",
number = "2",

}

RIS

TY - JOUR

T1 - Structural basis for recognition of bacterial cell wall teichoic acid by pseudo-symmetric SH3b-like repeats of a viral peptidoglycan hydrolase

AU - Shen, Yang

AU - Kalograiaki, Ioanna

AU - Prunotto, Alessio

AU - Dunne, Matthew

AU - Boulos, Samy

AU - Taylor, Nicholas M.I.

AU - Sumrall, Eric T.

AU - Eugster, Marcel R.

AU - Martin, Rebecca

AU - Julian-Rodero, Alicia

AU - Gerber, Benjamin

AU - Leiman, Petr G.

AU - Menéndez, Margarita

AU - Peraro, Matteo Dal

AU - Cañada, Francisco Javier

AU - Loessner, Martin J.

PY - 2021

Y1 - 2021

N2 - Endolysins are bacteriophage-encoded peptidoglycan hydrolases targeting the cell wall of host bacteria via their cell wall-binding domains (CBDs). The molecular basis for selective recognition of surface carbohydrate ligands by CBDs remains elusive. Here, we describe, in atomic detail, the interaction between the Listeria phage endolysin domain CBD500 and its cell wall teichoic acid (WTA) ligands. We show that 3′O-acetylated GlcNAc residues integrated into the WTA polymer chain are the key epitope recognized by a CBD binding cavity located at the interface of tandem copies of beta-barrel, pseudo-symmetric SH3b-like repeats. This cavity consists of multiple aromatic residues making extensive interactions with two GlcNAc acetyl groups via hydrogen bonds and van der Waals contacts, while permitting the docking of the diastereomorphic ligands. Our multidisciplinary approach tackled an extremely challenging protein-glycopolymer complex and delineated a previously unknown recognition mechanism by which a phage endolysin specifically recognizes and targets WTA, suggesting an adaptable model for regulation of endolysin specificity. This journal is

AB - Endolysins are bacteriophage-encoded peptidoglycan hydrolases targeting the cell wall of host bacteria via their cell wall-binding domains (CBDs). The molecular basis for selective recognition of surface carbohydrate ligands by CBDs remains elusive. Here, we describe, in atomic detail, the interaction between the Listeria phage endolysin domain CBD500 and its cell wall teichoic acid (WTA) ligands. We show that 3′O-acetylated GlcNAc residues integrated into the WTA polymer chain are the key epitope recognized by a CBD binding cavity located at the interface of tandem copies of beta-barrel, pseudo-symmetric SH3b-like repeats. This cavity consists of multiple aromatic residues making extensive interactions with two GlcNAc acetyl groups via hydrogen bonds and van der Waals contacts, while permitting the docking of the diastereomorphic ligands. Our multidisciplinary approach tackled an extremely challenging protein-glycopolymer complex and delineated a previously unknown recognition mechanism by which a phage endolysin specifically recognizes and targets WTA, suggesting an adaptable model for regulation of endolysin specificity. This journal is

U2 - 10.1039/d0sc04394j

DO - 10.1039/d0sc04394j

M3 - Journal article

C2 - 34163788

AN - SCOPUS:85099725495

VL - 12

SP - 576

EP - 589

JO - Chemical Science

JF - Chemical Science

SN - 2041-6520

IS - 2

ER -

ID: 256882397