Structural basis for recognition of bacterial cell wall teichoic acid by pseudo-symmetric SH3b-like repeats of a viral peptidoglycan hydrolase
| Autor: | Benjamin Gerber, Martin J. Loessner, Francisco Javier Cañada, Matthew Dunne, Matteo Dal Peraro, Ioanna Kalograiaki, Alicia Julian-Rodero, Yang Shen, Eric T. Sumrall, Rebecca Martin, Samy Boulos, Margarita Menéndez, Marcel R. Eugster, Petr G. Leiman, Alessio Prunotto, Nicholas M.I. Taylor |
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| Přispěvatelé: | Swiss National Science Foundation, Ministerio de Ciencia, Innovación y Universidades (España), Instituto de Salud Carlos III, Shen, Yang, Kalograiaki, Ioanna, Prunotto, Alessio, Dunne, M, Boulos, Samy, Taylor, Nicholas M. I., Sumrall, E, Leiman, P, Menéndez, Margarita, Dal Peraro, Matteo, Cañada, F. Javier, Loessner, Martin, Shen, Yang [0000-0003-4278-1477], Kalograiaki, Ioanna [0000-0001-7950-2334], Prunotto, Alessio [0000-0002-6425-964X], Dunne, M [0000-0002-2329-8183], Boulos, Samy [0000-0002-0442-2505], Taylor, Nicholas M. I. [0000-0003-0761-4921], Sumrall, E [0000-0001-9181-6918], Leiman, P [0000-0002-9091-0918], Menéndez, Margarita [0000-0002-3267-4443], Dal Peraro, Matteo [0000-0002-2973-3975], Cañada, F. Javier [000-0003-4462-1469], Loessner, Martin [0000-0002-8162-2631] |
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
listeria
binding o-acetylation high-affinity domain Lysin Epitope Bacterial cell structure Cell wall 03 medical and health sciences chemistry.chemical_compound phage endolysins transfer difference nmr 030304 developmental biology 0303 health sciences Teichoic acid biology 030306 microbiology crystal-structure General Chemistry biology.organism_classification 3. Good health Chemistry Biochemistry chemistry Docking (molecular) bacteriophage endolysins Peptidoglycan protein Bacteria |
| Zdroj: | Chemical Science, 12 (2) Chemical Science Digital.CSIC. Repositorio Institucional del CSIC instname |
| Popis: | 14 p.-6 fig.-1 tab. 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 30O-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, pseudosymmetric 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. E. T. S. has been supported by the Swiss National Science Foundation (SNF) grant 310030_156947/1. F. J. C.and M. M. have been supported by the Spanish Ministry of Science Innovation and Universities and FEDER funding (grants RTI2018-094751-B-C22 and BFU2015-70072R) and CIBERES, an initiative from the Spanish Institute of Health Carlos III. |
| Databáze: | OpenAIRE |
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