Please use this identifier to cite or link to this item: https://doi.org/10.21256/zhaw-18121
Publication type: Article in scientific journal
Type of review: Peer review (publication)
Title: Structural and functional diversity inListeriacell wall teichoic acids
Authors: Shen, Yang
Boulos, Samy
Sumrall, Eric
Gerber, Benjamin
Julian-Rodero, Alicia
Eugster, Marcel R.
Fieseler, Lars
Nyström, Laura
Ebert, Marc-Olivier
Loessner, Martin J.
et. al: No
DOI: 10.1074/jbc.M117.813964
10.21256/zhaw-18121
Published in: Journal of Biological Chemistry
Volume(Issue): 292
Issue: 43
Page(s): 17832
Pages to: 17844
Issue Date: 2017
Publisher / Ed. Institution: American Society for Biochemistry and Molecular Biology
ISSN: 0021-9258
1083-351X
Language: English
Subjects: Listeria; Bacteriophage derived endolysin; Carbohydrate structure; Carbohydrate-binding protein; High-performance liquid chromatography (HPLC); Nuclear magnetic resonance (NMR); Surface plasmon resonance (SPR); Teichoic acid; Acetylglucosamine; Cell wall; Listeria; Ribitol; Species specificity; Teichoic acid
Subject (DDC): 572: Biochemistry
Abstract: Wall teichoic acids (WTAs) are the most abundant glycopolymers found on the cell wall of many Gram-positive bacteria, whose diverse surface structures play key roles in multiple biological processes. Despite recent technological advances in glycan analysis, structural elucidation of WTAs remains challenging due to their complex nature. Here, we employed a combination of ultra-performance liquid chromatography-coupled electrospray ionization tandem-MS/MS and NMR to determine the structural complexity of WTAs from Listeria species. We unveiled more than 10 different types of WTA polymers that vary in their linkage and repeating units. Disparity in GlcNAc to ribitol connectivity, as well as variable O-acetylation and glycosylation of GlcNAc contribute to the structural diversity of WTAs. Notably, SPR analysis indicated that constitution of WTA determines the recognition by bacteriophage endolysins. Collectively, these findings provide detailed insight into Listeria cell wall-associated carbohydrates, and will guide further studies on the structure-function relationship of WTAs.
URI: https://digitalcollection.zhaw.ch/handle/11475/18121
Fulltext version: Published version
License (according to publishing contract): CC BY 4.0: Attribution 4.0 International
Departement: Life Sciences and Facility Management
Organisational Unit: Institute of Food and Beverage Innovation (ILGI)
Appears in collections:Publikationen Life Sciences und Facility Management

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Shen, Y., Boulos, S., Sumrall, E., Gerber, B., Julian-Rodero, A., Eugster, M. R., Fieseler, L., Nyström, L., Ebert, M.-O., & Loessner, M. J. (2017). Structural and functional diversity inListeriacell wall teichoic acids. Journal of Biological Chemistry, 292(43), 17832–17844. https://doi.org/10.1074/jbc.M117.813964
Shen, Y. et al. (2017) ‘Structural and functional diversity inListeriacell wall teichoic acids’, Journal of Biological Chemistry, 292(43), pp. 17832–17844. Available at: https://doi.org/10.1074/jbc.M117.813964.
Y. Shen et al., “Structural and functional diversity inListeriacell wall teichoic acids,” Journal of Biological Chemistry, vol. 292, no. 43, pp. 17832–17844, 2017, doi: 10.1074/jbc.M117.813964.
SHEN, Yang, Samy BOULOS, Eric SUMRALL, Benjamin GERBER, Alicia JULIAN-RODERO, Marcel R. EUGSTER, Lars FIESELER, Laura NYSTRÖM, Marc-Olivier EBERT und Martin J. LOESSNER, 2017. Structural and functional diversity inListeriacell wall teichoic acids. Journal of Biological Chemistry. 2017. Bd. 292, Nr. 43, S. 17832–17844. DOI 10.1074/jbc.M117.813964
Shen, Yang, Samy Boulos, Eric Sumrall, Benjamin Gerber, Alicia Julian-Rodero, Marcel R. Eugster, Lars Fieseler, Laura Nyström, Marc-Olivier Ebert, and Martin J. Loessner. 2017. “Structural and Functional Diversity inListeriacell Wall Teichoic Acids.” Journal of Biological Chemistry 292 (43): 17832–44. https://doi.org/10.1074/jbc.M117.813964.
Shen, Yang, et al. “Structural and Functional Diversity inListeriacell Wall Teichoic Acids.” Journal of Biological Chemistry, vol. 292, no. 43, 2017, pp. 17832–44, https://doi.org/10.1074/jbc.M117.813964.


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