Structural and mechanistic basis of capsule O-acetylation in Neisseria meningitidis serogroup A

Neisseria meningitidis capsular polysaccharide (CPS) is a major virulence factor and vaccine formulations against Neisseria meningitidis serogroup A (NmA) contain O-acetylated CPS. Here, the authors provide mechanistic insights into CPS O-acetylation in NmA by determining the crystal structure of th...

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Autores principales:	Timm Fiebig, Johannes T. Cramer, Andrea Bethe, Petra Baruch, Ute Curth, Jana I. Führing, Falk F. R. Buettner, Ulrich Vogel, Mario Schubert, Roman Fedorov, Martina Mühlenhoff
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/e72fba9673214d1d84ba89818eb3a079
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spelling	oai:doaj.org-article:e72fba9673214d1d84ba89818eb3a0792021-12-02T17:25:35ZStructural and mechanistic basis of capsule O-acetylation in Neisseria meningitidis serogroup A10.1038/s41467-020-18464-y2041-1723https://doaj.org/article/e72fba9673214d1d84ba89818eb3a0792020-09-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-18464-yhttps://doaj.org/toc/2041-1723Neisseria meningitidis capsular polysaccharide (CPS) is a major virulence factor and vaccine formulations against Neisseria meningitidis serogroup A (NmA) contain O-acetylated CPS. Here, the authors provide mechanistic insights into CPS O-acetylation in NmA by determining the crystal structure of the O-acetyltransferase CsaC and NMR measurements further reveal that the CsaC-mediated reaction is regioselective for O3 and that the O4 modification results from spontaneous O-acetyl migration.Timm FiebigJohannes T. CramerAndrea BethePetra BaruchUte CurthJana I. FühringFalk F. R. BuettnerUlrich VogelMario SchubertRoman FedorovMartina MühlenhoffNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-12 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Timm Fiebig Johannes T. Cramer Andrea Bethe Petra Baruch Ute Curth Jana I. Führing Falk F. R. Buettner Ulrich Vogel Mario Schubert Roman Fedorov Martina Mühlenhoff Structural and mechanistic basis of capsule O-acetylation in Neisseria meningitidis serogroup A
description	Neisseria meningitidis capsular polysaccharide (CPS) is a major virulence factor and vaccine formulations against Neisseria meningitidis serogroup A (NmA) contain O-acetylated CPS. Here, the authors provide mechanistic insights into CPS O-acetylation in NmA by determining the crystal structure of the O-acetyltransferase CsaC and NMR measurements further reveal that the CsaC-mediated reaction is regioselective for O3 and that the O4 modification results from spontaneous O-acetyl migration.
format	article
author	Timm Fiebig Johannes T. Cramer Andrea Bethe Petra Baruch Ute Curth Jana I. Führing Falk F. R. Buettner Ulrich Vogel Mario Schubert Roman Fedorov Martina Mühlenhoff
author_facet	Timm Fiebig Johannes T. Cramer Andrea Bethe Petra Baruch Ute Curth Jana I. Führing Falk F. R. Buettner Ulrich Vogel Mario Schubert Roman Fedorov Martina Mühlenhoff
author_sort	Timm Fiebig
title	Structural and mechanistic basis of capsule O-acetylation in Neisseria meningitidis serogroup A
title_short	Structural and mechanistic basis of capsule O-acetylation in Neisseria meningitidis serogroup A
title_full	Structural and mechanistic basis of capsule O-acetylation in Neisseria meningitidis serogroup A
title_fullStr	Structural and mechanistic basis of capsule O-acetylation in Neisseria meningitidis serogroup A
title_full_unstemmed	Structural and mechanistic basis of capsule O-acetylation in Neisseria meningitidis serogroup A
title_sort	structural and mechanistic basis of capsule o-acetylation in neisseria meningitidis serogroup a
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/e72fba9673214d1d84ba89818eb3a079
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Structural and mechanistic basis of capsule O-acetylation in Neisseria meningitidis serogroup A

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