Arginine glycosylation enhances methylglyoxal detoxification

Abstract Type III secretion system effector proteins have primarily been characterized for their interactions with host cell proteins and their ability to disrupt host signaling pathways. We are testing the hypothesis that some effectors are active within the bacterium, where they modulate bacterial...

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Autores principales:	Samir El Qaidi, Nichollas E. Scott, Philip R. Hardwidge
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/c9fd04c2a13f4bf293ff61a5d8363132
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spelling	oai:doaj.org-article:c9fd04c2a13f4bf293ff61a5d83631322021-12-02T14:03:46ZArginine glycosylation enhances methylglyoxal detoxification10.1038/s41598-021-83437-02045-2322https://doaj.org/article/c9fd04c2a13f4bf293ff61a5d83631322021-02-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-83437-0https://doaj.org/toc/2045-2322Abstract Type III secretion system effector proteins have primarily been characterized for their interactions with host cell proteins and their ability to disrupt host signaling pathways. We are testing the hypothesis that some effectors are active within the bacterium, where they modulate bacterial signal transduction and physiology. We previously determined that the Citrobacter rodentium effector NleB possesses an intra-bacterial glycosyltransferase activity that increases glutathione synthetase activity to protect the bacterium from oxidative stress. Here we investigated the potential intra-bacterial activities of NleB orthologs in Salmonella enterica and found that SseK1 and SseK3 mediate resistance to methylglyoxal. SseK1 glycosylates specific arginine residues on four proteins involved in methylglyoxal detoxification, namely GloA (R9), GloB (R190), GloC (R160), and YajL (R149). SseK1-mediated Arg-glycosylation of these four proteins significantly enhances their catalytic activity, thus providing another important example of the intra-bacterial activities of type three secretion system effector proteins. These data are also the first demonstration that a Salmonella T3SS effector is active within the bacterium.Samir El QaidiNichollas E. ScottPhilip R. HardwidgeNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-11 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Samir El Qaidi Nichollas E. Scott Philip R. Hardwidge Arginine glycosylation enhances methylglyoxal detoxification
description	Abstract Type III secretion system effector proteins have primarily been characterized for their interactions with host cell proteins and their ability to disrupt host signaling pathways. We are testing the hypothesis that some effectors are active within the bacterium, where they modulate bacterial signal transduction and physiology. We previously determined that the Citrobacter rodentium effector NleB possesses an intra-bacterial glycosyltransferase activity that increases glutathione synthetase activity to protect the bacterium from oxidative stress. Here we investigated the potential intra-bacterial activities of NleB orthologs in Salmonella enterica and found that SseK1 and SseK3 mediate resistance to methylglyoxal. SseK1 glycosylates specific arginine residues on four proteins involved in methylglyoxal detoxification, namely GloA (R9), GloB (R190), GloC (R160), and YajL (R149). SseK1-mediated Arg-glycosylation of these four proteins significantly enhances their catalytic activity, thus providing another important example of the intra-bacterial activities of type three secretion system effector proteins. These data are also the first demonstration that a Salmonella T3SS effector is active within the bacterium.
format	article
author	Samir El Qaidi Nichollas E. Scott Philip R. Hardwidge
author_facet	Samir El Qaidi Nichollas E. Scott Philip R. Hardwidge
author_sort	Samir El Qaidi
title	Arginine glycosylation enhances methylglyoxal detoxification
title_short	Arginine glycosylation enhances methylglyoxal detoxification
title_full	Arginine glycosylation enhances methylglyoxal detoxification
title_fullStr	Arginine glycosylation enhances methylglyoxal detoxification
title_full_unstemmed	Arginine glycosylation enhances methylglyoxal detoxification
title_sort	arginine glycosylation enhances methylglyoxal detoxification
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/c9fd04c2a13f4bf293ff61a5d8363132
work_keys_str_mv	AT samirelqaidi arginineglycosylationenhancesmethylglyoxaldetoxification AT nichollasescott arginineglycosylationenhancesmethylglyoxaldetoxification AT philiprhardwidge arginineglycosylationenhancesmethylglyoxaldetoxification
_version_	1718392109120094208

Arginine glycosylation enhances methylglyoxal detoxification

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