Cargando…
Arginine glycosylation enhances methylglyoxal detoxification
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 t...
Autores principales: | , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7884692/ https://www.ncbi.nlm.nih.gov/pubmed/33589708 http://dx.doi.org/10.1038/s41598-021-83437-0 |
_version_ | 1783651462729957376 |
---|---|
author | El Qaidi, Samir Scott, Nichollas E. Hardwidge, Philip R. |
author_facet | El Qaidi, Samir Scott, Nichollas E. Hardwidge, Philip R. |
author_sort | El Qaidi, Samir |
collection | PubMed |
description | 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 | Online Article Text |
id | pubmed-7884692 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-78846922021-02-16 Arginine glycosylation enhances methylglyoxal detoxification El Qaidi, Samir Scott, Nichollas E. Hardwidge, Philip R. Sci Rep Article 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. Nature Publishing Group UK 2021-02-15 /pmc/articles/PMC7884692/ /pubmed/33589708 http://dx.doi.org/10.1038/s41598-021-83437-0 Text en © The Author(s) 2021 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article El Qaidi, Samir Scott, Nichollas E. Hardwidge, Philip R. Arginine glycosylation enhances methylglyoxal detoxification |
title | 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_short | Arginine glycosylation enhances methylglyoxal detoxification |
title_sort | arginine glycosylation enhances methylglyoxal detoxification |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7884692/ https://www.ncbi.nlm.nih.gov/pubmed/33589708 http://dx.doi.org/10.1038/s41598-021-83437-0 |
work_keys_str_mv | AT elqaidisamir arginineglycosylationenhancesmethylglyoxaldetoxification AT scottnichollase arginineglycosylationenhancesmethylglyoxaldetoxification AT hardwidgephilipr arginineglycosylationenhancesmethylglyoxaldetoxification |