Cargando…
Rhs NADase effectors and their immunity proteins are exchangeable mediators of inter-bacterial competition in Serratia
Many bacterial species use Type VI secretion systems (T6SSs) to deliver anti-bacterial effector proteins into neighbouring bacterial cells, representing an important mechanism of inter-bacterial competition. Specific immunity proteins protect bacteria from the toxic action of their own effectors, wh...
Autores principales: | , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2023
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10539506/ https://www.ncbi.nlm.nih.gov/pubmed/37770429 http://dx.doi.org/10.1038/s41467-023-41751-3 |
_version_ | 1785113514099081216 |
---|---|
author | Hagan, Martin Pankov, Genady Gallegos-Monterrosa, Ramses Williams, David J. Earl, Christopher Buchanan, Grant Hunter, William N. Coulthurst, Sarah J. |
author_facet | Hagan, Martin Pankov, Genady Gallegos-Monterrosa, Ramses Williams, David J. Earl, Christopher Buchanan, Grant Hunter, William N. Coulthurst, Sarah J. |
author_sort | Hagan, Martin |
collection | PubMed |
description | Many bacterial species use Type VI secretion systems (T6SSs) to deliver anti-bacterial effector proteins into neighbouring bacterial cells, representing an important mechanism of inter-bacterial competition. Specific immunity proteins protect bacteria from the toxic action of their own effectors, whilst orphan immunity proteins without a cognate effector may provide protection against incoming effectors from non-self competitors. T6SS-dependent Rhs effectors contain a variable C-terminal toxin domain (CT), with the cognate immunity protein encoded immediately downstream of the effector. Here, we demonstrate that Rhs1 effectors from two strains of Serratia marcescens, the model strain Db10 and clinical isolate SJC1036, possess distinct CTs which both display NAD(P)(+) glycohydrolase activity but belong to different subgroups of NADase from each other and other T6SS-associated NADases. Comparative structural analysis identifies conserved functions required for NADase activity and reveals that unrelated NADase immunity proteins utilise a common mechanism of effector inhibition. By replicating a natural recombination event, we show successful functional exchange of CTs and demonstrate that Db10 encodes an orphan immunity protein which provides protection against T6SS-delivered SJC1036 NADase. Our findings highlight the flexible use of Rhs effectors and orphan immunity proteins during inter-strain competition and the repeated adoption of NADase toxins as weapons against bacterial cells. |
format | Online Article Text |
id | pubmed-10539506 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-105395062023-09-30 Rhs NADase effectors and their immunity proteins are exchangeable mediators of inter-bacterial competition in Serratia Hagan, Martin Pankov, Genady Gallegos-Monterrosa, Ramses Williams, David J. Earl, Christopher Buchanan, Grant Hunter, William N. Coulthurst, Sarah J. Nat Commun Article Many bacterial species use Type VI secretion systems (T6SSs) to deliver anti-bacterial effector proteins into neighbouring bacterial cells, representing an important mechanism of inter-bacterial competition. Specific immunity proteins protect bacteria from the toxic action of their own effectors, whilst orphan immunity proteins without a cognate effector may provide protection against incoming effectors from non-self competitors. T6SS-dependent Rhs effectors contain a variable C-terminal toxin domain (CT), with the cognate immunity protein encoded immediately downstream of the effector. Here, we demonstrate that Rhs1 effectors from two strains of Serratia marcescens, the model strain Db10 and clinical isolate SJC1036, possess distinct CTs which both display NAD(P)(+) glycohydrolase activity but belong to different subgroups of NADase from each other and other T6SS-associated NADases. Comparative structural analysis identifies conserved functions required for NADase activity and reveals that unrelated NADase immunity proteins utilise a common mechanism of effector inhibition. By replicating a natural recombination event, we show successful functional exchange of CTs and demonstrate that Db10 encodes an orphan immunity protein which provides protection against T6SS-delivered SJC1036 NADase. Our findings highlight the flexible use of Rhs effectors and orphan immunity proteins during inter-strain competition and the repeated adoption of NADase toxins as weapons against bacterial cells. Nature Publishing Group UK 2023-09-28 /pmc/articles/PMC10539506/ /pubmed/37770429 http://dx.doi.org/10.1038/s41467-023-41751-3 Text en © The Author(s) 2023 https://creativecommons.org/licenses/by/4.0/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/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Article Hagan, Martin Pankov, Genady Gallegos-Monterrosa, Ramses Williams, David J. Earl, Christopher Buchanan, Grant Hunter, William N. Coulthurst, Sarah J. Rhs NADase effectors and their immunity proteins are exchangeable mediators of inter-bacterial competition in Serratia |
title | Rhs NADase effectors and their immunity proteins are exchangeable mediators of inter-bacterial competition in Serratia |
title_full | Rhs NADase effectors and their immunity proteins are exchangeable mediators of inter-bacterial competition in Serratia |
title_fullStr | Rhs NADase effectors and their immunity proteins are exchangeable mediators of inter-bacterial competition in Serratia |
title_full_unstemmed | Rhs NADase effectors and their immunity proteins are exchangeable mediators of inter-bacterial competition in Serratia |
title_short | Rhs NADase effectors and their immunity proteins are exchangeable mediators of inter-bacterial competition in Serratia |
title_sort | rhs nadase effectors and their immunity proteins are exchangeable mediators of inter-bacterial competition in serratia |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10539506/ https://www.ncbi.nlm.nih.gov/pubmed/37770429 http://dx.doi.org/10.1038/s41467-023-41751-3 |
work_keys_str_mv | AT haganmartin rhsnadaseeffectorsandtheirimmunityproteinsareexchangeablemediatorsofinterbacterialcompetitioninserratia AT pankovgenady rhsnadaseeffectorsandtheirimmunityproteinsareexchangeablemediatorsofinterbacterialcompetitioninserratia AT gallegosmonterrosaramses rhsnadaseeffectorsandtheirimmunityproteinsareexchangeablemediatorsofinterbacterialcompetitioninserratia AT williamsdavidj rhsnadaseeffectorsandtheirimmunityproteinsareexchangeablemediatorsofinterbacterialcompetitioninserratia AT earlchristopher rhsnadaseeffectorsandtheirimmunityproteinsareexchangeablemediatorsofinterbacterialcompetitioninserratia AT buchanangrant rhsnadaseeffectorsandtheirimmunityproteinsareexchangeablemediatorsofinterbacterialcompetitioninserratia AT hunterwilliamn rhsnadaseeffectorsandtheirimmunityproteinsareexchangeablemediatorsofinterbacterialcompetitioninserratia AT coulthurstsarahj rhsnadaseeffectorsandtheirimmunityproteinsareexchangeablemediatorsofinterbacterialcompetitioninserratia |