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The type VI secretion system protein AsaA in Acinetobacter baumannii is a periplasmic protein physically interacting with TssM and required for T6SS assembly

Type VI secretion system (T6SS) is described as a macromolecular secretion machine that is utilized for bacterial competition. The gene clusters encoding T6SS are composed of core tss genes and tag genes. However, the clusters differ greatly in different pathogens due to the great changes accumulate...

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Autores principales: Li, Lei, Wang, Yi-Nuo, Jia, Hong-Bing, Wang, Ping, Dong, Jun-Fang, Deng, Juan, Lu, Feng-Min, Zou, Qing-Hua
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6602968/
https://www.ncbi.nlm.nih.gov/pubmed/31263148
http://dx.doi.org/10.1038/s41598-019-45875-9
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author Li, Lei
Wang, Yi-Nuo
Jia, Hong-Bing
Wang, Ping
Dong, Jun-Fang
Deng, Juan
Lu, Feng-Min
Zou, Qing-Hua
author_facet Li, Lei
Wang, Yi-Nuo
Jia, Hong-Bing
Wang, Ping
Dong, Jun-Fang
Deng, Juan
Lu, Feng-Min
Zou, Qing-Hua
author_sort Li, Lei
collection PubMed
description Type VI secretion system (T6SS) is described as a macromolecular secretion machine that is utilized for bacterial competition. The gene clusters encoding T6SS are composed of core tss genes and tag genes. However, the clusters differ greatly in different pathogens due to the great changes accumulated during the long-term evolution. In this work, we identified a novel hypothetical periplasmic protein designated as AsaA which is encoded by the first gene of the T6SS cluster in the genus Acinetobacter. By constructing asaA mutant, we delineated its relative contributions to bacterial competition and secretion of T6SS effector Hcp. Subsequently, we studied the localization of AsaA and potential proteins that may have interactions with AsaA. Our results showed that AsaA in Acinetobacter baumannii (A. baumannii) localized in the bacterial periplasmic space. Results based on bacterial two-hybrid system and protein pull-down assays indicated that it was most likely to affect the assembly or stability of T6SS by interacting with the T6SS core protein TssM. Collectively, our findings of AsaA is most likely a key step in understanding of the T6SS functions in A. baumannii.
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spelling pubmed-66029682019-07-14 The type VI secretion system protein AsaA in Acinetobacter baumannii is a periplasmic protein physically interacting with TssM and required for T6SS assembly Li, Lei Wang, Yi-Nuo Jia, Hong-Bing Wang, Ping Dong, Jun-Fang Deng, Juan Lu, Feng-Min Zou, Qing-Hua Sci Rep Article Type VI secretion system (T6SS) is described as a macromolecular secretion machine that is utilized for bacterial competition. The gene clusters encoding T6SS are composed of core tss genes and tag genes. However, the clusters differ greatly in different pathogens due to the great changes accumulated during the long-term evolution. In this work, we identified a novel hypothetical periplasmic protein designated as AsaA which is encoded by the first gene of the T6SS cluster in the genus Acinetobacter. By constructing asaA mutant, we delineated its relative contributions to bacterial competition and secretion of T6SS effector Hcp. Subsequently, we studied the localization of AsaA and potential proteins that may have interactions with AsaA. Our results showed that AsaA in Acinetobacter baumannii (A. baumannii) localized in the bacterial periplasmic space. Results based on bacterial two-hybrid system and protein pull-down assays indicated that it was most likely to affect the assembly or stability of T6SS by interacting with the T6SS core protein TssM. Collectively, our findings of AsaA is most likely a key step in understanding of the T6SS functions in A. baumannii. Nature Publishing Group UK 2019-07-01 /pmc/articles/PMC6602968/ /pubmed/31263148 http://dx.doi.org/10.1038/s41598-019-45875-9 Text en © The Author(s) 2019 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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Li, Lei
Wang, Yi-Nuo
Jia, Hong-Bing
Wang, Ping
Dong, Jun-Fang
Deng, Juan
Lu, Feng-Min
Zou, Qing-Hua
The type VI secretion system protein AsaA in Acinetobacter baumannii is a periplasmic protein physically interacting with TssM and required for T6SS assembly
title The type VI secretion system protein AsaA in Acinetobacter baumannii is a periplasmic protein physically interacting with TssM and required for T6SS assembly
title_full The type VI secretion system protein AsaA in Acinetobacter baumannii is a periplasmic protein physically interacting with TssM and required for T6SS assembly
title_fullStr The type VI secretion system protein AsaA in Acinetobacter baumannii is a periplasmic protein physically interacting with TssM and required for T6SS assembly
title_full_unstemmed The type VI secretion system protein AsaA in Acinetobacter baumannii is a periplasmic protein physically interacting with TssM and required for T6SS assembly
title_short The type VI secretion system protein AsaA in Acinetobacter baumannii is a periplasmic protein physically interacting with TssM and required for T6SS assembly
title_sort type vi secretion system protein asaa in acinetobacter baumannii is a periplasmic protein physically interacting with tssm and required for t6ss assembly
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6602968/
https://www.ncbi.nlm.nih.gov/pubmed/31263148
http://dx.doi.org/10.1038/s41598-019-45875-9
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