Pseudomonas aeruginosa T6SS-mediated molybdate transport contributes to bacterial competition during anaerobiosis

Type VI secretion system (T6SS) is widely distributed in Gram-negative bacteria and functions as a versatile protein export machinery that translocates effectors into eukaryotic or prokaryotic target cells. Growing evidence indicates that T6SS can deliver several effectors to promote bacterial survi...

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Published inCell reports (Cambridge) Vol. 35; no. 2; p. 108957
Main Authors Wang, Tietao, Du, Xiao, Ji, Linxuan, Han, Yuying, Dang, Jing, Wen, Jing, Wang, Yarong, Pu, Qinqin, Wu, Min, Liang, Haihua
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 13.04.2021
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Abstract Type VI secretion system (T6SS) is widely distributed in Gram-negative bacteria and functions as a versatile protein export machinery that translocates effectors into eukaryotic or prokaryotic target cells. Growing evidence indicates that T6SS can deliver several effectors to promote bacterial survival in harmful environments through metal ion acquisition. Here, we report that the Pseudomonas aeruginosa H2-T6SS mediates molybdate (MoO42−) acquisition by secretion of a molybdate-binding protein, ModA. The expression of H2-T6SS genes is activated by the master regulator Anr and anaerobiosis. We also identified a ModA-binding protein, IcmP, an insulin-cleaving metalloproteinase outer membrane protein. The T6SS-ModA-IcmP system provides P. aeruginosa with a growth advantage in bacterial competition under anaerobic conditions and plays an important role in bacterial virulence. Overall, this study clarifies the role of T6SS in secretion of an anion-binding protein, emphasizing the fundamental importance of this bacterium using T6SS-mediated molybdate uptake to adapt to complex environmental conditions. [Display omitted] •H2-T6SS mediates molybdate acquisition by secretion of ModA•Expression of H2-T6SS is activated by the master regulator Anr and anaerobiosis•ModA interacts with the outer membrane protein IcmP and uses it to deliver molybdate•The T6SS-ModA-IcmP system plays a role for P. aeruginosa in bacterial competition Wang et al. show that P. aeruginosa H2-T6SS secretes a molybdate-binding protein, ModA, which cooperates with IcmP for molybdate acquisition during anaerobiosis. The T6SS-ModA-IcmP system provides P. aeruginosa growth advantage in bacterial competition under anaerobic conditions and plays a role in bacterial virulence.
AbstractList Type VI secretion system (T6SS) is widely distributed in Gram-negative bacteria and functions as a versatile protein export machinery that translocates effectors into eukaryotic or prokaryotic target cells. Growing evidence indicates that T6SS can deliver several effectors to promote bacterial survival in harmful environments through metal ion acquisition. Here, we report that the Pseudomonas aeruginosa H2-T6SS mediates molybdate (MoO42−) acquisition by secretion of a molybdate-binding protein, ModA. The expression of H2-T6SS genes is activated by the master regulator Anr and anaerobiosis. We also identified a ModA-binding protein, IcmP, an insulin-cleaving metalloproteinase outer membrane protein. The T6SS-ModA-IcmP system provides P. aeruginosa with a growth advantage in bacterial competition under anaerobic conditions and plays an important role in bacterial virulence. Overall, this study clarifies the role of T6SS in secretion of an anion-binding protein, emphasizing the fundamental importance of this bacterium using T6SS-mediated molybdate uptake to adapt to complex environmental conditions. [Display omitted] •H2-T6SS mediates molybdate acquisition by secretion of ModA•Expression of H2-T6SS is activated by the master regulator Anr and anaerobiosis•ModA interacts with the outer membrane protein IcmP and uses it to deliver molybdate•The T6SS-ModA-IcmP system plays a role for P. aeruginosa in bacterial competition Wang et al. show that P. aeruginosa H2-T6SS secretes a molybdate-binding protein, ModA, which cooperates with IcmP for molybdate acquisition during anaerobiosis. The T6SS-ModA-IcmP system provides P. aeruginosa growth advantage in bacterial competition under anaerobic conditions and plays a role in bacterial virulence.
Type VI secretion system (T6SS) is widely distributed in Gram-negative bacteria and functions as a versatile protein export machinery that translocates effectors into eukaryotic or prokaryotic target cells. Growing evidence indicates that T6SS can deliver several effectors to promote bacterial survival in harmful environments through metal ion acquisition. Here, we report that the Pseudomonas aeruginosa H2-T6SS mediates molybdate (MoO42−) acquisition by secretion of a molybdate-binding protein, ModA. The expression of H2-T6SS genes is activated by the master regulator Anr and anaerobiosis. We also identified a ModA-binding protein, IcmP, an insulin-cleaving metalloproteinase outer membrane protein. The T6SS-ModA-IcmP system provides P. aeruginosa with a growth advantage in bacterial competition under anaerobic conditions and plays an important role in bacterial virulence. Overall, this study clarifies the role of T6SS in secretion of an anion-binding protein, emphasizing the fundamental importance of this bacterium using T6SS-mediated molybdate uptake to adapt to complex environmental conditions.
Type VI secretion system (T6SS) is widely distributed in Gram-negative bacteria and functions as a versatile protein export machinery that translocates effectors into eukaryotic or prokaryotic target cells. Growing evidence indicates that T6SS can deliver several effectors to promote bacterial survival in harmful environments through metal ion acquisition. Here, we report that the Pseudomonas aeruginosa H2-T6SS mediates molybdate (MoO ) acquisition by secretion of a molybdate-binding protein, ModA. The expression of H2-T6SS genes is activated by the master regulator Anr and anaerobiosis. We also identified a ModA-binding protein, IcmP, an insulin-cleaving metalloproteinase outer membrane protein. The T6SS-ModA-IcmP system provides P. aeruginosa with a growth advantage in bacterial competition under anaerobic conditions and plays an important role in bacterial virulence. Overall, this study clarifies the role of T6SS in secretion of an anion-binding protein, emphasizing the fundamental importance of this bacterium using T6SS-mediated molybdate uptake to adapt to complex environmental conditions.
ArticleNumber 108957
Author Wang, Yarong
Pu, Qinqin
Wu, Min
Liang, Haihua
Ji, Linxuan
Dang, Jing
Wen, Jing
Wang, Tietao
Du, Xiao
Han, Yuying
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Issue 2
Keywords Pseudomonas aeruginosa
molybdate acquisition
anaerobic condition
T6SS
Anr regulator
Language English
License This is an open access article under the CC BY license.
Copyright © 2021 The Author(s). Published by Elsevier Inc. All rights reserved.
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Snippet Type VI secretion system (T6SS) is widely distributed in Gram-negative bacteria and functions as a versatile protein export machinery that translocates...
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SubjectTerms anaerobic condition
Anaerobiosis - genetics
Animals
Anr regulator
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Carrier Proteins - genetics
Carrier Proteins - metabolism
Female
Gene Expression Regulation, Bacterial
Ion Transport
Metalloendopeptidases - genetics
Metalloendopeptidases - metabolism
Mice
Mice, Inbred C57BL
Microbial Interactions - genetics
Microbial Viability
molybdate acquisition
Molybdenum - metabolism
Pseudomonas aeruginosa
Pseudomonas aeruginosa - genetics
Pseudomonas aeruginosa - metabolism
Pseudomonas aeruginosa - pathogenicity
Pseudomonas Infections - microbiology
Pseudomonas Infections - mortality
Pseudomonas Infections - pathology
Survival Analysis
T6SS
Trans-Activators - genetics
Trans-Activators - metabolism
Type VI Secretion Systems - genetics
Type VI Secretion Systems - metabolism
Virulence
Virulence Factors - genetics
Virulence Factors - metabolism
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Title Pseudomonas aeruginosa T6SS-mediated molybdate transport contributes to bacterial competition during anaerobiosis
URI https://dx.doi.org/10.1016/j.celrep.2021.108957
https://www.ncbi.nlm.nih.gov/pubmed/33852869
https://doaj.org/article/a5dc9a27b9a349b9b88adc564b33f848
Volume 35
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