Abstract
The type VI secretion system (T6SS) of Gram-negative bacteria has been implicated in microbial competition; however, which components serve purely structural roles, and which serve as toxic effectors remains unresolved. Here, we present evidence that VgrG-3 of the Vibrio cholerae T6SS has both structural and toxin activity. Specifically, we demonstrate that the C-terminal extension of VgrG-3 acts to degrade peptidoglycan and hypothesize that this assists in the delivery of accessory T6SS toxins of V. cholerae. To avoid self-intoxication, V. cholerae expresses an anti-toxin encoded immediately downstream of vgrG-3 that inhibits VgrG-3-mediated lysis through direct interaction.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Antitoxins / metabolism*
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Antitoxins / physiology
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Bacterial Proteins / metabolism*
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Bacterial Proteins / physiology*
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Bacterial Secretion Systems / physiology*
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Cell Wall / metabolism
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Cloning, Molecular
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Computational Biology / methods
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Escherichia coli / metabolism
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Gene Expression Regulation, Bacterial*
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Hydrogen-Ion Concentration
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Hydrolysis
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Models, Biological
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Protein Structure, Tertiary
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Vibrio cholerae / metabolism*
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Virulence
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Virulence Factors / metabolism
Substances
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Antitoxins
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Bacterial Proteins
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Bacterial Secretion Systems
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Recombinant Proteins
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TsaB protein, Vibrio cholerae
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VgrG-3 protein, Vibrio cholerae
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Virulence Factors