Literature DB >> 26185092

Multifunctional-autoprocessing repeats-in-toxin (MARTX) Toxins of Vibrios.

Karla J F Satchell1.   

Abstract

Multifunctional-autoprocessing repeats-in-toxin (MARTX) toxins are a heterogeneous group of toxins found in a number of Vibrio species and other Gram-negative bacteria. The toxins are composed of conserved repeat regions and an autoprocessing protease domain that together function as a delivery platform for transfer of cytotoxic and cytopathic domains into target eukaryotic cell cytosol. Within the cells, the effectors can alter biological processes such as signaling or cytoskeletal structure, presumably to the benefit of the bacterium. Ten effector domains are found in the various Vibrio MARTX toxins, although any one toxin carries only two to five effector domains. The specific toxin variant expressed by a species can be modified by homologous recombination to acquire or lose effector domains, such that different strains within the same species can express distinct variants of the toxins. This review examines the conserved structural elements of the MARTX toxins and details the different toxin arrangements carried by Vibrio species and strains. The catalytic function of domains and how the toxins are linked to pathogenesis of human and animals is described.

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Year:  2015        PMID: 26185092      PMCID: PMC4509488          DOI: 10.1128/microbiolspec.VE-0002-2014

Source DB:  PubMed          Journal:  Microbiol Spectr        ISSN: 2165-0497


  111 in total

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Review 5.  MARTX toxins as effector delivery platforms.

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Review 6.  Targeting and inactivation of bacterial toxins by human defensins.

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7.  The Vibrio cholerae MARTX toxin silences the inflammatory response to cytoskeletal damage before inducing actin cytoskeleton collapse.

Authors:  Patrick J Woida; Karla J F Satchell
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8.  N-terminal autoprocessing and acetylation of multifunctional-autoprocessing repeats-in-toxins (MARTX) Makes Caterpillars Floppy-like effector is stimulated by adenosine diphosphate (ADP)-Ribosylation Factor 1 in advance of Golgi fragmentation.

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