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Published on: May 31, 2024
Multifunctional-autoprocessing repeats-in-toxin (MARTX) Toxins of Vibrios
1Department of Microbiology-Immunology, Northwestern University Feinberg School of Medicine, Chicago, IL 60611.
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.
Insights
Multifunctional-autoprocessing repeats-in-toxin (MARTX) toxins deliver cytotoxic effectors into host cells. These bacterial toxins, varying in domain composition, are linked to Vibrio pathogenesis in humans and animals.
Area of Science:
- Microbiology
- Molecular Biology
- Toxicology
Background:
- Multifunctional-autoprocessing repeats-in-toxin (MARTX) toxins are secreted by Gram-negative bacteria, notably Vibrio species.
- These toxins utilize conserved repeat regions and an autoprocessing protease domain for effector delivery into eukaryotic cells.
Purpose of the Study:
- To review the conserved structural elements of MARTX toxins.
- To detail the diverse toxin arrangements within Vibrio species and strains.
- To describe the catalytic functions and pathogenic roles of MARTX toxins.
Main Methods:
- Literature review of existing research on MARTX toxins.
- Analysis of conserved structural features and effector domain variations.
- Examination of toxin-pathogenesis relationships.
Main Results:
- MARTX toxins possess conserved repeat regions and an autoprocessing protease domain for effector translocation.
- Ten distinct effector domains exist, with individual toxins carrying two to five.
- Toxin variants can be acquired or lost via homologous recombination, leading to strain-specific differences.
Conclusions:
- MARTX toxins are versatile virulence factors with adaptable effector repertoires.
- Understanding MARTX toxin structure and function is crucial for elucidating bacterial pathogenesis.
- These toxins play a significant role in the pathogenicity of human and animal infections.
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