TY - JOUR
T1 - Multifunctional-autoprocessing repeats-in-toxin (MARTX) toxins of Vibrios
AU - Satchell, Karla J.F.
N1 - Publisher Copyright:
© 2014 American Society for Microbiology.
PY - 2015
Y1 - 2015
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84959051743&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84959051743&partnerID=8YFLogxK
U2 - 10.1128/microbiolspec.VE-0002-2014
DO - 10.1128/microbiolspec.VE-0002-2014
M3 - Article
C2 - 26185092
AN - SCOPUS:84959051743
SN - 2165-0497
VL - 3
JO - Microbiology Spectrum
JF - Microbiology Spectrum
IS - 3
M1 - VE-0002-2014
ER -