ArticleCellular microbiology2015
Induced autoprocessing of the cytopathic Makes caterpillars floppy-like effector domain of the Vibrio vulnificus MARTX toxin.
Article in Cellular microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 26 citations in OpenAlex.
- Article
- The Achilles Heel of Protein Biochemistry: Insolubility of Recombinant Proteins-A Case Study About Producing a Rice Enzyme.International journal of molecular sciences · 2025Article
- Article
- Structure and activation mechanism of the Makes caterpillars floppy 1 toxin.Nature communications · 2023Article
- Actin Cross-Linking Effector Domain of theInfection and immunity · 2022Article
- Cross-Kingdom Activation ofJournal of bacteriology · 2020Review
- 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.Cellular microbiology · 2020Article
- Makes caterpillars floppy-like effector-containing MARTX toxins require host ADP-ribosylation factor (ARF) proteins for systemic pathogenicity.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- RRSP and RID Effector Domains Dominate the Virulence Impact of Vibrio vulnificus MARTX Toxin.The Journal of infectious diseases · 2019Article
- A cysteine protease-like domain enhances the cytotoxic effects of theThe Journal of biological chemistry · 2019Article
- The Modes of Action of MARTX Toxin Effector Domains.Toxins · 2018Review
- Coordinated delivery and function of bacterial MARTX toxin effectors.Molecular microbiology · 2018Review
- Vibrio vulnificus MARTX cytotoxin causes inactivation of phagocytosis-related signaling molecules in macrophages.Journal of biomedical science · 2017Article
- The Effector Domain Region of the Vibrio vulnificus MARTX Toxin Confers Biphasic Epithelial Barrier Disruption and Is Essential for Systemic Spread from the Intestine.PLoS pathogens · 2017Article
- MARTX effector cross kingdom activation by Golgi-associated ADP-ribosylation factors.Cellular microbiology · 2016Article
- MARTX toxins as effector delivery platforms.Pathogens and disease · 2015Review
- Comparison of Xenorhabdus bovienii bacterial strain genomes reveals diversity in symbiotic functions.BMC genomics · 2015Article
- The Makes Caterpillars Floppy (MCF)-Like Domain of Vibrio vulnificus Induces Mitochondrion-Mediated Apoptosis.Infection and immunity · 2015Article
- Multifunctional-autoprocessing repeats-in-toxin (MARTX) Toxins of Vibrios.Microbiology spectrum · 2015Review
- Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The multifunctional-autoprocessing repeats-in-toxin (MARTX(Vv)) toxin that harbours a varied repertoire of effector domains is the primary virulence factor of Vibrio vulnificus. Although ubiquitously present among Biotype I toxin variants, the 'Makes caterpillars floppy-like' effector domain (MCF(Vv)) is previously unstudied. Using transient expression and protein delivery, MCF(Vv) and MCF(Ah) from the Aeromonas hydrophila MARTX(Ah)) toxin are shown for the first time to induce cell rounding. Alanine mutagenesis across the C-terminal subdomain of MCF(Vv) identified an Arg-Cys-Asp (RCD) tripeptide motif shown to comprise a cysteine protease catalytic site essential for autoprocessing of MCF(Vv). The autoprocessing could be recapitulated in vitro by the addition of host cell lysate to recombinant MCF(Vv), indicating induced autoprocessing by cellular factors. The RCD motif is also essential for cytopathicity, suggesting autoprocessing is essential first to activate the toxin and then to process a cellular target protein resulting in cell rounding. Sequence homology places MCF(Vv) within the C58 cysteine protease family that includes the type III secretion effectors YopT from Yersinia spp. and AvrPphB from Pseudomonas syringae. However, the catalytic site RCD motif is unique compared with other C58 peptidases and is here proposed to represent a new subgroup of autopeptidase found within a number of putative large bacterial toxins.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.