ArticleThe Journal of biological chemistry2012
Crystal structure of the VgrG1 actin cross-linking domain of the Vibrio cholerae type VI secretion system.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 68 citations in OpenAlex.
- The VgrG2 effector of Acinetobacter baumannii mediates immune evasion by repressing Csu pilus assembly and triggering phagocyte methuosis.Nature communications · 2026Article
- Type VI secretion system effectors as modulators of host immunometabolism: organelle stress, nutritional immunity, and therapeutic opportunities.Frontiers in microbiology · 2026Review
- The SPI-6 T6SS gene cluster fromFrontiers in microbiology · 2026Article
- The SPI-20 and SPI-21 T6SS gene clusters fromFrontiers in microbiology · 2026Article
- TseCurrent research in microbial sciences · 2026Article
- Genomic signatures of resistance and adaptability in Aeromonas and Pseudomonas from a Brazilian Hope Spot.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2025Article
- Deciphering theJournal of bacteriology · 2025Review
- The Competitive Edge: T6SS-Mediated Interference Competition byMicroorganisms · 2025Review
- The C-terminal extension of VgrG4 from Klebsiella pneumoniae remodels host cell microfilaments.Proteins · 2022Article
- Identification of Type VI Secretion Systems Effector Proteins That Contribute to Interbacterial Competition inFrontiers in microbiology · 2022Article
- Beyond dueling: roles of the type VI secretion system in microbiome modulation, pathogenesis and stress resistance.Stress biology · 2021Review
- A New Contact Killing Toxin Permeabilizes Cells and Belongs to a Broadly Distributed Protein Family.mSphere · 2021Article
- Article
- Endogenous membrane stress induces T6SS activity inProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Anchoring the T6SS to the cell wall: Crystal structure of the peptidoglycan binding domain of the TagL accessory protein.PloS one · 2021Article
- Burkholderia pseudomallei as an Enteric Pathogen: Identification of Virulence Factors Mediating Gastrointestinal Infection.Infection and immunity · 2020Article
- An Overview of Anti-Eukaryotic T6SS Effectors.Frontiers in cellular and infection microbiology · 2020Review
- Article
- Pan-genome diversification and recombination in Cronobacter sakazakii, an opportunistic pathogen in neonates, and insights to its xerotolerant lifestyle.BMC microbiology · 2019Article
- Cyclic di-GMP inactivates T6SS and T4SS activity in Agrobacterium tumefaciens.Molecular microbiology · 2019Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Vibrio cholerae is the cause of the diarrheal disease cholera. V. cholerae produces RtxA, a large toxin of the MARTX family, which is targeted to the host cell cytosol, where its actin cross-linking domain (ACD) cross-links G-actin, leading to F-actin depolymerization, cytoskeleton rearrangements, and cell rounding. These effects on the cytoskeleton prevent phagocytosis and bacterial engulfment by macrophages, thus preventing V. cholerae clearance from the gut. The V. cholerae Type VI secretion-associated VgrG1 protein also contains a C-terminal ACD, which shares 61% identity with MARTX ACD and has been shown to covalently cross-link G-actin. Here, we purified the VgrG1 C-terminal domain and determined its crystal structure. The VgrG1 ACD exhibits a V-shaped three-dimensional structure, formed of 12 β-strands and nine α-helices. Its active site comprises five residues that are conserved in MARTX ACD toxin, within a conserved area of ∼10 Å radius. We showed that less than 100 ACD molecules are sufficient to depolymerize the actin filaments of a fibroblast cell in vivo. Mutagenesis studies confirmed that Glu-16 is critical for the F-actin depolymerization function. Co-crystals with divalent cations and ATP reveal the molecular mechanism of the MARTX/VgrG toxins and offer perspectives for their possible inhibition.
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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.