ArticleProceedings of the National Academy of Sciences of the United States of America2005
Structures of two core subunits of the bacterial type IV secretion system, VirB8 from Brucella suis and ComB10 from Helicobacter pylori.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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Who cites it
57 citing papers in PubMed, 119 citations in OpenAlex.
- Inner membrane components of the plasmid pKM101 type IV secretion system TraE and TraD are DNA-binding proteins.Scientific reports · 2025Article
- ThemicroLife · 2025Review
- Cryo-EM structure of a conjugative type IV secretion system suggests a molecular switch regulating pilus biogenesis.The EMBO journal · 2024Article
- Small Molecule Inhibitors against the Bacterial PathogenCurrent medicinal chemistry · 2024Review
- Comparative Analysis of T4SS Molecular Architectures.Journal of microbiology and biotechnology · 2023Review
- Article
- Cryo-EM structure of a type IV secretion system.Nature · 2022Article
- The VirB System Plays a Crucial Role inInternational journal of molecular sciences · 2021Review
- Type IV secretion systems: Advances in structure, function, and activation.Molecular microbiology · 2021Review
- Uncovering the Hidden Credentials ofMicrobiology and molecular biology reviews : MMBR · 2021Review
- Biological and Structural Diversity of Type IV Secretion Systems.Microbiology spectrum · 2019Review
- Bacteria-Killing Type IV Secretion Systems.Frontiers in microbiology · 2019Review
- VirB8 homolog TraE from plasmid pKM101 forms a hexameric ring structure and interacts with the VirB6 homolog TraD.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Article
- Fragment-based screening identifies novel targets for inhibitors of conjugative transfer of antimicrobial resistance by plasmid pKM101.Scientific reports · 2017Article
- Use of chimeric type IV secretion systems to define contributions of outer membrane subassemblies for contact-dependent translocation.Molecular microbiology · 2017Article
- Analyzing the role of CagV, a VirB8 homolog of the type IV secretion system ofFEBS open bio · 2017Article
- Structural Analysis and Inhibition of TraE from the pKM101 Type IV Secretion System.The Journal of biological chemistry · 2016Article
- The Mosaic Type IV Secretion Systems.EcoSal Plus · 2016Review
- The Rickettsia type IV secretion system: unrealized complexity mired by gene family expansion.Pathogens and disease · 2016Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Type IV secretion systems (T4SSs) are commonly used secretion machineries in Gram-negative bacteria. They are used in the infection of human, animal, or plant cells and the propagation of antibiotic resistance. The T4SS apparatus spans both membranes of the bacterium and generally is composed of 12 proteins, named VirB1-11 and VirD4 after proteins of the canonical Agrobacterium tumefaciens T4SS. The periplasmic core complex of VirB8/VirB10 structurally and functionally links the cytoplasmic NTPases of the system with its outer membrane and pilus components. Here we present crystal structures of VirB8 of Brucella suis, the causative agent of brucellosis, and ComB10, a VirB10 homolog of Helicobacter pylori, the causative agent of gastric ulcers. The structures of VirB8 and ComB10 resemble known folds, albeit with novel secondary-structure modifications unique to and conserved within their respective families. Both proteins crystallized as dimers, providing detailed predictions about their self associations. These structures make a substantial contribution to the repertoire of T4SS component structures and will serve as springboards for future functional and protein-protein interaction studies by using knowledge-based site-directed and deletion mutagenesis.
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