ArticleProceedings of the National Academy of Sciences of the United States of America2006
Dimerization and interactions of Brucella suis VirB8 with VirB4 and VirB10 are required for its biological activity.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- Inner membrane components of the plasmid pKM101 type IV secretion system TraE and TraD are DNA-binding proteins.Scientific reports · 2025Article
- ThemicroLife · 2025Review
- Small Molecule Inhibitors against the Bacterial PathogenCurrent medicinal chemistry · 2024Review
- Uncovering the Hidden Credentials ofMicrobiology and molecular biology reviews : MMBR · 2021Review
- 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
- 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 Rickettsia type IV secretion system: unrealized complexity mired by gene family expansion.Pathogens and disease · 2016Article
- VirB8-like protein TraH is crucial for DNA transfer in Enterococcus faecalis.Scientific reports · 2016Article
- An orphaned Mce-associated membrane protein of Mycobacterium tuberculosis is a virulence factor that stabilizes Mce transporters.Molecular microbiology · 2016Article
- AFrontiers in cellular and infection microbiology · 2016Article
- Article
- Pathogenesis and immunobiology of brucellosis: review of Brucella-host interactions.The American journal of pathology · 2015Review
- Mechanism and structure of the bacterial type IV secretion systems.Biochimica et biophysica acta · 2014Review
- Isolation of bacterial type IV machine subassemblies.Methods in molecular biology (Clifton, N.J.) · 2013Article
- The dimer interface of Agrobacterium tumefaciens VirB8 is important for type IV secretion system function, stability, and association of VirB2 with the core complex.Journal of bacteriology · 2011Article
- An in vivo high-throughput screening approach targeting the type IV secretion system component VirB8 identified inhibitors of Brucella abortus 2308 proliferation.Infection and immunity · 2011Article
- The small heat-shock protein HspL is a VirB8 chaperone promoting type IV secretion-mediated DNA transfer.The Journal of biological chemistry · 2010Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
VirB8-like proteins are essential components of type IV secretion systems, bacterial virulence factors that mediate the translocation of effector molecules from many bacterial pathogens into eukaryotic cells. Based on cell biological, genetic, and x-ray crystallographic data, VirB8 was proposed to undergo multiple protein-protein interactions to mediate assembly of the translocation machinery. Here we report the results of a structure-function analysis of the periplasmic domain of VirB8 from the mammalian pathogen Brucella suis, which identifies amino acid residues required for three protein-protein interactions. VirB8 variants changed at residues proposed to be involved in dimerization, and protein-protein interactions were purified and characterized in vitro and in vivo. Changes at M102, Y105, and E214 affected the self-association as measured by analytical ultracentrifugation and gel filtration. The interaction with B. suis VirB10 was reduced by changes at T201, and change at R230 inhibited the interaction with VirB4 in vitro. The in vivo functionality of VirB8 variants was determined by complementation of growth in macrophages by a B. suis virB8 mutant and by using a heterologous assay of type IV secretion system assembly in Agrobacterium tumefaciens. Changes at Y105, T201, R230, and at several other residues impaired the in vivo function of VirB8, suggesting that we have identified interaction sites of relevance in the natural biological context.
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