ArticleJournal of bacteriology2000
VirB6 is required for stabilization of VirB5 and VirB3 and formation of VirB7 homodimers in Agrobacterium tumefaciens.
Article in Journal of bacteriology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 80 citations in OpenAlex.
- Saucerneol D Suppresses the Growth ofCurrent issues in molecular biology · 2025Article
- Evolution and exchange of plasmids in pathogenicmSphere · 2023Article
- Interaction via the N terminus of the type IV secretion system (T4SS) protein VirB6 with VirB10 is required for VirB2 and VirB5 incorporation into T-pili and for T4SS function.The Journal of biological chemistry · 2018Article
- Structure of a VirD4 coupling protein bound to a VirB type IV secretion machinery.The EMBO journal · 2017Article
- Use of chimeric type IV secretion systems to define contributions of outer membrane subassemblies for contact-dependent translocation.Molecular microbiology · 2017Article
- Isolation of bacterial type IV machine subassemblies.Methods in molecular biology (Clifton, N.J.) · 2013Article
- Surface organelles assembled by secretion systems of Gram-negative bacteria: diversity in structure and function.FEMS microbiology reviews · 2012Review
- CagI is an essential component of the Helicobacter pylori Cag type IV secretion system and forms a complex with CagL.PloS one · 2012Article
- Helicobacter pylori exploits a unique repertoire of type IV secretion system components for pilus assembly at the bacteria-host cell interface.PLoS pathogens · 2011Article
- 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
- The coupling protein Cagbeta and its interaction partner CagZ are required for type IV secretion of the Helicobacter pylori CagA protein.Infection and immunity · 2010Article
- Agrobacterium tumefaciens type IV secretion protein VirB3 is an inner membrane protein and requires VirB4, VirB7, and VirB8 for stabilization.Journal of bacteriology · 2010Article
- An IcmF family protein, ImpLM, is an integral inner membrane protein interacting with ImpKL, and its walker a motif is required for type VI secretion system-mediated Hcp secretion in Agrobacterium tumefaciens.Journal of bacteriology · 2009Article
- Four VirB6 paralogs and VirB9 are expressed and interact in Ehrlichia chaffeensis-containing vacuoles.Journal of bacteriology · 2009Article
- Article
- Stabilization of the pertussis toxin secretion apparatus by the C terminus of PtlD.Journal of bacteriology · 2008Article
- VirB3 to VirB6 and VirB8 to VirB11, but not VirB7, are essential for mediating persistence of Brucella in the reticuloendothelial system.Journal of bacteriology · 2008Article
- Genetic and functional characterization of the type IV secretion system in Wolbachia.Journal of bacteriology · 2008Article
- VirB1* promotes T-pilus formation in the vir-Type IV secretion system of Agrobacterium tumefaciens.Journal of bacteriology · 2007Article
- Spatial location and requirements for the assembly of the Agrobacterium tumefaciens type IV secretion apparatus.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
VirB6 from Agrobacterium tumefaciens is an essential component of the type IV secretion machinery for T pilus formation and genetic transformation of plants. Due to its predicted topology as a polytopic inner membrane protein, it was proposed to form the transport pore for cell-to-cell transfer of genetic material and proteinaceous virulence factors. Here, we show that the absence of VirB6 leads to reduced cellular levels of VirB5 and VirB3, which were proposed to assist T pilus formation as minor component(s) or assembly factor(s), respectively. Overexpression of virB6 in trans restored levels of cell-bound and T pilus-associated VirB5 to wild type but did not restore VirB3 levels. Thus, VirB6 has a stabilizing effect on VirB5 accumulation, thereby regulating T pilus assembly. In the absence of VirB6, cell-bound VirB7 monomers and VirB7-VirB9 heterodimers were reduced and VirB7 homodimer formation was abolished. This effect could not be restored by expression of VirB6 in trans. Expression of TraD, a component of the transfer machinery of the IncN plasmid pKM101, with significant sequence similarity to VirB6, restored neither protein levels nor bacterial virulence but partly permitted T pilus formation in a virB6 deletion strain. VirB6 may therefore regulate T pilus formation by direct interaction with VirB5, and wild-type levels of VirB3 and VirB7 homodimers are not required.
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