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Gene Review

BMEII0032  -  VirB8

Brucella melitensis bv. 1 str. 16M

 
 
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Disease relevance of BMEII0032

  • Structural comparison of pVirB8(AT) with Brucella suis VirB8 confirms that the monomers have a similar fold [1].
  • Agrobacterium tumefaciens VirB8 structure reveals potential protein-protein interaction sites [1].
  • Structures of two core subunits of the bacterial type IV secretion system, VirB8 from Brucella suis and ComB10 from Helicobacter pylori [2].
  • 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 [2].
  • Genes encoding VirB1, VirB8, VirB9, VirB10 and VirB11 were cloned into expression vectors; the affinity-tagged proteins were purified from Escherichia coli, and analyses by gel filtration chromatography showed that they form monomers or homo-multimers [3].
 

High impact information on BMEII0032

  • Dimerization and interactions of Brucella suis VirB8 with VirB4 and VirB10 are required for its biological activity [4].
  • 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 [4].
  • 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 [4].
  • Complementation with the B. suis VirB8 protein expressed from the virB promoter restored virulence [5].
  • To analyze the production of VirB proteins, polyclonal antisera against B. suis VirB5 and VirB8 were generated [6].
 

Analytical, diagnostic and therapeutic context of BMEII0032

  • Western blot analysis revealed that VirB5 and VirB8 were detected after 3 h in acidic minimal medium and that the amounts increased after prolonged incubation [6].

References

  1. Agrobacterium tumefaciens VirB8 structure reveals potential protein-protein interaction sites. Bailey, S., Ward, D., Middleton, R., Grossmann, J.G., Zambryski, P.C. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  2. Structures of two core subunits of the bacterial type IV secretion system, VirB8 from Brucella suis and ComB10 from Helicobacter pylori. Terradot, L., Bayliss, R., Oomen, C., Leonard, G.A., Baron, C., Waksman, G. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  3. The putative lytic transglycosylase VirB1 from Brucella suis interacts with the type IV secretion system core components VirB8, VirB9 and VirB11. Höppner, C., Carle, A., Sivanesan, D., Hoeppner, S., Baron, C. Microbiology (Reading, Engl.) (2005) [Pubmed]
  4. Dimerization and interactions of Brucella suis VirB8 with VirB4 and VirB10 are required for its biological activity. Paschos, A., Patey, G., Sivanesan, D., Gao, C., Bayliss, R., Waksman, G., O'callaghan, D., Baron, C. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  5. Swapping of periplasmic domains between Brucella suis VirB8 and a pSB102 VirB8 homologue allows heterologous complementation. Patey, G., Qi, Z., Bourg, G., Baron, C., O'Callaghan, D. Infect. Immun. (2006) [Pubmed]
  6. Production of the type IV secretion system differs among Brucella species as revealed with VirB5- and VirB8-specific antisera. Rouot, B., Alvarez-Martinez, M.T., Marius, C., Menanteau, P., Guilloteau, L., Boigegrain, R.A., Zumbihl, R., O'Callaghan, D., Domke, N., Baron, C. Infect. Immun. (2003) [Pubmed]
 
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