The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
Gene Review

BSLF1  -  helicase/primase complex protein

Human herpesvirus 4

 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of BSLF1

 

High impact information on BSLF1

  • We now show in mice that low doses of this papillomavirus peptide were optimal in selecting a subpopulation of papillomavirus peptide-specific T cells that cross-reacted with MBP(87-99) and with an unrelated viral peptide derived from the BSLF1 protein of Epstein-Barr virus (EBV) [2].
  • The three helicase-primase proteins BBLF4 (helicase), BSLF1 (primase), and BBLF2/3 (primase-associated factor) were expressed fused to the Myc epitope [3].
  • An affinity assay using glutathione S-transferase-Zta fusion proteins demonstrated that Myc-BBLF4 and Myc-BBLF2/3 plus BSLF1 bound to the Zta activation domain (amino acids 1 to 133) [3].
  • Epstein-Barr virus (EBV) encodes putative helicase-primase proteins BBLF4, BSLF1 and BBLF2/3, which are essential for the lytic phase of viral DNA replication [4].
 

Biological context of BSLF1

  • When expression plasmids for BBLF4 or BBLF2/3 plus BSLF1 (primase subcomplex) were separately transfected, the proteins localized to the cytoplasm [3].
 

Physical interactions of BSLF1

  • Furthermore, experiments performed by using the extracts from insect cells co-infected with each pair of the recombinant viruses demonstrated that the BSLF1 protein could interact separately with both the BBLF4 and BBLF2/3 proteins and that the BBLF2/3 protein also interacted with the BBLF4 protein [4].
 

Analytical, diagnostic and therapeutic context of BSLF1

  • The anti-BSLF1 or anti-BBLF2/3 protein-specific antibody, which recognizes its target protein in both Western blotting and immunoprecipitation analyses, immunoprecipitated all of the BSLF1, BBLF4 and BBLF2/3 proteins from the extract of the cells with a virus productive cycle, indicating that these viral proteins are assembled together in vivo [4].

References

  1. Multiple Roles of Epstein-Barr Virus SM Protein in Lytic Replication. Han, Z., Marendy, E., Wang, Y.D., Yuan, J., Sample, J.T., Swaminathan, S. J. Virol. (2007) [Pubmed]
  2. In vivo survival of viral antigen-specific T cells that induce experimental autoimmune encephalomyelitis. Ufret-Vincenty, R.L., Quigley, L., Tresser, N., Pak, S.H., Gado, A., Hausmann, S., Wucherpfennig, K.W., Brocke, S. J. Exp. Med. (1998) [Pubmed]
  3. The Epstein-Barr virus lytic transactivator Zta interacts with the helicase-primase replication proteins. Gao, Z., Krithivas, A., Finan, J.E., Semmes, O.J., Zhou, S., Wang, Y., Hayward, S.D. J. Virol. (1998) [Pubmed]
  4. Assembly of the epstein-barr virus BBLF4, BSLF1 and BBLF2/3 proteins and their interactive properties. Yokoyama, N., Fujii, K., Hirata, M., Tamai, K., Kiyono, T., Kuzushima, K., Nishiyama, Y., Fujita, M., Tsurumi, T. J. Gen. Virol. (1999) [Pubmed]
 
WikiGenes - Universities