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

BALF2  -  major DNA-binding 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 BALF2

  • The immunohistochemical staining of EBV proteins showed that the EBV latent membrane protein-1 was detected in four of seven cases and that BZLF1, BALF2, and gp350/220 proteins associating with virus production were not expressed [1].
  • Since the BALF2 gene encodes a 135-kDa DNA-binding protein which was immunoprecipitated by antibody against ICP8 protein, a key protein in herpes simplex virus replication, we asked whether the lack of productive cycle in Raji cells is due to the absence of expression of the BALF2 gene [2].
  • In order to obtain the amount of EBV SSB required for characterization, a recombinant baculovirus containing the complete sequence of the BALF2 open reading frame under the control of the baculovirus polyhedrin promoter was constructed [3].
 

High impact information on BALF2

  • Transcriptional activity was found in peripheral blood B lymphocytes (PBLs) for BZLF1 in 88%, BALF2 in 50%, and BcLF1 in 25% of the tested IM patients [4].
  • Bromodeoxyuridine-labeled chromatin immunodepletion analyses confirmed that PCNA is loaded onto newly synthesized viral DNA as well as BALF2 and BMRF1 viral proteins during lytic replication [5].
  • In contrast, the BALF5 Pol catalytic protein, the BALF2 single-stranded-DNA binding protein, and the BBLF2/3 protein, a component of the helicase-primase complex, were colocalized as distinct dots distributed within replication compartments, representing viral replication factories [6].
  • This assay also provided evidence for an interaction between the single-stranded DNA binding protein, BALF2, and the Zta-tethered helicase-primase complex [7].
  • We previously showed the absence of two messenger RNAs that are encoded by the BamHI-A fragment of the EBV genome and that correspond to open reading frames BALF2 and BARF1 in chemically induced Raji cells [2].
 

Biological context of BALF2

 

Anatomical context of BALF2

 

Analytical, diagnostic and therapeutic context of BALF2

  • SDS-polyacrylamide gel electrophoresis showed the presence of a single polypeptide with a molecular weight of 130 K, which was identified as BALF2 protein by Western immunoblot analysis [8].
  • On Superose 6 HR 10/30 gel filtration the BALF2 protein eluted at a position corresponding to an apparent molecular mass of approximately 128 K, indicating that the BALF2 protein behaves as a monomer in solution [8].

References

  1. Association of Epstein-Barr virus (EBV) with Sjögren's syndrome: differential EBV expression between epithelial cells and lymphocytes in salivary glands. Wen, S., Shimizu, N., Yoshiyama, H., Mizugaki, Y., Shinozaki, F., Takada, K. Am. J. Pathol. (1996) [Pubmed]
  2. The lytic cycle of Epstein-Barr virus in the nonproducer Raji line can be rescued by the expression of a 135-kilodalton protein encoded by the BALF2 open reading frame. Decaussin, G., Leclerc, V., Ooka, T. J. Virol. (1995) [Pubmed]
  3. Overexpression, purification and helix-destabilizing properties of Epstein-Barr virus ssDNA-binding protein. Tsurumi, T., Kishore, J., Yokoyama, N., Fujita, M., Daikoku, T., Yamada, H., Yamashita, Y., Nishiyama, Y. J. Gen. Virol. (1998) [Pubmed]
  4. Lytic replication of Epstein-Barr virus in the peripheral blood: analysis of viral gene expression in B lymphocytes during infectious mononucleosis and in the normal carrier state. Prang, N.S., Hornef, M.W., Jäger, M., Wagner, H.J., Wolf, H., Schwarzmann, F.M. Blood (1997) [Pubmed]
  5. Postreplicative mismatch repair factors are recruited to epstein-barr virus replication compartments. Daikoku, T., Kudoh, A., Sugaya, Y., Iwahori, S., Shirata, N., Isomura, H., Tsurumi, T. J. Biol. Chem. (2006) [Pubmed]
  6. Architecture of replication compartments formed during Epstein-Barr virus lytic replication. Daikoku, T., Kudoh, A., Fujita, M., Sugaya, Y., Isomura, H., Shirata, N., Tsurumi, T. J. Virol. (2005) [Pubmed]
  7. 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]
  8. Epstein-Barr virus single-stranded DNA-binding protein: purification, characterization, and action on DNA synthesis by the viral DNA polymerase. Tsurumi, T., Kobayashi, A., Tamai, K., Yamada, H., Daikoku, T., Yamashita, Y., Nishiyama, Y. Virology (1996) [Pubmed]
  9. Characterization of the Epstein-Barr virus BALF2 promoter. Hung, C.H., Liu, S.T. J. Gen. Virol. (1999) [Pubmed]
  10. Targeted gene disruption in Epstein-Barr virus. Lee, M.A., Kim, O.J., Yates, J.L. Virology (1992) [Pubmed]
  11. Epstein-Barr virus (EBV) infection in salivary gland tumors: lytic EBV infection in nonmalignant epithelial cells surrounded by EBV-positive T-lymphoma cells. Wen, S., Mizugaki, Y., Shinozaki, F., Takada, K. Virology (1997) [Pubmed]
 
WikiGenes - Universities