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Gene Review

bel2  -  Bel2

Human spumaretrovirus

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Disease relevance of bel2

  • One of the characteristic features of spumavirus transcription is the existence of singly spliced bel1 and bel2 mRNAs that alternatively are multiply spliced, thereby generating a complexity comparable to, but different from, that of lentiviruses and from that of other known retroviruses [1].
  • For the generation of the recombinant baculovirus, Acbel-1, the bel-1 gene of an HFV mutant was used, that bears truncations in the bel-1 overlapping bel-2 open reading frame [2].
 

High impact information on bel2

  • In contrast, deletions in bel 2 and bel 3 had only minor effects on the ability to transactivate [3].
  • Mutagenesis was used to alter the Bel 2 and Bet or to abrogate their expression [4].
  • The predominant HSRV protein detected in immunoblots by both Bel 1- and Bel 2-specific antisera had an apparent molecular weight of 56 kDa and corresponds to Bet [5].
  • The results showed the presence of both 257 base pair (bp) and 299 bp DNA fragments representing a part of gag and bel-2 sequences, respectively, in all four thymuses [6].
 

Biological context of bel2

  • In the corresponding region of the human foamy virus, three ORFs (bel-1, bel-2, and bel-3) have been identified (R. M. Flugel, A. Rethwilm, B. Maurer, and G. Darai, EMBO J. 6:2077-2084, 1987) [7].
 

Other interactions of bel2

  • Analysis of these mutants reveals that while the bel3 gene is not required for viral replication in vitro, mutations in the bel2 or bet gene decrease cell-free viral transmission approximately 10-fold [8].
 

Analytical, diagnostic and therapeutic context of bel2

  • Radioimmunoprecipitation analysis of 293T cells transfected with appropriate expression constructs by using antisera specific for the HFV Env, Bel1, and Bel2 proteins, as well as reverse transcription-PCR analysis of HFV-infected cells, demonstrated that this protein is an Env-Bet fusion protein that is secreted into the supernatant [9].
  • The functions of the bel 2 and bet genes are unknown and both are dispensable for replication of the prototypic human foamy virus in cell cultures [4].

References

  1. Analysis of splicing patterns of human spumaretrovirus by polymerase chain reaction reveals complex RNA structures. Muranyi, W., Flügel, R.M. J. Virol. (1991) [Pubmed]
  2. Expression of the human foamy virus bel-1 transactivator in insect cells. Hong, L., Bräutigam, S., Rethwilm, A. Virus Res. (1993) [Pubmed]
  3. The transcriptional transactivator of human foamy virus maps to the bel 1 genomic region. Rethwilm, A., Erlwein, O., Baunach, G., Maurer, B., ter Meulen, V. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  4. The bet gene of feline foamy virus is required for virus replication. Alke, A., Schwantes, A., Kido, K., Flötenmeyer, M., Flügel, R.M., Löchelt, M. Virology (2001) [Pubmed]
  5. Construction of an infectious DNA clone of the full-length human spumaretrovirus genome and mutagenesis of the bel 1 gene. Löchelt, M., Zentgraf, H., Flügel, R.M. Virology (1991) [Pubmed]
  6. Human foamy virus genome in the thymus of myasthenia gravis patients. Liu, W.T., Kao, K.P., Liu, Y.C., Chang, K.S. Zhonghua Min Guo Wei Sheng Wu Ji Mian Yi Xue Za Zhi (1996) [Pubmed]
  7. Identification of the simian foamy virus transcriptional transactivator gene (taf). Mergia, A., Shaw, K.E., Pratt-Lowe, E., Barry, P.A., Luciw, P.A. J. Virol. (1991) [Pubmed]
  8. Analysis of the role of the bel and bet open reading frames of human foamy virus by using a new quantitative assay. Yu, S.F., Linial, M.L. J. Virol. (1993) [Pubmed]
  9. Characterization of a human foamy virus 170-kilodalton Env-Bet fusion protein generated by alternative splicing. Lindemann, D., Rethwilm, A. J. Virol. (1998) [Pubmed]
 
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