| Virus Name | Human immunodeficiency virus 2 |
| Virus Short Name | HIV2 |
| Order | Unassigned |
| Virus Family | Retroviridae |
| Virus Subfamily | Orthoretrovirinae |
| Genus | Lentivirus |
| Species | Human immunodeficiency virus 2 |
| Host | Vertebrates |
| Cell Tropism | CD4+ T cells, macrophages and dendritic cells |
| Associated Disease | Acquired immunodeficiency syndrome |
| Mode of Transmission | Sexual contact, blood, breast feeding |
| VIPR DB link | N.A. |
| ICTV DB link | https://talk.ictvonline.org/ictv-reports/ictv_9th_report/reverse-transcribing-dna-and-rna-viruses-2011/w/rt_viruses/161/retroviridae |
| Virus Host DB link | http://www.genome.jp/virushostdb/view/?virus_lineage=Retroviridae |
| Paper Title | Interactions between Tat of HIV-2 and Transcription Factor Sp1 |
| Author's Name | A. Santos Pagtakhan and Sandra E. Tong-Starksen |
| Journal Name | Virology |
| Pubmed ID | 9400595 |
| Abstract | Tat of HIV-2 (Tat-2) requires host cellular factors for optimal function. We show that transactivation by Tat-2 of the HIV promoter requires cis-acting binding sites for Sp1 or Sp1 brought to the promoter via a heterologous system. We demonstrate that an activation domain in Tat-2 consists of one of two potential alpha-helices in the amino-terminal region, the cysteine-rich region, and the core region and that this independent activation domain requires cis-acting Sp1-binding sites for function. Tat-2 interacts with Sp1 in in vitro binding assays, and these interactions require basic residues outside of the Tat-2 activation domain. The regions in Sp1 sufficient for functional synergy with Tat are the Sp1 activation domains, while the DNA-binding region is dispensable. Substitution mutations of a glutamine-rich region in one Sp1 activation domain, which eliminate interactions with a TBP-associated factor, also significantly decrease synergy with Tat. Thus, the functional synergy between Tat-2 and Sp1 localizes to domains in each activator that interact with components of the transcription complex. We suggest that these interactions, rather than direct Tat/Sp1 binding, result in highly processive RNA polymerase II complexes and full-length viral transcripts. |
| Used Model | HeLa cells |
| DOI | 10.1006/viro.1997.8847 |
