Vpr content of HIV-1 virions determines infection of resting peripheral blood CD4+ lymphocytes
| Autor: | Elien Vandermarliere, Kathleen Moens, Hanne Vanderstraeten, Sophie Vermaut, Stijn Vanhee, Petra Van Damme, Ann Baeyens, Wojciech Witkowski, Bruno Verhasselt, Francis Impens, Anouk Van Nuffel, Kathleen Vanlandeghem, Evelien Naessens, Kris Gevaert |
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| Jazyk: | angličtina |
| Rok vydání: | 2013 |
| Předmět: |
chemistry.chemical_classification
biology business.industry viruses Kozak consensus sequence virus diseases biochemical phenomena metabolism and nutrition Amino acid Cell biology Infectious Diseases medicine.anatomical_structure Protein structure chemistry Docking (molecular) Transcription (biology) Virology Immunology Poster Presentation Medicine and Health Sciences medicine biology.protein Antibody Nuclear pore business Nucleus |
| Zdroj: | Retrovirology RETROVIROLOGY |
| ISSN: | 1742-4690 |
| Popis: | Background The HIV-1 Vpr protein is a 14 kDa accessory protein, required for efficient replication in macrophages. Vpr is incorporated into HIV virions, believed to participate in the docking of the HIV-1 pre-integration complex to the nucleus and to facilitate it’s transport through the nuclear pore. By inducing G2 arrest, Vpr favors transcription from the HIV-1 LTR, which it also transactivates. We noticed two N-terminal amino acids of the HIV-1, SIVmac and SIVcpz Vpr proteins are fully conserved. This N-terminal motif is predicted to be a NatB substrate motif (i.e., Met-Glu-), expected to lead to full Nt-acetylation of the protein, but it also allows the conservation of the Kozak consensus sequence (A/GCCAUGG), critical for efficient protein translation. Nt-acetylation is one of the most common protein modifications in eukaryotes and is believed to affect protein stability, degradation and function. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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