Diversity of HIV-1 Vpr Interactions Involves Usage of the WXXF Motif of Host Cell Proteins
| Autor: | Roger J. Pomerantz, Lingxun Duan, YanNing Xue, Yves Baudat, Joséphine Sire, Baocheng Hu, Mohamad Bouhamdan |
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| Rok vydání: | 1998 |
| Předmět: |
Phage display
viruses Molecular Sequence Data Peptide Biology Virus Replication Biochemistry Humans Macromolecular docking Amino Acid Sequence Molecular Biology Gene chemistry.chemical_classification Binding Sites Base Sequence Gene Products vpr Proteins virus diseases RNA vpr Gene Products Human Immunodeficiency Virus Cell Biology biochemical phenomena metabolism and nutrition Fusion protein chemistry Docking (molecular) Uracil-DNA glycosylase HIV-1 Sequence Analysis Protein Binding |
| Zdroj: | Journal of Biological Chemistry. 273:8009-8016 |
| ISSN: | 0021-9258 |
| Popis: | Targeting protein or RNA moieties to specific cellular compartments may enhance their desired functions and specificities. Human immunodeficiency virus type I (HIV-1) encodes proteins in addition to Gag, Pol, and Env that are packaged into virus particles. One such retroviral-incorporated protein is Vpr, which is present in all primate lentiviruses. Vpr has been implicated in different roles within the HIV-1 life cycle. In testing a new hypothesis in which viral proteins are utilized as docking sites to incorporate protein moieties into virions, we used the peptide phage display approach to search for Vpr-specific binding peptides. In the present studies, we demonstrate that most of the peptides that bind to Vpr have a common motif, WXXF. More importantly, we demonstrate that the WXXF motif of uracil DNA glycosylase is implicated in the interaction of uracil DNA glycosylase with Vpr intracellularly. Finally, a dimer of the WXXF motif was fused to the chloramphenicol acetyl transferase (CAT) gene, and it was demonstrated that the WXXF dimer-CAT fusion protein construct produces CAT activity within virions in the presence of Vpr as a docking protein. This study provides a novel potential strategy in the targeting of anti-viral agents to interfere with HIV-1 replication. |
| Databáze: | OpenAIRE |
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