Equivalent inhibition of half-site and full-site retroviral strand transfer reactions by structurally diverse compounds
| Autor: | Daria J. Hazuda, D Grandgenett, K Brackmann, B Pramanik, J C Hastings, G Goodarzi, Abigail Wolfe, Peter J. Felock, A Vora |
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| Rok vydání: | 1997 |
| Předmět: |
Virus Integration
Immunology Integrase inhibitor Integrase Inhibitors HIV Integrase Biology Microbiology law.invention chemistry.chemical_compound law Virology Animals Humans Magnesium HIV Integrase Inhibitors Avian Myeloblastosis Virus Manganese Integrases Molecular Structure Oligonucleotide In vitro toxicology Molecular biology In vitro Recombinant Proteins Integrase chemistry Oligodeoxyribonucleotides Insect Science Recombinant DNA biology.protein HIV-1 DNA Research Article |
| Zdroj: | Journal of virology. 71(1) |
| ISSN: | 0022-538X |
| Popis: | In vitro assay systems which use recombinant retroviral integrase (IN) and short DNA oligonucleotides fail to recapitulate the full-site integration reaction as it is known to occur in vivo. The relevance of using such circumscribed in vitro assays to define inhibitors of retroviral integration has not been formerly demonstrated. Therefore, we analyzed a series of structurally diverse inhibitors with respect to inhibition of both half-site and full-site strand transfer reactions with either recombinant or virion-produced IN. Half-site and full-site reactions catalyzed by avian myeloblastosis virus and human immunodeficiency virus type 1 (HIV-1) IN from virions are shown to be equivalently sensitive to inhibition by compounds which inhibit half-site reactions catalyzed by the recombinant HIV-1 IN. These studies therefore support the utility of using in vitro assays employing either recombinant or virion-derived IN to identify inhibitors of integration. |
| Databáze: | OpenAIRE |
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