Correction: A new potent HIV-1 reverse transcriptase inhibitor: A synthetic peptide derived from the interface subunit domains
| Autor: | Roger S. Goody, Gilles Divita, Véronique Robert-Hebmann, Christian Devaux, Jean Mery, May C. Morris, Laurent Chaloin, Frédéric Heitz |
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| Přispěvatelé: | Institut des Biomolécules Max Mousseron [Pôle Chimie Balard] (IBMM), Ecole Nationale Supérieure de Chimie de Montpellier (ENSCM)-Institut de Chimie du CNRS (INC)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Centre de recherche en Biologie Cellulaire (CRBM), Université Montpellier 1 (UM1)-Université Montpellier 2 - Sciences et Techniques (UM2)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Max Planck Institute of Molecular Physiology, Max-Planck-Gesellschaft, Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université de Montpellier (UM)-Ecole Nationale Supérieure de Chimie de Montpellier (ENSCM), Université Montpellier 2 - Sciences et Techniques (UM2)-Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Université Montpellier 1 (UM1) |
| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
chemistry.chemical_classification
0303 health sciences Conformational change Reverse-transcriptase inhibitor Protein subunit 030302 biochemistry & molecular biology Tryptophan Peptide Cell Biology Biology Biochemistry Reverse transcriptase In vitro 3. Good health Protein–protein interaction 03 medical and health sciences chemistry medicine Additions and Corrections Molecular Biology [SDV.MHEP]Life Sciences [q-bio]/Human health and pathology 030304 developmental biology medicine.drug |
| Zdroj: | Journal of Biological Chemistry Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2019, 294 (16), pp.6658. ⟨10.1074/jbc.AAC119.008640⟩ |
| ISSN: | 0021-9258 1083-351X |
| Popis: | The biologically relevant and active forms of human immunodeficiency viruses type 1 and 2 reverse transcriptase found in infectious virions are heterodimers produced in a two-step dimerization process. Dimerization involves first the rapid association of the two subunits, followed by a slow conformational change yielding a fully active form. We have shown that the dimeric nature of reverse transcriptase represents a important target for the design of a new class of antiviral agents. In this work, we propose a new strategy for its inhibition by targeting protein/protein interactions during viral formation in infected cells. From the screening of peptides derived from the tryptophan cluster at the interface of the connection subdomain, we have designed a short peptide (10 residues) corresponding to residues 395–404, which can block dimerization of reverse transcriptase in vitro and in infected cells. This peptide is highly efficient in abolishing the production of viral particles, without any adverse toxic side effects, when transduced into human immunodeficiency virus type 1-infected cells together with a new peptide carrier. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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