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Targeting Human Immunodeficiency Virus Type 1 Assembly, Maturation and Budding

The targets for licensed drugs used for the treatment of human immunodeficiency virus type 1 (HIV-1) are confined to the viral reverse transcriptase (RT), protease (PR), and the gp41 transmembrane protein (TM). While currently approved drugs are effective in controlling HIV-1 infections, new drug ta...

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Autores principales: Wapling, Johanna, Srivastava, Seema, Shehu-Xhilaga, Miranda, Tachedjian, Gilda
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Libertas Academica 2007
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3155237/
https://www.ncbi.nlm.nih.gov/pubmed/21901072
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author Wapling, Johanna
Srivastava, Seema
Shehu-Xhilaga, Miranda
Tachedjian, Gilda
author_facet Wapling, Johanna
Srivastava, Seema
Shehu-Xhilaga, Miranda
Tachedjian, Gilda
author_sort Wapling, Johanna
collection PubMed
description The targets for licensed drugs used for the treatment of human immunodeficiency virus type 1 (HIV-1) are confined to the viral reverse transcriptase (RT), protease (PR), and the gp41 transmembrane protein (TM). While currently approved drugs are effective in controlling HIV-1 infections, new drug targets and agents are needed due to the eventual emergence of drug resistant strains and drug toxicity. Our increased understanding of the virus life-cycle and how the virus interacts with the host cell has unveiled novel mechanisms for blocking HIV-1 replication. This review focuses on inhibitors that target the late stages of virus replication including the synthesis and trafficking of the viral polyproteins, viral assembly, maturation and budding. Novel approaches to blocking the oligomerization of viral enzymes and the interactions between viral proteins and host cell factors, including their feasibility as drug targets, are discussed.
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spelling pubmed-31552372011-09-07 Targeting Human Immunodeficiency Virus Type 1 Assembly, Maturation and Budding Wapling, Johanna Srivastava, Seema Shehu-Xhilaga, Miranda Tachedjian, Gilda Drug Target Insights Review The targets for licensed drugs used for the treatment of human immunodeficiency virus type 1 (HIV-1) are confined to the viral reverse transcriptase (RT), protease (PR), and the gp41 transmembrane protein (TM). While currently approved drugs are effective in controlling HIV-1 infections, new drug targets and agents are needed due to the eventual emergence of drug resistant strains and drug toxicity. Our increased understanding of the virus life-cycle and how the virus interacts with the host cell has unveiled novel mechanisms for blocking HIV-1 replication. This review focuses on inhibitors that target the late stages of virus replication including the synthesis and trafficking of the viral polyproteins, viral assembly, maturation and budding. Novel approaches to blocking the oligomerization of viral enzymes and the interactions between viral proteins and host cell factors, including their feasibility as drug targets, are discussed. Libertas Academica 2007-07-20 /pmc/articles/PMC3155237/ /pubmed/21901072 Text en © the author(s), publisher and licensee Libertas Academica Ltd. This is an open access article. Unrestricted non-commercial use is permitted provided the original work is properly cited.
spellingShingle Review
Wapling, Johanna
Srivastava, Seema
Shehu-Xhilaga, Miranda
Tachedjian, Gilda
Targeting Human Immunodeficiency Virus Type 1 Assembly, Maturation and Budding
title Targeting Human Immunodeficiency Virus Type 1 Assembly, Maturation and Budding
title_full Targeting Human Immunodeficiency Virus Type 1 Assembly, Maturation and Budding
title_fullStr Targeting Human Immunodeficiency Virus Type 1 Assembly, Maturation and Budding
title_full_unstemmed Targeting Human Immunodeficiency Virus Type 1 Assembly, Maturation and Budding
title_short Targeting Human Immunodeficiency Virus Type 1 Assembly, Maturation and Budding
title_sort targeting human immunodeficiency virus type 1 assembly, maturation and budding
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3155237/
https://www.ncbi.nlm.nih.gov/pubmed/21901072
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