Viruses 2010, 2(4), 900-926; doi:10.3390/v2040900
Review

HIV-1 Ribonuclease H: Structure, Catalytic Mechanism and Inhibitors

Greg L. Beilhartz and Matthias Götte* email
Department of Microbiology and Immunology, McGill University, Lyman Duff Medical Building (D6), 3775 University St., Montreal, QC, H3A 2B4, Canada
* Author to whom correspondence should be addressed.
Received: 28 January 2010; in revised form: 22 March 2010 / Accepted: 24 March 2010 / Published: 30 March 2010
(This article belongs to the Special Issue Retroviral Enzymes)
PDF Full-text Download PDF Full-Text [814 KB, uploaded 30 March 2010 16:12 CEST]
Abstract: Since the human immunodeficiency virus (HIV) was discovered as the etiological agent of acquired immunodeficiency syndrome (AIDS), it has encouraged much research into antiviral compounds. The reverse transcriptase (RT) of HIV has been a main target for antiviral drugs. However, all drugs developed so far inhibit the polymerase function of the enzyme, while none of the approved antiviral agents inhibit specifically the necessary ribonuclease H (RNase H) function of RT. This review provides a background on structure-function relationships of HIV-1 RNase H, as well as an outline of current attempts to develop novel, potent chemotherapeutics against a difficult drug target.
Keywords: HIV; reverse transcriptase; RNase H; inhibitors; drug resistance

Article Statistics

Click here to load and display the download statistics.

Cite This Article

MDPI and ACS Style

Beilhartz, G.L.; Götte, M. HIV-1 Ribonuclease H: Structure, Catalytic Mechanism and Inhibitors. Viruses 2010, 2, 900-926.

AMA Style

Beilhartz GL, Götte M. HIV-1 Ribonuclease H: Structure, Catalytic Mechanism and Inhibitors. Viruses. 2010; 2(4):900-926.

Chicago/Turabian Style

Beilhartz, Greg L.; Götte, Matthias. 2010. "HIV-1 Ribonuclease H: Structure, Catalytic Mechanism and Inhibitors." Viruses 2, no. 4: 900-926.

Viruses EISSN 1999-4915 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert