HIV-1 protease

From WikiMD's Wellness Encyclopedia

HIV-1 protease is an enzyme that plays a critical role in the life cycle of the Human Immunodeficiency Virus Type 1 (HIV-1), which is the virus responsible for the Acquired Immunodeficiency Syndrome (AIDS). This enzyme is essential for the post-translational processing of the viral polyproteins, leading to the maturation of the virus and its ability to infect new cells. Due to its crucial role in the viral life cycle, HIV-1 protease has been a prime target for antiretroviral therapy aimed at treating HIV/AIDS.

Function[edit | edit source]

HIV-1 protease is a dimer, consisting of two identical subunits, each comprising 99 amino acids. It cleaves the Gag and Gag-Pol polyproteins at specific sites, leading to the structural proteins and enzymes necessary for the assembly of new virions. Without the activity of HIV-1 protease, the viral particles remain immature and non-infectious.

Structure[edit | edit source]

The enzyme's active site is located in a cleft between the two subunits, and it has a unique Aspartyl protease mechanism, utilizing two aspartate residues to cleave the peptide bond. The specificity of HIV-1 protease for its substrates is highly precise, making it an attractive target for drug design.

Inhibition and Drug Resistance[edit | edit source]

The inhibition of HIV-1 protease disrupts the viral replication cycle, making protease inhibitors (PIs) a key component of Highly Active Antiretroviral Therapy (HAART). However, the high mutation rate of HIV-1 leads to the emergence of drug-resistant strains, posing significant challenges to the effectiveness of PIs. Continuous efforts in drug development are necessary to overcome resistance and improve treatment outcomes.

Clinical Significance[edit | edit source]

The discovery of HIV-1 protease and its role in the viral life cycle has had a profound impact on the management of HIV/AIDS. Protease inhibitors have significantly improved the life expectancy and quality of life for individuals living with HIV. Ongoing research focuses on developing new inhibitors with better efficacy and resistance profiles, as well as understanding the mechanisms of drug resistance.

See Also[edit | edit source]


WikiMD
Navigation: Wellness - Encyclopedia - Health topics - Disease Index‏‎ - Drugs - World Directory - Gray's Anatomy - Keto diet - Recipes

Search WikiMD

Ad.Tired of being Overweight? Try W8MD's physician weight loss program.
Semaglutide (Ozempic / Wegovy and Tirzepatide (Mounjaro / Zepbound) available.
Advertise on WikiMD

WikiMD's Wellness Encyclopedia

Let Food Be Thy Medicine
Medicine Thy Food - Hippocrates

Medical Disclaimer: WikiMD is not a substitute for professional medical advice. The information on WikiMD is provided as an information resource only, may be incorrect, outdated or misleading, and is not to be used or relied on for any diagnostic or treatment purposes. Please consult your health care provider before making any healthcare decisions or for guidance about a specific medical condition. WikiMD expressly disclaims responsibility, and shall have no liability, for any damages, loss, injury, or liability whatsoever suffered as a result of your reliance on the information contained in this site. By visiting this site you agree to the foregoing terms and conditions, which may from time to time be changed or supplemented by WikiMD. If you do not agree to the foregoing terms and conditions, you should not enter or use this site. See full disclaimer.
Credits:Most images are courtesy of Wikimedia commons, and templates Wikipedia, licensed under CC BY SA or similar.

Contributors: Prab R. Tumpati, MD