A role for the aspartyl protease from the human immunodeficiency virus type 1 (HIV-1) in the orchestration of virus assembly

• Published in: Annals of the New York Academy of Sciences Vol. 616; p. 73
• Main Authors: Navia, M A, McKeever, B M
• Format: Journal Article
• Language: English
• Published: United States 01-12-1990
• Subjects: Animals; Aspartic Acid Endopeptidases - chemistry; Aspartic Acid Endopeptidases - metabolism; HIV Protease - chemistry; HIV Protease - metabolism; HIV-1 - enzymology; HIV-1 - growth & development; Humans; Models, Biological; Virus Replication; X-Ray Diffraction
• ISSN: 0077-8923
• DOI: 10.1111/j.1749-6632.1990.tb17829.x

Functional HIV-1 protease (PR) is required for the maturation of viral proteins, for the appearance of characteristic structural features in the virion (as determined by electron microscopy), and for the final assembly of mature virus. Most importantly, HIV-1 PR activity is required for the development of infectivity. Still largely undefined, however, is the timing and control of protease action in this assembly process. Based on the three-dimensional structure of HIV-1 PR2,3 and experimental data reported in the literature, we propose a comprehensive virus assembly model that highlights the role of HIV-1 PR, suggests further experiments to verify the validity of the model, and poses specific questions relevant to the ultimate exploitation of HIV-1 protease as a therapeutic target.