Analysis of Temperature-Sensitive Mutants of the HIV-1 Protease

  • M. Manchester
  • D. D. Loeb
  • L. Everitt
  • M. Moody
  • C. A. HutchisonIII
  • R. Swanstrom
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 306)


Human Immunodeficiency Virus Type-1, like other retroviruses, encodes an aspartic proteinase whose activity is required for the production of infectious virions.1–6 The protease (PR) is encoded at the 5′ end of the viral pol gene and is responsible for cleavage of the viral gag and gag/pol precursor proteins to their mature forms.7,8 Viruses with inactivating mutations in their protease domain yield immature, noninfectious particles containing unprocessed gag and gag/pol polyproteins;1 for this reason the enzyme has been a prime target for structural and biochemical studies leading to the design of inhibitors of virus replication.


Human Immunodeficiency Virus Human Immunodeficiency Virus Type Aspartic Proteinase Protease Domain Human Immunodeficiency Virus Protease 
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Copyright information

© Plenum Press, New York 1991

Authors and Affiliations

  • M. Manchester
    • 1
    • 4
  • D. D. Loeb
    • 2
    • 4
  • L. Everitt
    • 2
    • 4
  • M. Moody
    • 2
    • 4
  • C. A. HutchisonIII
    • 3
    • 4
  • R. Swanstrom
    • 2
    • 4
  1. 1.Curriculum in GeneticsUniversity of North Carolina at Chapel HillChapel HillUSA
  2. 2.Department of BiochemistryUniversity of North Carolina at Chapel HillChapel HillUSA
  3. 3.Department of Microbiology and ImmunologyUniversity of North Carolina at Chapel HillChapel HillUSA
  4. 4.Lineberger Cancer Research CenterUniversity of North Carolina at Chapel HillChapel HillUSA

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