Processing sites in the human immunodeficiency virus type 1 (HIV-1) Gag-Pro-Pol precursor are cleaved by the viral protease at different rates Public Deposited

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  • Swanstrom, Ronald
    • Affiliation: School of Medicine, Department of Biochemistry and Biophysics
  • Pettit, Steve C
    • Affiliation: School of Medicine, Department of Medicine
  • Kaplan, Andrew H
    • Affiliation: School of Medicine, Department of Medicine
  • Lindquist, Jeffrey N
    • Affiliation: School of Medicine, Department of Biochemistry and Biophysics
    • Other Affiliation: Department of Pathology, Moores UCSD Cancer Center, 3855 Health Sciences Dr. #0803, La Jolla, CA 92093-0803, USA
  • Abstract We have examined the kinetics of processing of the HIV-1 Gag-Pro-Pol precursor in an in vitro assay with mature protease added in trans. The processing sites were cleaved at different rates to produce distinct intermediates. The initial cleavage occurred at the p2/NC site. Intermediate cleavages occurred at similar rates at the MA/CA and RT/IN sites, and to a lesser extent at sites upstream of RT. Late cleavages occurred at the sites flanking the protease (PR) domain, suggesting sequestering of these sites. We observed paired intermediates indicative of half- cleavage of RT/RH site, suggesting that the RT domain in Gag-Pro-Pol was in a dimeric form under these assay conditions. These results clarify our understanding of the processing kinetics of the Gag-Pro-Pol precursor and suggest regulated cleavage. Our results further suggest that early dimerization of the PR and RT domains may serve as a regulatory element to influence the kinetics of processing within the Pol domain.
Date of publication
Resource type
  • Article
Rights statement
  • In Copyright
Rights holder
  • Steve C Pettit et al.; licensee BioMed Central Ltd.
Journal title
  • Retrovirology
Journal volume
  • 2
Journal issue
  • 1
Page start
  • 66
  • English
Is the article or chapter peer-reviewed?
  • Yes
  • 1742-4690
Bibliographic citation
  • Retrovirology. 2005 Nov 01;2(1):66
  • Open Access
  • BioMed Central Ltd

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