Comparative Study
doi: 10.1016/0014-5793(91)80362-7.
Comparison of the HIV-1 and HIV-2 proteinases using oligopeptide substrates representing cleavage sites in Gag and Gag-Pol polyproteins
Affiliations
- PMID: 2015912
- DOI: 10.1016/0014-5793(91)80362-7
Item in Clipboard
Comparative Study
Comparison of the HIV-1 and HIV-2 proteinases using oligopeptide substrates representing cleavage sites in Gag and Gag-Pol polyproteins
FEBS Lett.
.
Free article
Abstract
The substrate specificity of the human immunodeficiency virus type 1 (HIV-1) and type 2 (HIV-2) proteinases was compared using oligopeptides corresponding to cleavage sites in the Gag and Gag-Pol polyproteins of both viruses. All peptides mimicking cleavage sites at the junction of major functional protein domains were correctly cleaved by both enzymes. However, some other peptides thought to represent secondary cleavage sites remained intact. The kinetic parameters (Km and kcat) obtained for the different substrates showed several hundred-fold variation but were similar for the same substrate.
Similar articles
-
Proteolytic activity of novel human immunodeficiency virus type 1 proteinase proteins from a precursor with a blocking mutation at the N terminus of the PR domain.J Virol. 1994 Jan;68(1):240-50. doi: 10.1128/JVI.68.1.240-250.1994. J Virol. 1994. PMID: 8254734 Free PMC article.
-
Naturally occurring amino acid polymorphisms in human immunodeficiency virus type 1 (HIV-1) Gag p7(NC) and the C-cleavage site impact Gag-Pol processing by HIV-1 protease.Virology. 2002 Jan 5;292(1):137-49. doi: 10.1006/viro.2001.1184. Virology. 2002. PMID: 11878916
-
Mechanism of inhibition of the retroviral protease by a Rous sarcoma virus peptide substrate representing the cleavage site between the gag p2 and p10 proteins.J Biol Chem. 1992 Nov 25;267(33):23735-41. J Biol Chem. 1992. PMID: 1331099
-
Subsite preferences of retroviral proteinases.Methods Enzymol. 1994;241:254-78. doi: 10.1016/0076-6879(94)41068-2. Methods Enzymol. 1994. PMID: 7854181 Review. No abstract available.
-
Specificity of retroviral proteases: an analysis of viral and nonviral protein substrates.Methods Enzymol. 1994;241:279-301. doi: 10.1016/0076-6879(94)41069-0. Methods Enzymol. 1994. PMID: 7854182 Review. No abstract available.
Cited by
-
A Direct Interaction with RNA Dramatically Enhances the Catalytic Activity of the HIV-1 Protease In Vitro.J Mol Biol. 2015 Jul 17;427(14):2360-78. doi: 10.1016/j.jmb.2015.05.007. Epub 2015 May 15. J Mol Biol. 2015. PMID: 25986307 Free PMC article.
-
Dynamics of HIV-1 Gag Processing as Revealed by Fluorescence Lifetime Imaging Microscopy and Single Virus Tracking.Viruses. 2022 Feb 8;14(2):340. doi: 10.3390/v14020340. Viruses. 2022. PMID: 35215933 Free PMC article.
-
Highly Drug-Resistant HIV-1 Protease Mutant PRS17 Shows Enhanced Binding to Substrate Analogues.ACS Omega. 2019 May 31;4(5):8707-8719. doi: 10.1021/acsomega.9b00683. Epub 2019 May 17. ACS Omega. 2019. PMID: 31172041 Free PMC article.
-
The p2 domain of human immunodeficiency virus type 1 Gag regulates sequential proteolytic processing and is required to produce fully infectious virions.J Virol. 1994 Dec;68(12):8017-27. doi: 10.1128/JVI.68.12.8017-8027.1994. J Virol. 1994. PMID: 7966591 Free PMC article.
-
Development of a novel anti-HIV-1 agent from within: effect of chimeric Vpr-containing protease cleavage site residues on virus replication.Proc Natl Acad Sci U S A. 1997 Apr 1;94(7):3346-51. doi: 10.1073/pnas.94.7.3346. Proc Natl Acad Sci U S A. 1997. PMID: 9096396 Free PMC article.
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
