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Human immunodeficiency virus type 1 and type 2 protease monomers are functionally interchangeable in the dimeric
C E Patterson1, R Seetharam, C A Kettner
1DuPont Merck Pharmaceutical Company, Wilmington, Delaware 19880-0328.
Journal of Virology
|February 1, 1992
Summary
Researchers created active hybrid dimers of human immunodeficiency virus (HIV) proteases, combining HIV-1 and HIV-2. This suggests similar functional folding for both HIV protease types, despite low sequence identity.
Area of Science:
- Biochemistry
- Virology
- Molecular Biology
Background:
- Human immunodeficiency virus type 1 (HIV-1) and HIV-2 proteases function as dimers of identical subunits.
- Previous work established active one-chain dimer constructs for HIV-1 protease.
Purpose of the Study:
- To create and assess the activity of a one-chain recombinant dimer of HIV-2 protease.
- To generate and evaluate hybrid one-chain dimers combining HIV-1 and HIV-2 protease monomers.
Main Methods:
- Constructing recombinant DNA for one-chain HIV-2 protease dimer expression.
- Modifying constructs to create hybrid one-chain dimers of HIV-1 and HIV-2 protease monomers.
- Assessing the enzymatic activity of the resulting one-chain dimers.
Main Results:
- A fully active one-chain recombinant HIV-2 protease dimer was successfully expressed.
- Hybrid one-chain dimers composed of both HIV-1 and HIV-2 protease monomers were created.
- These hybrid dimers demonstrated full enzymatic activity, despite only 47.5% sequence identity between monomers.
Conclusions:
- The functional activity of the hybrid dimers suggests that HIV-1 and HIV-2 protease monomers exhibit functionally similar folding mechanisms.
- This finding has implications for understanding protease structure-function relationships and potential therapeutic strategies targeting viral proteases.