ArticleLife (Basel, Switzerland)2021
Biochemical Characterization, Specificity and Inhibition Studies of HTLV-1, HTLV-2, and HTLV-3 Proteases.
Article in Life (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 14 citations in OpenAlex.
- Conformational Dynamics of Viral Protease Precursors in Maturation, Inhibition, and Drug-Resistance Development.Viruses · 2026Review
- The challenge of HTLV-1 therapeutics: lessons from anti-protease approaches.New microbes and new infections · 2026Review
- Discovery of Galangin Derivatives as a Potential T-cell Leukemia Virus 1 Protease Inhibitor Through Chemoinformatics Approaches.Cell biochemistry and biophysics · 2025Article
- New Perspectives about Drug Candidates Targeting HTLV-1 and Related Diseases.Pharmaceuticals (Basel, Switzerland) · 2023Review
- Article
- Different Mutation Tolerance of Lentiviral (HIV-1) and Deltaretroviral (BLV and HTLV) Protease Precursors.Viruses · 2022Article
- Current Approaches in Molecular Enzymology.Life (Basel, Switzerland) · 2022Article
- Kinetics of Bovine leukemia virus aspartic protease reveals its dimerization and conformational change.PloS one · 2022Article
- Development of a Bio-Layer Interferometry-Based Protease Assay Using HIV-1 Protease as a Model.Viruses · 2021Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The human T-lymphotropic viruses (HTLVs) are causative agents of severe diseases including adult T-cell leukemia. Similar to human immunodeficiency viruses (HIVs), the viral protease (PR) plays a crucial role in the viral life-cycle via the processing of the viral polyproteins. Thus, it is a potential target of anti-retroviral therapies. In this study, we performed in vitro comparative analysis of human T-cell leukemia virus type 1, 2, and 3 (HTLV-1, -2, and -3) proteases. Amino acid preferences of S4 to S1' subsites were studied by using a series of synthetic oligopeptide substrates representing the natural and modified cleavage site sequences of the proteases. Biochemical characteristics of the different PRs were also determined, including catalytic efficiencies and dependence of activity on pH, temperature, and ionic strength. We investigated the effects of different HIV-1 PR inhibitors (atazanavir, darunavir, DMP-323, indinavir, ritonavir, and saquinavir) on enzyme activities, and inhibitory potentials of IB-268 and IB-269 inhibitors that were previously designed against HTLV-1 PR. Comparative biochemical analysis of HTLV-1, -2, and -3 PRs may help understand the characteristic similarities and differences between these enzymes in order to estimate the potential of the appearance of drug-resistance against specific HTLV-1 PR inhibitors.
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