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Literature summary for 3.4.23.47 extracted from

  • Raugi, D.N.; Smith, R.A.; Gottlieb, G.S.; Gottlieb, G.S.
    Four amino acid changes in HIV-2 protease confer class-wide sensitivity to protease inhibitors (2016), J. Virol., 90, 1062-1069 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.23.47

Protein Variants

Protein Variants Comment Organism
I32V site-directed mutagenesis, mutation analogous to wild-type HIV-1 protease sequence (EC 3.4.23.16). The mutation increases the susceptibility of HIV-2 to multiple protease inhibitors Human immunodeficiency virus 2
I82V site-directed mutagenesis, mutation analogous to wild-type HIV-1 protease sequence (EC 3.4.23.16) Human immunodeficiency virus 2
M76L site-directed mutagenesis, mutation analogous to wild-type HIV-1 protease sequence (EC 3.4.23.16). The mutation increases the susceptibility of HIV-2 to multiple protease inhibitors Human immunodeficiency virus 2
additional information construction of HIV-2ROD9 molecular clones containing amino acid changes corresponding to wild-type HIV-1 amino acids (I32V, V47I, M76L, and I82V) either individually or together (clone PRDELTA4) and comparison of the phenotypic sensitivities (50% effective concentration [EC50]) of mutant and wild-type viruses to nine FDA-approved protease inhibitors, overview. Clone PRDELTA4 show protease inhibitor susceptibility equivalent to or greater than that of HIV-1 for all protease inhibitors Human immunodeficiency virus 2
V47I site-directed mutagenesis, mutation analogous to wild-type HIV-1 protease sequence (EC 3.4.23.16). The mutation increases the susceptibility of HIV-2 to multiple protease inhibitors Human immunodeficiency virus 2
V47I/M76L/I32V/I82V site-directed mutagenesis, mutation analogous to wild-type HIV-1 protease sequence (EC 3.4.23.16). The combination of the four amino acid changes in HIV-2 protease confers a pattern of protease inhibitor susceptibility comparable to that of HIV-1 Human immunodeficiency virus 2

Inhibitors

Inhibitors Comment Organism Structure
darunavir
-
 Human immunodeficiency virus 2
lopinavir
-
 Human immunodeficiency virus 2
additional information HIV-2 exhibits intrinsic resistance to most FDA-approved HIV-1 protease inhibitors, retaining clinically useful susceptibility only to lopinavir, darunavir, and saquinavir. Structural rationale for intrinsic HIV-2 PI resistance. No inhibition by amprenavir, atazanavir, indinavir, nelfinavir, ritonavir, and tipranavir. Phenotypic protease inhibitor sensitivities of wild-type HIV-1, wild-type HIV-2, and mutant HIV-2 strains, overview Human immunodeficiency virus 2
saquinavir
-
 Human immunodeficiency virus 2

Organism

Organism UniProt Comment Textmining
Human immunodeficiency virus 2 P04584 Gag-Pol polyprotein; HIV-2
-

Synonyms

Synonyms Comment Organism
HIV-2 protease
-
 Human immunodeficiency virus 2
PR2
-
 Human immunodeficiency virus 2