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Relevant bibliographies by topics / HIV-1 Cyclic Mutant

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Journal articles

Academic literature on the topic 'HIV-1 Cyclic Mutant'

Author: Grafiati

Published: 6 September 2023

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Journal articles on the topic "HIV-1 Cyclic Mutant"

1

Sree Kanth, S., and M. Vijjulatha. "Tetrahydroxy Cyclic Urea-Potent Inhibitor for HIV-1 Protease Wild Type and Mutant Type—A Computational Design." E-Journal of Chemistry 5, no. 3 (2008): 584–92. http://dx.doi.org/10.1155/2008/154030.

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A series of novel tetrahydroxy cyclic urea molecules as HIV-1 protease inhibitors were designed using computational techniques. The designed molecules were compared with the known cyclic urea molecules by performing docking studies on six of wild type protein and three mutant protein varieties and calculating their ADME properties. A series of novel molecules were designed by substituting hydrogen at the P1/ P1′ positions with hydroxyl group increasing the bioavailability these had better ADME properties and binding affinity towards HIV-1 protease. The biological activity of these inhibitors were predicted by a model equation generated by the regression analysis between biological activity (log 1/Ki) of known inhibitors and there combined docking scores from six of the wild type protein docking. The synthetic studies are in progress.

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2

Nillroth, U., L. Vrang, P. O. Markgren, J. Hultén, A. Hallberg, and U. H. Danielson. "Human immunodeficiency virus type 1 proteinase resistance to symmetric cyclic urea inhibitor analogs." Antimicrobial Agents and Chemotherapy 41, no. 11 (November 1997): 2383–88. http://dx.doi.org/10.1128/aac.41.11.2383.

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Resistant virus was isolated from virus propagated in cell culture in the presence of the human immunodeficiency virus type 1 (HIV-1) proteinase inhibitor DMP 323, Ro 31-8959, or A-75925. The proteinase gene of resistant virus was sequenced, and key mutations (G48V, V82A, I84V, L90M, and G48V/L90M) were introduced into clones used for the expression, purification, and further characterization of the enzyme. The mutant enzymes were all less active than the wild-type enzyme, as judged by k(cat) and k(cat)/Km values. L90M had a lower Km than the wild type, whereas the G48V/L90M double mutant had an increased Km compared with that of the wild type, contributing to a 10-fold reduction in the k(cat)/Km. Vitality values were used to show that the enzyme of the I84V mutant is the enzyme most resistant to the two cyclic urea inhibitors DMP 323 and AHA 008. Virus with the same mutation is also resistant, although the double mutation L10F/I84V confers even greater resistance. All of these mutants are more resistant to DMP 323 than to AHA 008. The resistance of the I84V mutant may be attributed to a loss of van der Waals interactions with the inhibitor, since the larger amino acid side chain involved in the interaction is replaced by a smaller side chain. This is supported by the lower level of resistance to AHA 008 that was observed. The phenyl groups of AHA 008 should protrude deeper into the S1 and S1' subsites than those of the smaller compound DMP 323, reducing the loss of interaction energy. These results reveal that small structural modifications of inhibitors that do not affect the inhibitory effect on wild-type virus can influence the inhibition of resistant strains. This is of importance for optimizing drugs with respect to their potency and resistance.

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3

Avram, Speranta, Cristian Bologa, and Maria-Luiza Flonta. "Quantitative structure-activity relationship by CoMFA for cyclic urea and nonpeptide-cyclic cyanoguanidine derivatives on wild type and mutant HIV-1 protease." Journal of Molecular Modeling 11, no. 2 (February 16, 2005): 105–15. http://dx.doi.org/10.1007/s00894-004-0226-5.

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4

Thomas, Christian A., Ofra K. Weinberger, Benedikt L. Ziegler, Steven Greenberg, Ira Schieren, Samuel C. Silverstein, and Joseph El Khoury. "Human Immunodeficiency Virus-1 env Impairs Fcγ Receptor-Mediated Phagocytosis Via a Cyclic Adenosine Monophosphate-Dependent Mechanism." Blood 90, no. 9 (November 1, 1997): 3760–65. http://dx.doi.org/10.1182/blood.v90.9.3760.

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Abstract Human immunodeficiency virus (HIV)-1 expression in mononuclear phagocytes is associated with multiple functional defects, including phagocytosis. To assess Fcγ receptor (FcγR) function in cells expressing HIV-1, human promonocytic cells (U937) acutely or chronically infected with HIV-1, or stably transfected with a noninfectious reverse transcriptase (RT) defective HIV-1 provirus (Δpol), were treated with phorbol 12-myristate 13-acetate for 48 hours and tested for their ability to ingest sheep erythrocytes coated with IgG (E-IgG). HIV-1–infected or transfected U937 cells ingested 50% to 65% fewer E-IgG than controls despite normal surface expression of FcγRs. HIV-1 specifically impaired FcγR-mediated phagocytosis, as ingestion of complement-coated erythrocytes was unaffected. U937 cells transfected with an env deficient mutant of HIV-1 ingested E-IgG normally, suggesting that the expression of HIV-1 env was required for HIV-1 to inhibit FcγR-mediated phagocytosis. Expression of HIV-1 in U937 cells was associated with an increased accumulation of intracellular cyclic adenosine monophosphate (cAMP); addition of the adenylate cyclase inhibitor 2′,5′-dideoxyadenosine to these cells decreased intracellular cAMP levels to that of controls and restored FcγR-mediated phagocytosis. Addition of either interferon (IFN)-γ or an inhibitor of cAMP-dependent protein kinase A (KT 5720) to HIV-1–transfected U937 cells also restored FcγR-mediated phagocytosis. Expression of HIV-1 induces a specific defect of FcγR function in mononuclear phagocytes that correlates with increased levels of cAMP, and can be corrected by pharmacologic manipulation.

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5

Ala, Paul J., Edward E. Huston, Ronald M. Klabe, Denise D. McCabe, Jodie L. Duke, Christopher J. Rizzo, Bruce D. Korant, et al. "Molecular Basis of HIV-1 Protease Drug Resistance: Structural Analysis of Mutant Proteases Complexed with Cyclic Urea Inhibitors." Biochemistry 36, no. 21 (May 1997): 6556. http://dx.doi.org/10.1021/bi9750044.

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6

Ala, Paul J., Edward E. Huston, Ronald M. Klabe, Denise D. McCabe, Jodie L. Duke, Christopher J. Rizzo, Bruce D. Korant, et al. "Molecular Basis of HIV-1 Protease Drug Resistance: Structural Analysis of Mutant Proteases Complexed with Cyclic Urea Inhibitors†." Biochemistry 36, no. 7 (February 1997): 1573–80. http://dx.doi.org/10.1021/bi962234u.

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7

Garg, Rajni, and Barun Bhhatarai. "Possible allosteric interactions of monoindazole-substituted P2 cyclic urea analogues with wild-type and mutant HIV-1 protease." Journal of Computer-Aided Molecular Design 22, no. 10 (March 27, 2008): 737–45. http://dx.doi.org/10.1007/s10822-008-9210-y.

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8

Ala, Paul J., Edward E. Huston, Ronald M. Klabe, Prabhakar K. Jadhav, Patrick Y. S. Lam, and Chong-Hwan Chang. "Counteracting HIV-1 Protease Drug Resistance: Structural Analysis of Mutant Proteases Complexed with XV638 and SD146, Cyclic Urea Amides with Broad Specificities." Biochemistry 37, no. 43 (October 1998): 15042–49. http://dx.doi.org/10.1021/bi980386e.

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9

Ammosova, Tatyana, Marina Jerebtsova, Monique Beullens, Bart Lesage, Angela Jackson, Fatah Kashanchi, William Southerland, Victor R. Gordeuk, Mathieu Bollen, and Sergei Nekhai. "Nuclear Targeting of Protein Phosphatase-1 by HIV-1 Tat Protein." Journal of Biological Chemistry 280, no. 43 (August 29, 2005): 36364–71. http://dx.doi.org/10.1074/jbc.m503673200.

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Transcription of human immunodeficiency virus (HIV)-1 genes is activated by HIV-1 Tat protein, which induces phosphorylation of the C-terminal domain of RNA polymerase-II by CDK9/cyclin T1. We previously showed that Tat-induced HIV-1 transcription is regulated by protein phosphatase-1 (PP1). In the present study we demonstrate that Tat interacts with PP1 and that disruption of this interaction prevents induction of HIV-1 transcription. We show that PP1 interacts with Tat in part through the binding of Val36 and Phe38 of Tat to PP1 and that Tat is involved in the nuclear and subnuclear targeting of PP1. The PP1 binding mutant Tat-V36A/F38A displayed a decreased affinity for PP1 and was a poor activator of HIV-1 transcription. Surprisingly, Tat-Q35R mutant that had a higher affinity for PP1 was also a poor activator of HIV-1 transcription, because strong PP1 binding competed out binding of Tat to CDK9/cyclin T1. Our results suggest that Tat might function as a nuclear regulator of PP1 and that interaction of Tat with PP1 is critical for activation of HIV-1 transcription by Tat.

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10

Jadlowsky, Julie K., Masanori Nojima, Takashi Okamoto, and Koh Fujinaga. "Dominant negative mutant cyclin T1 proteins that inhibit HIV transcription by forming a kinase inactive complex with Tat." Journal of General Virology 89, no. 11 (November 1, 2008): 2783–87. http://dx.doi.org/10.1099/vir.0.2008/002857-0.

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Transcription of the human immunodeficiency virus type 1 (HIV) requires the interaction of the cyclin T1 (CycT1) subunit of a host cellular factor, the positive transcription elongation factor b (P-TEFb), with the viral Tat protein, at the transactivation response element (TAR) of nascent transcripts. Because of this virus-specific interaction, CycT1 may potentially serve as a target for the development of anti-HIV therapies. Here we report the development of a mutant CycT1 protein, containing three threonine-to-alanine substitutions in the linker region between two of the cyclin boxes, which displays a potent dominant negative effect on HIV transcription. Investigation into the inhibitory mechanism revealed that this mutant CycT1 interacted with Tat and the cyclin-dependent kinase 9 (Cdk9) subunit of P-TEFb, but failed to stimulate the Cdk9 kinase activity critical for elongation. This mutant CycT1 protein may represent a novel class of specific inhibitors of HIV transcription which could lead to development of new antiviral therapies.

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