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Article ; Online: Effect of P-body component Mov10 on HCV virus production and infectivity.

Liu, Dandan / Ndongwe, Tanyaradzwa P / Puray-Chavez, Maritza / Casey, Mary C / Izumi, Taisuke / Pathak, Vinay K / Tedbury, Philip R / Sarafianos, Stefan G

FASEB journal : official publication of the Federation of American Societies for Experimental Biology

2020 Volume 34, Issue 7, Page(s) 9433–9449

Abstract: Mov10 is a processing body (P-body) protein and an interferon-stimulated gene that can affect replication of retroviruses, hepatitis B virus, and hepatitis C virus (HCV). The mechanism of HCV inhibition by Mov10 is unknown. Here, we investigate the ... ...

Abstract	Mov10 is a processing body (P-body) protein and an interferon-stimulated gene that can affect replication of retroviruses, hepatitis B virus, and hepatitis C virus (HCV). The mechanism of HCV inhibition by Mov10 is unknown. Here, we investigate the effect of Mov10 on HCV infection and determine the virus life cycle steps affected by changes in Mov10 overexpression. Mov10 overexpression suppresses HCV RNA in both infectious virus and subgenomic replicon systems. Additionally, Mov10 overexpression decreases the infectivity of released virus, unlike control P-body protein DCP1a that has no effect on HCV RNA production or infectivity of progeny virus. Confocal imaging of uninfected cells shows endogenous Mov10 localized at P-bodies. However, in HCV-infected cells, Mov10 localizes in circular structures surrounding cytoplasmic lipid droplets with NS5A and core protein. Mutagenesis experiments show that the RNA binding activity of Mov10 is required for HCV inhibition, while its P-body localization, helicase, and ATP-binding functions are not required. Unexpectedly, endogenous Mov10 promotes HCV replication, as CRISPR-Cas9-based Mov10 depletion decreases HCV replication and infection levels. Our data reveal an important and complex role for Mov10 in HCV replication, which can be perturbed by excess or insufficient Mov10.
MeSH term(s)	Hepacivirus/isolation & purification ; Hepacivirus/physiology ; Hepatitis C/pathology ; Hepatitis C/prevention & control ; Hepatitis C/virology ; Host-Pathogen Interactions ; Humans ; RNA Helicases/genetics ; RNA Helicases/metabolism ; Virus Replication
Chemical Substances	Mov10 protein, human (EC 2.7.7.-) ; RNA Helicases (EC 3.6.4.13)
Language	English
Publishing date	2020-06-04
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	639186-2
ISSN	1530-6860 ; 0892-6638
ISSN (online)	1530-6860
ISSN	0892-6638
DOI	10.1096/fj.201800641R
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Design, Synthesis and Characterization of HIV-1 CA-Targeting Small Molecules: Conformational Restriction of PF74.

Sahani, Rajkumar Lalji / Diana-Rivero, Raquel / Vernekar, Sanjeev Kumar V / Wang, Lei / Du, Haijuan / Zhang, Huanchun / Castaner, Andres Emanuelli / Casey, Mary C / Kirby, Karen A / Tedbury, Philip R / Xie, Jiashu / Sarafianos, Stefan G / Wang, Zhengqiang

Viruses

2021 Volume 13, Issue 3

Abstract: Small molecules targeting the PF74 binding site of the HIV-1 capsid protein (CA) confer potent and mechanistically unique antiviral activities. Structural modifications of PF74 could further the understanding of ligand binding modes, diversify ligand ... ...

Abstract	Small molecules targeting the PF74 binding site of the HIV-1 capsid protein (CA) confer potent and mechanistically unique antiviral activities. Structural modifications of PF74 could further the understanding of ligand binding modes, diversify ligand chemical classes, and allow identification of new variants with balanced antiviral activity and metabolic stability. In the current work, we designed and synthesized three series of PF74-like analogs featuring conformational constraints at the aniline terminus or the phenylalanine carboxamide moiety, and characterized them using a biophysical thermal shift assay (TSA), cell-based antiviral and cytotoxicity assays, and in vitro metabolic stability assays in human and mouse liver microsomes. These studies showed that the two series with the phenylalanine carboxamide moiety replaced by a pyridine or imidazole ring can provide viable hits. Subsequent SAR identified an improved analog
MeSH term(s)	Animals ; Anti-HIV Agents/chemical synthesis ; Anti-HIV Agents/isolation & purification ; Anti-HIV Agents/pharmacology ; Binding Sites ; Capsid Proteins/chemistry ; Capsid Proteins/genetics ; Capsid Proteins/metabolism ; Cell Line ; Drug Design ; HEK293 Cells ; HIV-1/drug effects ; Humans ; Indoles/metabolism ; Indoles/pharmacology ; Liver/drug effects ; Mice ; Microsomes/drug effects ; Models, Molecular ; Molecular Conformation ; Phenylalanine/analogs & derivatives ; Phenylalanine/metabolism ; Phenylalanine/pharmacology ; Small Molecule Libraries/metabolism ; Small Molecule Libraries/pharmacology ; Virus Replication/drug effects
Chemical Substances	Anti-HIV Agents ; Capsid Proteins ; Indoles ; PF-3450074 ; Small Molecule Libraries ; Phenylalanine (47E5O17Y3R)
Language	English
Publishing date	2021-03-15
Publishing country	Switzerland
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2516098-9
ISSN	1999-4915 ; 1999-4915
ISSN (online)	1999-4915
ISSN	1999-4915
DOI	10.3390/v13030479
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Article: Design, Synthesis and Characterization of HIV-1 CA-Targeting Small Molecules: Conformational Restriction of PF74

Viruses. 2021 Mar. 15, v. 13, no. 3

2021

Abstract	Small molecules targeting the PF74 binding site of the HIV-1 capsid protein (CA) confer potent and mechanistically unique antiviral activities. Structural modifications of PF74 could further the understanding of ligand binding modes, diversify ligand chemical classes, and allow identification of new variants with balanced antiviral activity and metabolic stability. In the current work, we designed and synthesized three series of PF74-like analogs featuring conformational constraints at the aniline terminus or the phenylalanine carboxamide moiety, and characterized them using a biophysical thermal shift assay (TSA), cell-based antiviral and cytotoxicity assays, and in vitro metabolic stability assays in human and mouse liver microsomes. These studies showed that the two series with the phenylalanine carboxamide moiety replaced by a pyridine or imidazole ring can provide viable hits. Subsequent SAR identified an improved analog 15 which effectively inhibited HIV-1 (EC₅₀ = 0.31 μM), strongly stabilized CA hexamer (ΔTm = 8.7 °C), and exhibited substantially enhanced metabolic stability (t₁/₂ = 27 min for 15 vs. 0.7 min for PF74). Metabolic profiles from the microsomal stability assay also indicate that blocking the C5 position of the indole ring could lead to increased resistance to oxidative metabolism.
Keywords	aerobiosis ; aniline ; antiviral properties ; carboxamides ; coat proteins ; cytotoxicity ; humans ; imidazole ; indoles ; ligands ; liver microsomes ; mice ; moieties ; phenylalanine ; pyridines
Language	English
Dates of publication	2021-0315
Publishing place	Multidisciplinary Digital Publishing Institute
Document type	Article
Note	NAL-light
ZDB-ID	2516098-9
ISSN	1999-4915
ISSN	1999-4915
DOI	10.3390/v13030479
Database	NAL-Catalogue (AGRICOLA)

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Article: Novel PF74-like small molecules targeting the HIV-1 capsid protein: Balance of potency and metabolic stability.

Wang, Lei / Casey, Mary C / Vernekar, Sanjeev Kumar V / Sahani, Rajkumar Lalji / Kirby, Karen A / Du, Haijuan / Zhang, Huanchun / Tedbury, Philip R / Xie, Jiashu / Sarafianos, Stefan G / Wang, Zhengqiang

Acta pharmaceutica Sinica. B

2020 Volume 11, Issue 3, Page(s) 810–822

Abstract: Of all known small molecules targeting human immunodeficiency virus (HIV) capsid protein (CA), PF74 represents by far the best characterized chemotype, due to its ability to confer antiviral phenotypes in both early and late phases of viral replication. ... ...

Abstract	Of all known small molecules targeting human immunodeficiency virus (HIV) capsid protein (CA), PF74 represents by far the best characterized chemotype, due to its ability to confer antiviral phenotypes in both early and late phases of viral replication. However, the prohibitively low metabolic stability renders PF74 a poor antiviral lead. We report herein our medicinal chemistry efforts toward identifying novel and metabolically stable small molecules targeting the PF74 binding site. Specifically, we replaced the inter-domain-interacting, electron-rich indole ring of PF74 with less electron-rich isosteres, including imidazolidine-2,4-dione, pyrimidine-2,4-dione, and benzamide, and identified four potent antiviral compounds (
Language	English
Publishing date	2020-07-31
Publishing country	Netherlands
Document type	Journal Article
ISSN	2211-3835
ISSN	2211-3835
DOI	10.1016/j.apsb.2020.07.016
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Article ; Online: Toward Structurally Novel and Metabolically Stable HIV-1 Capsid-Targeting Small Molecules.

Vernekar, Sanjeev Kumar V / Sahani, Rajkumar Lalji / Casey, Mary C / Kankanala, Jayakanth / Wang, Lei / Kirby, Karen A / Du, Haijuan / Zhang, Huanchun / Tedbury, Philip R / Xie, Jiashu / Sarafianos, Stefan G / Wang, Zhengqiang

Viruses

2020 Volume 12, Issue 4

Abstract: HIV-1 capsid protein (CA) plays an important role in many steps of viral replication and represents an appealing antiviral target. Several CA-targeting small molecules of various chemotypes have been studied, but the ... ...

Abstract	HIV-1 capsid protein (CA) plays an important role in many steps of viral replication and represents an appealing antiviral target. Several CA-targeting small molecules of various chemotypes have been studied, but the peptidomimetic
MeSH term(s)	Anti-HIV Agents/chemistry ; Anti-HIV Agents/pharmacology ; Binding Sites ; Capsid/chemistry ; Capsid/drug effects ; Capsid/metabolism ; HIV-1/drug effects ; HIV-1/metabolism ; Humans ; Models, Molecular ; Molecular Structure ; Protein Binding ; Structure-Activity Relationship ; Virus Replication/drug effects
Chemical Substances	Anti-HIV Agents
Language	English
Publishing date	2020-04-16
Publishing country	Switzerland
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2516098-9
ISSN	1999-4915 ; 1999-4915
ISSN (online)	1999-4915
ISSN	1999-4915
DOI	10.3390/v12040452
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Chemical profiling of HIV-1 capsid-targeting antiviral PF74.

Wang, Lei / Casey, Mary C / Vernekar, Sanjeev Kumar V / Do, Ha T / Sahani, Rajkumar Lalji / Kirby, Karen A / Du, Haijuan / Hachiya, Atsuko / Zhang, Huanchun / Tedbury, Philip R / Xie, Jiashu / Sarafianos, Stefan G / Wang, Zhengqiang

European journal of medicinal chemistry

2020 Volume 200, Page(s) 112427

Abstract: The capsid protein (CA) of HIV-1 plays essential roles in multiple steps of the viral replication cycle by assembling into functional capsid core, controlling the kinetics of uncoating and nuclear entry, and interacting with various host factors. ... ...

Abstract	The capsid protein (CA) of HIV-1 plays essential roles in multiple steps of the viral replication cycle by assembling into functional capsid core, controlling the kinetics of uncoating and nuclear entry, and interacting with various host factors. Targeting CA represents an attractive yet underexplored antiviral approach. Of all known CA-targeting small molecule chemotypes, the peptidomimetic PF74 is particularly interesting because it binds to the same pocket used by a few important host factors, resulting in highly desirable antiviral phenotypes. However, further development of PF74 entails understanding its pharmacophore and mitigating its poor metabolic stability. We report herein the design, synthesis, and evaluation of a large number of PF74 analogs aiming to provide a comprehensive chemical profiling of PF74 and advance the understanding on its detailed binding mechanism and pharmacophore. The analogs, containing structural variations mainly in the aniline domain and/or the indole domain, were assayed for their effect on stability of CA hexamers, antiviral activity, and cytotoxicity. Selected analogs were also tested for metabolic stability in liver microsomes, alone or in the presence of a CYP3A inhibitor. Collectively, our studies identified important pharmacophore elements and revealed additional binding features of PF74, which could aid in future design of improved ligands to better probe the molecular basis of CA-host factor interactions, design strategies to disrupt them, and ultimately identify viable CA-targeting antiviral leads.
MeSH term(s)	Animals ; Anti-HIV Agents/chemistry ; Anti-HIV Agents/pharmacology ; Capsid Proteins/antagonists & inhibitors ; Capsid Proteins/metabolism ; Cell Line ; Dose-Response Relationship, Drug ; HIV-1/drug effects ; HIV-1/metabolism ; Humans ; Indoles/chemistry ; Indoles/pharmacology ; Mice ; Microbial Sensitivity Tests ; Models, Molecular ; Molecular Structure ; Phenylalanine/analogs & derivatives ; Phenylalanine/chemistry ; Phenylalanine/pharmacology ; Structure-Activity Relationship ; Virus Replication/drug effects
Chemical Substances	Anti-HIV Agents ; Capsid Proteins ; Indoles ; PF-3450074 ; Phenylalanine (47E5O17Y3R)
Language	English
Publishing date	2020-05-12
Publishing country	France
Document type	Journal Article
ZDB-ID	188597-2
ISSN	1768-3254 ; 0009-4374 ; 0223-5234
ISSN (online)	1768-3254
ISSN	0009-4374 ; 0223-5234
DOI	10.1016/j.ejmech.2020.112427
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Article ; Online: Novel HIV-1 capsid-targeting small molecules of the PF74 binding site.

Wang, Lei / Casey, Mary C / Vernekar, Sanjeev Kumar V / Sahani, Rajkumar Lalji / Kankanala, Jayakanth / Kirby, Karen A / Du, Haijuan / Hachiya, Atsuko / Zhang, Huanchun / Tedbury, Philip R / Xie, Jiashu / Sarafianos, Stefan G / Wang, Zhengqiang

European journal of medicinal chemistry

2020 Volume 204, Page(s) 112626

Abstract: The PF74 binding site in HIV-1 capsid protein (CA) is a compelling antiviral drug target. Although PF74 confers mechanistically distinct antiviral phenotypes by competing against host factors for CA binding, it suffers from prohibitively low metabolic ... ...

Abstract	The PF74 binding site in HIV-1 capsid protein (CA) is a compelling antiviral drug target. Although PF74 confers mechanistically distinct antiviral phenotypes by competing against host factors for CA binding, it suffers from prohibitively low metabolic stability. Therefore, there has been increasing interest in designing novel sub-chemotypes of PF74 with similar binding mode and improved metabolic stability. We report herein our efforts to explore the inter-domain interacting indole moiety for designing novel CA-targeting small molecules. Our design includes simple substitution on the indole ring, and more importantly, novel sub-chemotypes with the indole moiety replaced with a few less electron-rich rings. All 56 novel analogs were synthesized and evaluated for antiviral activity, cytotoxicity, and impact on CA hexamer stability. Selected analogs were tested for metabolic stability in liver microsomes. Molecular modeling was performed to verify compound binding to the PF74 site. In the end, 5-hydroxyindole analogs (8,9 and 12) showed improved potency (up to 20-fold) over PF74. Of the novel sub-chemotypes, α- and β-naphthyl analogs (33 and 27) exhibited sub micromolar antiviral potencies comparable to that of PF74. Interestingly, although only moderately inhibiting HIV-1 (single-digit micromolar EC
MeSH term(s)	Anti-HIV Agents/chemistry ; Anti-HIV Agents/pharmacology ; Binding Sites ; Capsid/drug effects ; Capsid/metabolism ; Cell Line ; HIV-1/metabolism ; HIV-1/physiology ; Humans ; Indoles/pharmacology ; Microsomes, Liver/drug effects ; Molecular Docking Simulation ; Structure-Activity Relationship ; Virus Replication/drug effects
Chemical Substances	Anti-HIV Agents ; Indoles
Language	English
Publishing date	2020-07-19
Publishing country	France
Document type	Journal Article
ZDB-ID	188597-2
ISSN	1768-3254 ; 0009-4374 ; 0223-5234
ISSN (online)	1768-3254
ISSN	0009-4374 ; 0223-5234
DOI	10.1016/j.ejmech.2020.112626
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Article: Toward Structurally Novel and Metabolically Stable HIV-1 Capsid-Targeting Small Molecules

Viruses. 2020 Apr. 16, v. 12, no. 4

2020

Abstract	HIV-1 capsid protein (CA) plays an important role in many steps of viral replication and represents an appealing antiviral target. Several CA-targeting small molecules of various chemotypes have been studied, but the peptidomimetic PF74 has drawn particular interest due to its potent antiviral activity, well-characterized binding mode, and unique mechanism of action. Importantly, PF74 competes against important host factors for binding, conferring highly desirable antiviral phenotypes. However, further development of PF74 is hindered by its prohibitively poor metabolic stability, which necessitates the search for structurally novel and metabolically stable chemotypes. We have conducted a pharmacophore-based shape similarity search for compounds mimicking PF74. We report herein the analog synthesis and structure-activity relationship (SAR) of two hits from the search, and a third hit designed via molecular hybridization. All analogs were characterized for their effect on CA hexamer stability, antiviral activity, and cytotoxicity. These assays identified three active compounds that moderately stabilize CA hexamer and inhibit HIV-1. The most potent analog (10) inhibited HIV-1 comparably to PF74 but demonstrated drastically improved metabolic stability in liver microsomes (31 min vs. 0.7 min t₁/₂). Collectively, the current studies identified a structurally novel and metabolically stable PF74-like chemotype for targeting HIV-1 CA.
Keywords	Human immunodeficiency virus 1 ; active ingredients ; antiviral properties ; chemotypes ; coat proteins ; cytotoxicity ; liver microsomes ; mechanism of action ; nucleic acid hybridization ; phenotype ; structure-activity relationships ; virus replication
Language	English
Dates of publication	2020-0416
Publishing place	Multidisciplinary Digital Publishing Institute
Document type	Article
ZDB-ID	2516098-9
ISSN	1999-4915
ISSN	1999-4915
DOI	10.3390/v12040452
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Design, synthesis and biological evaluations of N-Hydroxy thienopyrimidine-2,4-diones as inhibitors of HIV reverse transcriptase-associated RNase H.

Kankanala, Jayakanth / Kirby, Karen A / Huber, Andrew D / Casey, Mary C / Wilson, Daniel J / Sarafianos, Stefan G / Wang, Zhengqiang

European journal of medicinal chemistry

2017 Volume 141, Page(s) 149–161

Abstract: Human immunodeficiency virus (HIV) reverse transcriptase (RT) associated ribonuclease H (RNase H) is the only HIV enzymatic function not targeted by current antiviral drugs. Although various chemotypes have been reported to inhibit HIV RNase H, few have ... ...

Abstract	Human immunodeficiency virus (HIV) reverse transcriptase (RT) associated ribonuclease H (RNase H) is the only HIV enzymatic function not targeted by current antiviral drugs. Although various chemotypes have been reported to inhibit HIV RNase H, few have shown significant antiviral activities. We report herein the design, synthesis and biological evaluation of a novel N-hydroxy thienopyrimidine-2,3-dione chemotype (11) which potently and selectively inhibited RNase H with considerable potency against HIV-1 in cell culture. Current structure-activity-relationship (SAR) identified analogue 11d as a nanomolar inhibitor of RNase H (IC
Language	English
Publishing date	2017-12-01
Publishing country	France
Document type	Journal Article
ZDB-ID	188597-2
ISSN	1768-3254 ; 0009-4374 ; 0223-5234
ISSN (online)	1768-3254
ISSN	0009-4374 ; 0223-5234
DOI	10.1016/j.ejmech.2017.09.054
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Article ; Online: 6-Cyclohexylmethyl-3-hydroxypyrimidine-2,4-dione as an inhibitor scaffold of HIV reverase transcriptase: Impacts of the 3-OH on inhibiting RNase H and polymerase.

Tang, Jing / Kirby, Karen A / Huber, Andrew D / Casey, Mary C / Ji, Juan / Wilson, Daniel J / Sarafianos, Stefan G / Wang, Zhengqiang

European journal of medicinal chemistry

2017 Volume 128, Page(s) 168–179

Abstract: 3-Hydroxypyrimidine-2,4-dione (HPD) represents a versatile chemical core in the design of inhibitors of human immunodeficiency virus (HIV) reverse transcriptase (RT)-associated RNase H and integrase strand transfer (INST). We report herein the design, ... ...

Abstract	3-Hydroxypyrimidine-2,4-dione (HPD) represents a versatile chemical core in the design of inhibitors of human immunodeficiency virus (HIV) reverse transcriptase (RT)-associated RNase H and integrase strand transfer (INST). We report herein the design, synthesis and biological evaluation of an HPD subtype (4) featuring a cyclohexylmethyl group at the C-6 position. Antiviral testing showed that most analogues of 4 inhibited HIV-1 in the low nanomolar to submicromolar range, without cytotoxicity at concentrations up to 100 μM. Biochemically, these analogues dually inhibited both the polymerase (pol) and the RNase H functions of RT, but not INST. Co-crystal structure of 4a with RT revealed a nonnucleoside RT inhibitor (NNRTI) binding mode. Interestingly, chemotype 11, the synthetic precursor of 4 lacking the 3-OH group, did not inhibit RNase H while potently inhibiting pol. By virtue of the potent antiviral activity and biochemical RNase H inhibition, HPD subtype 4 could provide a viable platform for eventually achieving potent and selective RNase H inhibition through further medicinal chemistry.
MeSH term(s)	Anti-HIV Agents/chemical synthesis ; Anti-HIV Agents/pharmacology ; Binding Sites ; Crystallization ; HIV Infections/drug therapy ; HIV Infections/virology ; HIV Reverse Transcriptase/antagonists & inhibitors ; HIV-1/drug effects ; Humans ; Models, Molecular ; Molecular Docking Simulation ; Polymerase Chain Reaction ; Pyrimidinones/chemical synthesis ; Pyrimidinones/pharmacology ; Reverse Transcriptase Inhibitors/chemical synthesis ; Reverse Transcriptase Inhibitors/pharmacology ; Ribonuclease H, Human Immunodeficiency Virus/antagonists & inhibitors ; Structure-Activity Relationship ; Uracil/analogs & derivatives ; Uracil/chemical synthesis ; Uracil/pharmacology
Chemical Substances	6-cyclohexylmethyl-3-hydroxypyrimidine-2,4-dione ; Anti-HIV Agents ; Pyrimidinones ; Reverse Transcriptase Inhibitors ; Uracil (56HH86ZVCT) ; HIV Reverse Transcriptase (EC 2.7.7.49) ; Ribonuclease H, Human Immunodeficiency Virus (EC 3.1.26.4)
Language	English
Publishing date	2017-03-10
Publishing country	France
Document type	Journal Article
ZDB-ID	188597-2
ISSN	1768-3254 ; 0009-4374 ; 0223-5234
ISSN (online)	1768-3254
ISSN	0009-4374 ; 0223-5234
DOI	10.1016/j.ejmech.2017.01.041
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