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Article ; Online: Backbone NMR resonance assignment of the apo human Tsg101-UEV domain.

Moschidi, Danai / Cantrelle, François-Xavier / Boll, Emmanuelle / Hanoulle, Xavier

2023 Volume 17, Issue 1, Page(s) 49–54

Abstract: The Endosomal Sorting Complex Required for Transport (ESCRT) pathway, through inverse topology membrane remodeling, is involved in many biological functions, such as ubiquitinated membrane receptor trafficking and degradation, multivesicular bodies (MVB) ...

Abstract	The Endosomal Sorting Complex Required for Transport (ESCRT) pathway, through inverse topology membrane remodeling, is involved in many biological functions, such as ubiquitinated membrane receptor trafficking and degradation, multivesicular bodies (MVB) formation and cytokinesis. Dysfunctions in ESCRT pathway have been associated to several human pathologies, such as cancers and neurodegenerative diseases. The ESCRT machinery is also hijacked by many enveloped viruses to bud away from the plasma membrane of infected cells. Human tumor susceptibility gene 101 (Tsg101) protein is an important ESCRT-I complex component. The structure of the N-terminal ubiquitin E2 variant (UEV) domain of Tsg101 (Tsg101-UEV) comprises an ubiquitin binding pocket next to a late domain [P(S/T)AP] binding groove. These two binding sites have been shown to be involved both in the physiological roles of ESCRT-I and in the release of the viral particles, and thus are attractive targets for antivirals. The structure of the Tsg101-UEV domain has been characterized, using X-ray crystallography or NMR spectroscopy, either in its apo-state or bound to ubiquitin or late domains. In this study, we report the backbone NMR resonance assignments, including the proline signals, of the apo human Tsg101-UEV domain, that so far was not publicly available. These data, that are in good agreement with the crystallographic structure of Tsg101-UEV domain, can therefore be used for further NMR studies, including protein-protein interaction studies and drug discovery.
MeSH term(s)	Humans ; Ubiquitin/metabolism ; Nuclear Magnetic Resonance, Biomolecular ; DNA-Binding Proteins/chemistry ; Endosomal Sorting Complexes Required for Transport/chemistry ; Endosomal Sorting Complexes Required for Transport/genetics ; Endosomal Sorting Complexes Required for Transport/metabolism
Chemical Substances	Tsg101 protein ; Ubiquitin ; DNA-Binding Proteins ; Endosomal Sorting Complexes Required for Transport
Language	English
Publishing date	2023-02-06
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2388861-1
ISSN	1874-270X ; 1874-2718
ISSN (online)	1874-270X
ISSN	1874-2718
DOI	10.1007/s12104-023-10119-5
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Article ; Online: Magnetic resonance investigation of conformational responses of tau protein to specific phosphorylation.

Lasorsa, Alessia / Merzougui, Hamida / Cantrelle, François-Xavier / Sicoli, Giuseppe / Dupré, Elian / Hanoulle, Xavier / Belle, Valérie / Smet-Nocca, Caroline / Landrieu, Isabelle

Biophysical chemistry

2023 Volume 305, Page(s) 107155

Abstract: Intrinsically disordered proteins (IDPs) are known to adopt many rapidly interconverting structures, making it difficult to pinpoint the specific conformational states that are relevant for their function. Tau is an important IDP, and its conformation is ...

Abstract	Intrinsically disordered proteins (IDPs) are known to adopt many rapidly interconverting structures, making it difficult to pinpoint the specific conformational states that are relevant for their function. Tau is an important IDP, and its conformation is known to be affected by post-translational modifications (PTMs), such as phosphorylation. To investigate the effect of specific phosphorylation on full-length Tau's dynamic global conformation, we employed a combination of nuclear magnetic resonance-based paramagnetic relaxation interference methods and electron paramagnetic resonance spectroscopy. By reproducing the AT8 epitope, comprising exclusive phosphorylation at residues S202 and T205, we were able to identify conformations specific to phosphorylated Tau, which exhibited a tendency towards less compact states. These mechanistic details are of significance to understand the path leading from soluble Tau to the ordered structure of Tau fibers. This approach proved to be successful for studying the conformational changes of (phosphorylated) full-length Tau and can potentially be extended to the study of other IDPs that undergo various PTMs.
MeSH term(s)	Phosphorylation ; tau Proteins/chemistry ; Magnetic Resonance Spectroscopy ; Protein Conformation ; Electron Spin Resonance Spectroscopy ; Intrinsically Disordered Proteins/chemistry ; Nuclear Magnetic Resonance, Biomolecular
Chemical Substances	tau Proteins ; Intrinsically Disordered Proteins
Language	English
Publishing date	2023-12-14
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	185052-0
ISSN	1873-4200 ; 0301-4622
ISSN (online)	1873-4200
ISSN	0301-4622
DOI	10.1016/j.bpc.2023.107155
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Article: NMR and circular dichroism data for domain 2 of the HCV NS5A protein phosphorylated by the Casein Kinase II.

Bessa, Luiza M / Schneider, Robert / Hanoulle, Xavier

Data in brief

2018 Volume 17, Page(s) 325–333

Abstract: The Hepatitis C Virus (HCV) nonstructural 5A protein (NS5A) is a phosphoprotein (Evans et al., 2004; Ross-Thriepland and Harris, 2014) [1], [2] composed of an N-terminal well-structured domain and two C-terminal intrinsically disordered domains ( ... ...

Abstract	The Hepatitis C Virus (HCV) nonstructural 5A protein (NS5A) is a phosphoprotein (Evans et al., 2004; Ross-Thriepland and Harris, 2014) [1], [2] composed of an N-terminal well-structured domain and two C-terminal intrinsically disordered domains (Moradpour et al., 2007; Bartenschlager et al., 2013; Badillo et al., 2017) [3], [4], [5]. So far, no precise molecular function has been identified for this viral protein (Ross-Thriepland and Harris, 2015) [6] which is required for viral replication (Tellinghuisen et al., 2008) [7]. In this article, we present datasets of NMR and circular dichroism analyses of the domain 2 of the HCV NS5A protein (NS5A-D2) phosphorylated
Language	English
Publishing date	2018-01-31
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	2786545-9
ISSN	2352-3409
ISSN	2352-3409
DOI	10.1016/j.dib.2018.01.038
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Article: Glycan Shielding and Modulation of Hepatitis C Virus Neutralizing Antibodies.

Lavie, Muriel / Hanoulle, Xavier / Dubuisson, Jean

Frontiers in immunology

2018 Volume 9, Page(s) 910

Abstract: Hepatitis C virus (HCV) envelope glycoprotein heterodimer, E1E2, plays an essential role in virus entry and assembly. Furthermore, due to their exposure at the surface of the virion, these proteins are the major targets of anti-HCV neutralizing ... ...

Abstract	Hepatitis C virus (HCV) envelope glycoprotein heterodimer, E1E2, plays an essential role in virus entry and assembly. Furthermore, due to their exposure at the surface of the virion, these proteins are the major targets of anti-HCV neutralizing antibodies. Their ectodomain are heavily glycosylated with up to 5 sites on E1 and up to 11 sites on E2 modified by N-linked glycans. Thus, one-third of the molecular mass of E1E2 heterodimer corresponds to glycans. Despite the high sequence variability of E1 and E2, N-glycosylation sites of these proteins are generally conserved among the seven major HCV genotypes. N-glycans have been shown to be involved in E1E2 folding and modulate different functions of the envelope glycoproteins. Indeed, site-directed mutagenesis studies have shown that specific glycans are needed for virion assembly and infectivity. They can notably affect envelope protein entry functions by modulating their affinity for HCV receptors and their fusion activity. Importantly, glycans have also been shown to play a key role in immune evasion by masking antigenic sites targeted by neutralizing antibodies. It is well known that the high mutational rate of HCV polymerase facilitates the appearance of neutralization resistant mutants, and occurrence of mutations leading to glycan shifting is one of the mechanisms used by this virus to escape host humoral immune response. As a consequence of the importance of the glycan shield for HCV immune evasion, the deletion of N-glycans also leads to an increase in E1E2 immunogenicity and can induce a more potent antibody response against HCV.
MeSH term(s)	Animals ; Antibodies, Neutralizing/immunology ; Cell Line ; Glycosylation ; Hepacivirus/immunology ; Hepatitis C Antibodies/immunology ; Humans ; Immunity, Humoral ; Mice ; Polysaccharides/chemistry ; Polysaccharides/immunology ; Viral Envelope Proteins/immunology ; Viral Envelope Proteins/metabolism ; Virus Assembly ; Virus Internalization
Chemical Substances	Antibodies, Neutralizing ; Hepatitis C Antibodies ; Polysaccharides ; Viral Envelope Proteins
Language	English
Publishing date	2018-04-27
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2606827-8
ISSN	1664-3224
ISSN	1664-3224
DOI	10.3389/fimmu.2018.00910
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Article ; Online: X-ray structure of alisporivir in complex with cyclophilin A at 1.5 Å resolution.

Dujardin, Marie / Bouckaert, Julie / Rucktooa, Prakash / Hanoulle, Xavier

Acta crystallographica. Section F, Structural biology communications

2018 Volume 74, Issue Pt 9, Page(s) 583–592

Abstract: Alisporivir (ALV) is an 11-amino-acid hydrophobic cyclic peptide with N-methyl-D-alanine and N-ethyl-L-valine (NEV) residues at positions 3 and 4, respectively. ALV is a non-immunosuppressive cyclosporin A (CsA) derivative. This inhibitor targets ... ...

Abstract	Alisporivir (ALV) is an 11-amino-acid hydrophobic cyclic peptide with N-methyl-D-alanine and N-ethyl-L-valine (NEV) residues at positions 3 and 4, respectively. ALV is a non-immunosuppressive cyclosporin A (CsA) derivative. This inhibitor targets cyclophilins (Cyps), a family of proteins with peptidyl-prolyl cis/trans isomerase enzymatic activity. Cyps act as protein chaperones and are involved in numerous cellular functions. Moreover, Cyps have been shown to be an essential cofactor for the replication of many viruses, including Hepatitis C virus and Human immunodeficiency virus, and have also been shown to be involved in mitochondrial diseases. For these reasons, cyclophilins represent an attractive drug target. The structure of ALV in complex with cyclophilin A (CypA), the most abundant Cyp in humans, has been determined at 1.5 Å resolution. This first structure of the CypA-ALV complex shows that the binding of ALV is highly similar to that of CsA. The high resolution allowed the unambiguous determination of the conformations of residues 3 and 4 in ALV when bound to its target. In particular, the side-chain conformation of NEV4 precludes the interaction of the CypA-ALV complex with calcineurin, a cellular protein phosphatase involved in the immune response, which explains the non-immunosuppressive property of ALV. This study provides detailed molecular insights into the CypA-ALV interaction.
MeSH term(s)	Amino Acid Motifs ; Binding Sites ; Cloning, Molecular ; Crystallography, X-Ray ; Cyclophilin A/chemistry ; Cyclophilin A/genetics ; Cyclophilin A/metabolism ; Cyclosporine/chemistry ; Cyclosporine/metabolism ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Gene Expression ; Genetic Vectors/chemistry ; Genetic Vectors/metabolism ; Humans ; Kinetics ; Models, Molecular ; Protein Binding ; Protein Conformation, alpha-Helical ; Protein Conformation, beta-Strand ; Protein Interaction Domains and Motifs ; Protein Multimerization ; Protein Subunits/chemistry ; Protein Subunits/genetics ; Protein Subunits/metabolism ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism
Chemical Substances	Protein Subunits ; Recombinant Proteins ; Cyclosporine (83HN0GTJ6D) ; Cyclophilin A (EC 5.2.1.-) ; alisporivir (VBP9099AA6)
Language	English
Publishing date	2018-09-03
Publishing country	United States
Document type	Journal Article
ISSN	2053-230X
ISSN (online)	2053-230X
DOI	10.1107/S2053230X18010415
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Article: NMR and circular dichroism data for domain 2 of the HCV NS5A protein phosphorylated by the Casein Kinase II

Bessa, Luiza M. / Schneider, Robert / Hanoulle, Xavier

Data in Brief. 2018 Apr., v. 17

2018

Abstract: The Hepatitis C Virus (HCV)¹1HCV: Hepatitis C Virus; HSQC: heteronuclear single-quantum coherence; NS5A: nonstructural protein 5A; NS5A-D2: domain 2 of the nonstructural protein 5A; CKII: Casein kinase II, NS5A-D2_CKII: NS5A-D2 phosphorylated by CKII; ... ...

Abstract	The Hepatitis C Virus (HCV)¹1HCV: Hepatitis C Virus; HSQC: heteronuclear single-quantum coherence; NS5A: nonstructural protein 5A; NS5A-D2: domain 2 of the nonstructural protein 5A; CKII: Casein kinase II, NS5A-D2_CKII: NS5A-D2 phosphorylated by CKII; CSP: combined chemical shift perturbations; THP: (Tris(hydroxypropyl)phosphine). nonstructural 5A protein (NS5A) is a phosphoprotein (Evans et al., 2004; Ross-Thriepland and Harris, 2014) [1,2] composed of an N-terminal well-structured domain and two C-terminal intrinsically disordered domains (Moradpour et al., 2007; Bartenschlager et al., 2013; Badillo et al., 2017) [3–5]. So far, no precise molecular function has been identified for this viral protein (Ross-Thriepland and Harris, 2015) [6] which is required for viral replication (Tellinghuisen et al., 2008) [7]. In this article, we present datasets of NMR and circular dichroism analyses of the domain 2 of the HCV NS5A protein (NS5A-D2) phosphorylated in vitro by the Casein Kinase II (CKII) (Dal Pero et al., 2007; Clemens et al., 2015; Masak et al., 2014; Kim et al., 2014) [8–11]. We describe the in vitro phosphorylation of the serine 288 (pS288) of NS5A-D2 by CKII and report the circular dichroism spectrum of the phosphorylated domain (NS5-D2_CKII). This data article also contains the ¹H, ¹⁵N and ¹³C NMR chemical shift assignments (HN, N, Cα, Cβ and C’) for the phosphorylated NS5A-D2 domain, and an assigned ¹H,¹⁵N-HSQC spectrum is shown. The NMR data have been acquired on an 800 MHz spectrometer. These NMR data have been used to calculate both the ¹H,¹⁵N combined chemical shift perturbations (CSP) induced by the phosphorylation of pS288 and the secondary structural propensity (SSP) scores that describe the structural tendencies in this intrinsically disordered domain. The circular dichroism spectrum and the SSP scores of NS5A-D2_CKII have been compared with those of unphosphorylated NS5A-D2 [12,13].
Keywords	Hepatitis C virus ; circular dichroism spectroscopy ; data collection ; non-specific serine/threonine protein kinase ; phosphine ; phosphoproteins ; protein phosphorylation ; serine ; spectrometers ; viral nonstructural proteins ; virus replication
Language	English
Dates of publication	2018-04
Size	p. 325-333.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	2786545-9
ISSN	2352-3409
ISSN	2352-3409
DOI	10.1016/j.dib.2018.01.038
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Article ; Online: A selection and optimization strategy for single-domain antibodies targeting the PHF6 linear peptide within the tau intrinsically disordered protein.

Mortelecque, Justine / Zejneli, Orgeta / Bégard, Séverine / Simões, Margarida C / ElHajjar, Lea / Nguyen, Marine / Cantrelle, François-Xavier / Hanoulle, Xavier / Rain, Jean-Christophe / Colin, Morvane / Gomes, Cláudio M / Buée, Luc / Landrieu, Isabelle / Danis, Clément / Dupré, Elian

The Journal of biological chemistry

2024 Volume 300, Issue 4, Page(s) 107163

Abstract: The use of variable domain of the heavy-chain of the heavy-chain-only antibodies (VHHs) as disease-modifying biomolecules in neurodegenerative disorders holds promises, including targeting of aggregation-sensitive proteins. Exploitation of their clinical ...

Abstract	The use of variable domain of the heavy-chain of the heavy-chain-only antibodies (VHHs) as disease-modifying biomolecules in neurodegenerative disorders holds promises, including targeting of aggregation-sensitive proteins. Exploitation of their clinical values depends however on the capacity to deliver VHHs with optimal physico-chemical properties for their specific context of use. We described previously a VHH with high therapeutic potential in a family of neurodegenerative diseases called tauopathies. The activity of this promising parent VHH named Z70 relies on its binding within the central region of the tau protein. Accordingly, we carried out random mutagenesis followed by yeast two-hybrid screening to obtain optimized variants. The VHHs selected from this initial screen targeted the same epitope as VHH Z70 as shown using NMR spectroscopy and had indeed improved binding affinities according to dissociation constant values obtained by surface plasmon resonance spectroscopy. The improved affinities can be partially rationalized based on three-dimensional structures and NMR data of three complexes consisting of an optimized VHH and a peptide containing the tau epitope. Interestingly, the ability of the VHH variants to inhibit tau aggregation and seeding could not be predicted from their affinity alone. We indeed showed that the in vitro and in cellulo VHH stabilities are other limiting key factors to their efficacy. Our results demonstrate that only a complete pipeline of experiments, here described, permits a rational selection of optimized VHH variants, resulting in the selection of VHH variants with higher affinities and/or acting against tau seeding in cell models.
MeSH term(s)	tau Proteins/immunology ; tau Proteins/metabolism ; tau Proteins/chemistry ; tau Proteins/genetics ; Humans ; Single-Domain Antibodies/chemistry ; Single-Domain Antibodies/immunology ; Intrinsically Disordered Proteins/chemistry ; Intrinsically Disordered Proteins/immunology ; Intrinsically Disordered Proteins/metabolism ; Intrinsically Disordered Proteins/genetics ; Epitopes/chemistry ; Epitopes/immunology ; Peptides/chemistry ; Peptides/immunology
Chemical Substances	tau Proteins ; Single-Domain Antibodies ; Intrinsically Disordered Proteins ; Epitopes ; Peptides ; MAPT protein, human
Language	English
Publishing date	2024-03-12
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2024.107163
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Article ; Online: Conformation and Affinity Modulations by Multiple Phosphorylation Occurring in the BIN1 SH3 Domain Binding Site of the Tau Protein Proline-Rich Region.

Lasorsa, Alessia / Bera, Krishnendu / Malki, Idir / Dupré, Elian / Cantrelle, François-Xavier / Merzougui, Hamida / Sinnaeve, Davy / Hanoulle, Xavier / Hritz, Jozef / Landrieu, Isabelle

Biochemistry

2023 Volume 62, Issue 11, Page(s) 1631–1642

Abstract: An increase in phosphorylation of the Tau protein is associated with Alzheimer's disease (AD) progression through unclear molecular mechanisms. In general, phosphorylation modifies the interaction of intrinsically disordered proteins, such as Tau, with ... ...

Abstract	An increase in phosphorylation of the Tau protein is associated with Alzheimer's disease (AD) progression through unclear molecular mechanisms. In general, phosphorylation modifies the interaction of intrinsically disordered proteins, such as Tau, with other proteins; however, elucidating the structural basis of this regulation mechanism remains challenging. The bridging integrator-1 gene is an AD genetic determinant whose gene product, BIN1, directly interacts with Tau. The proline-rich motif recognized within a Tau(210-240) peptide by the SH3 domain of BIN1 (BIN1 SH3) is defined as
MeSH term(s)	Humans ; tau Proteins/metabolism ; Phosphorylation ; src Homology Domains ; Protein Binding ; Alzheimer Disease/metabolism ; Peptides/chemistry ; Binding Sites ; Proline/metabolism ; Nuclear Proteins/metabolism ; Tumor Suppressor Proteins/chemistry ; Adaptor Proteins, Signal Transducing/metabolism
Chemical Substances	tau Proteins ; Peptides ; Proline (9DLQ4CIU6V) ; BIN1 protein, human ; Nuclear Proteins ; Tumor Suppressor Proteins ; Adaptor Proteins, Signal Transducing
Language	English
Publishing date	2023-05-11
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/acs.biochem.2c00717
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Article ; Online: The phosphatidylserine receptor TIM1 promotes infection of enveloped hepatitis E virus.

Corneillie, Laura / Lemmens, Irma / Montpellier, Claire / Ferrié, Martin / Weening, Karin / Van Houtte, Freya / Hanoulle, Xavier / Cocquerel, Laurence / Amara, Ali / Tavernier, Jan / Meuleman, Philip

Cellular and molecular life sciences : CMLS

2023 Volume 80, Issue 11, Page(s) 326

Abstract: The hepatitis E virus (HEV) is an underestimated RNA virus of which the viral life cycle and pathogenicity remain partially understood and for which specific antivirals are lacking. The virus exists in two forms: nonenveloped HEV that is shed in feces ... ...

Abstract	The hepatitis E virus (HEV) is an underestimated RNA virus of which the viral life cycle and pathogenicity remain partially understood and for which specific antivirals are lacking. The virus exists in two forms: nonenveloped HEV that is shed in feces and transmits between hosts; and membrane-associated, quasi-enveloped HEV that circulates in the blood. It is suggested that both forms employ different mechanisms for cellular entry and internalization but little is known about the exact mechanisms. Interestingly, the membrane of enveloped HEV is enriched with phosphatidylserine, a natural ligand for the T-cell immunoglobulin and mucin domain-containing protein 1 (TIM1) during apoptosis and involved in 'apoptotic mimicry', a process by which viruses hijack the apoptosis pathway to promote infection. We here investigated the role of TIM1 in the entry process of HEV. We determined that HEV infection with particles derived from culture supernatant, which are cloaked by host-derived membranes (eHEV), was significantly impaired after knockout of TIM1, whereas infection with intracellular HEV particles (iHEV) was unaffected. eHEV infection was restored upon TIM1 expression; and enhanced after ectopic TIM1 expression. The significance of TIM1 during entry was further confirmed by viral binding assay, and point mutations of the PS-binding pocket diminished eHEV infection. In addition, Annexin V, a PS-binding molecule also significantly reduced infection. Taken together, our findings support a role for TIM1 in eHEV-mediated cell entry, facilitated by the PS present on the viral membrane, a strategy HEV may use to promote viral spread throughout the infected body.
MeSH term(s)	Hepatitis E virus/genetics ; Hepatitis E virus/metabolism ; Virus Internalization ; Receptors, Cell Surface/metabolism ; Viruses
Chemical Substances	phosphatidylserine receptor ; Receptors, Cell Surface
Language	English
Publishing date	2023-10-13
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	1358415-7
ISSN	1420-9071 ; 1420-682X
ISSN (online)	1420-9071
ISSN	1420-682X
DOI	10.1007/s00018-023-04977-4
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Article ; Online: Identification of a Potential Inhibitor of the FIV p24 Capsid Protein and Characterization of Its Binding Site.

Long, Mathieu / Cantrelle, François-Xavier / Robert, Xavier / Boll, Emmanuelle / Sierra, Natalia / Gouet, Patrice / Hanoulle, Xavier / Alvarez, Guzmán I / Guillon, Christophe

Biochemistry

2021 Volume 60, Issue 24, Page(s) 1896–1908

Abstract: Feline immunodeficiency virus (FIV) is a veterinary infective agent for which there is currently no efficient drug available. Drugs targeting the lentivirus capsid are currently under development for the treatment of human immunodeficiency virus 1 (HIV-1) ...

Abstract	Feline immunodeficiency virus (FIV) is a veterinary infective agent for which there is currently no efficient drug available. Drugs targeting the lentivirus capsid are currently under development for the treatment of human immunodeficiency virus 1 (HIV-1). Here we describe a lead compound that interacts with the FIV capsid. This compound,
MeSH term(s)	Animals ; Antiviral Agents/pharmacology ; Benzimidazoles/pharmacology ; Binding Sites ; Capsid/metabolism ; Capsid Proteins/antagonists & inhibitors ; Capsid Proteins/metabolism ; Cats ; Gene Products, gag/antagonists & inhibitors ; Gene Products, gag/metabolism ; Immunodeficiency Virus, Feline/drug effects ; Immunodeficiency Virus, Feline/metabolism ; Lead/pharmacology ; Protein Domains
Chemical Substances	Antiviral Agents ; Benzimidazoles ; Capsid Proteins ; Gene Products, gag ; p24 protein, Feline immunodeficiency virus ; Lead (2P299V784P)
Language	English
Publishing date	2021-06-05
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/acs.biochem.1c00228
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