The N-terminal region containing the zinc finger domain of tobacco streak virus coat protein is essential for the formation of virus-like particles

Mathur, Chhavi; Mohan, Kalyani; Rani, T.R.Usha; Reddy, M. Krishna; Savithri, H.S.

doi:10.1007/s00705-013-1822-4

Cited by 4 publications

(3 citation statements)

References 44 publications

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“…Viral proteins from divergent influenza A, hendra, measles, and herpes simplex viruses also appear to use LLPS for virus replication ( Alenquer et al, 2019 ; McSwiggen et al, 2019 ; Zhou et al, 2019 ). In a greater perspective, the association between viral nucleoproteins and vRNA appears responsible for LLPS ( Alberti et al, 2019 ; Kondo et al, 2013 ; Lifland et al, 2012 ; Nikolic et al, 2019 ; Zhou et al, 2019 ), and the association between ZnF and RING finger proteins lead to the assembly of virus factories, virus-like particles, and inclusion bodies ( Brick et al, 1998 ; Fehling et al, 2012 ; Hanslip et al, 2006 ; Hoenen et al, 2012 ; Mathur et al, 2014 ; Nerenberg et al, 2005 ; Senkevich et al, 1995 ). Our work demonstrates that Gag and pan-retrovirus NC proteins induce Zn 2+ -dependent LLPS and SGs, supporting the notion that translational silencing of vRNA ushers it into trafficking cytoplasmic RNPs slated for virus assembly.…”

Section: Discussionmentioning

confidence: 99%

Pan-retroviral Nucleocapsid-Mediated Phase Separation Regulates Genomic RNA Positioning and Trafficking

et al. 2020

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Section: Discussionmentioning

confidence: 99%

Pan-retroviral Nucleocapsid-Mediated Phase Separation Regulates Genomic RNA Positioning and Trafficking

et al. 2020

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“…Viral proteins from divergent viruses, including influenza A, hendra, and herpes simplex, utilize LLPS to generate “liquid organelles” assisting replication [ 33 , 34 , 35 ]. Across divergent virus families, association of viral nucleoproteins (N) and viral RNA (vRNA) promotes LLPS [ 34 , 36 , 37 , 38 ], and association of zinc fingers (ZnFs) and RING finger proteins establishes virus factories, VLPs, and inclusion bodies [ 39 , 40 , 41 , 42 , 43 , 44 , 45 ]. As the ability of proteins to phase-separate stems from their PrLDs, large in silico meta-analyses demonstrate disproportionately higher degrees of PrLDs in viral proteins relative to eukaryotic proteins [ 46 ].…”

Section: Introductionmentioning

confidence: 99%

Zinc and Copper Ions Differentially Regulate Prion-Like Phase Separation Dynamics of Pan-Virus Nucleocapsid Biomolecular Condensates

Monette

Mouland

2020

Viruses

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Liquid-liquid phase separation (LLPS) is a rapidly growing research focus due to numerous demonstrations that many cellular proteins phase-separate to form biomolecular condensates (BMCs) that nucleate membraneless organelles (MLOs). A growing repertoire of mechanisms supporting BMC formation, composition, dynamics, and functions are becoming elucidated. BMCs are now appreciated as required for several steps of gene regulation, while their deregulation promotes pathological aggregates, such as stress granules (SGs) and insoluble irreversible plaques that are hallmarks of neurodegenerative diseases. Treatment of BMC-related diseases will greatly benefit from identification of therapeutics preventing pathological aggregates while sparing BMCs required for cellular functions. Numerous viruses that block SG assembly also utilize or engineer BMCs for their replication. While BMC formation first depends on prion-like disordered protein domains (PrLDs), metal ion-controlled RNA-binding domains (RBDs) also orchestrate their formation. Virus replication and viral genomic RNA (vRNA) packaging dynamics involving nucleocapsid (NC) proteins and their orthologs rely on Zinc (Zn) availability, while virus morphology and infectivity are negatively influenced by excess Copper (Cu). While virus infections modify physiological metal homeostasis towards an increased copper to zinc ratio (Cu/Zn), how and why they do this remains elusive. Following our recent finding that pan-retroviruses employ Zn for NC-mediated LLPS for virus assembly, we present a pan-virus bioinformatics and literature meta-analysis study identifying metal-based mechanisms linking virus-induced BMCs to neurodegenerative disease processes. We discover that conserved degree and placement of PrLDs juxtaposing metal-regulated RBDs are associated with disease-causing prion-like proteins and are common features of viral proteins responsible for virus capsid assembly and structure. Virus infections both modulate gene expression of metalloproteins and interfere with metal homeostasis, representing an additional virus strategy impeding physiological and cellular antiviral responses. Our analyses reveal that metal-coordinated virus NC protein PrLDs initiate LLPS that nucleate pan-virus assembly and contribute to their persistence as cell-free infectious aerosol droplets. Virus aerosol droplets and insoluble neurological disease aggregates should be eliminated by physiological or environmental metals that outcompete PrLD-bound metals. While environmental metals can control virus spreading via aerosol droplets, therapeutic interference with metals or metalloproteins represent additional attractive avenues against pan-virus infection and virus-exacerbated neurological diseases.

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“…Zn 2+ mediates the conformational changes of hepatitis B virus (HBV) CP to increase the production of virus-like particles (VLPs) [ 29 ]. In plants, the zinc finger domain in tobacco streak virus (TSV) CP is required for the assembly of VLPs, and the stability of TSV particles is significantly increased in the presence of Zn 2+ [ 30 ].…”

Section: Introductionmentioning

confidence: 99%

Zn2+-dependent association of cysteine-rich protein with virion orchestrates morphogenesis of rod-shaped viruses

Yue,

Jiang,

et al. 2024

PLoS Pathog

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The majority of rod-shaped and some filamentous plant viruses encode a cysteine-rich protein (CRP) that functions in viral virulence; however, the roles of these CRPs in viral infection remain largely unknown. Here, we used barley stripe mosaic virus (BSMV) as a model to investigate the essential role of its CRP in virus morphogenesis. The CRP protein γb directly interacts with BSMV coat protein (CP), the mutations either on the His-85 site in γb predicted to generate a potential CCCH motif or on the His-13 site in CP exposed to the surface of the virions abolish the zinc-binding activity and their interaction. Immunogold-labeling assays show that γb binds to the surface of rod-shaped BSMV virions in a Zn2+-dependent manner, which enhances the RNA binding activity of CP and facilitates virion assembly and stability, suggesting that the Zn2+-dependent physical association of γb with the virion is crucial for BSMV morphogenesis. Intriguingly, the tightly binding of diverse CRPs to their rod-shaped virions is a general feature employed by the members in the families Virgaviridae (excluding the genus Tobamovirus) and Benyviridae. Together, these results reveal a hitherto unknown role of CRPs in the assembly and stability of virus particles, and expand our understanding of the molecular mechanism underlying virus morphogenesis.

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The N-terminal region containing the zinc finger domain of tobacco streak virus coat protein is essential for the formation of virus-like particles

Cited by 4 publications

References 44 publications

Pan-retroviral Nucleocapsid-Mediated Phase Separation Regulates Genomic RNA Positioning and Trafficking

Pan-retroviral Nucleocapsid-Mediated Phase Separation Regulates Genomic RNA Positioning and Trafficking

Zinc and Copper Ions Differentially Regulate Prion-Like Phase Separation Dynamics of Pan-Virus Nucleocapsid Biomolecular Condensates

Zn2+-dependent association of cysteine-rich protein with virion orchestrates morphogenesis of rod-shaped viruses

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