The red clover necrotic mosaic virus capsid protein N-terminal amino acids possess specific RNA binding activity and are required for stable virion assembly

The 17-kDa capsid protein (CP) of satellite panicum mosaic virus (SPMV) contains a distinct N-terminal arginine-rich motif (N-ARM) which is required for SPMV virion assembly and the activity of SPMV CP to promote systemic accumulation of its cognate RNA. The present study indicates that SPMV CP also is involved in SPMV RNA accumulation in inoculated leaves and that this activity is also dependent on a functional N-ARM. In addition, deletions of a C-terminal region abolish virion assembly and impair SPMV RNA accumulation in both inoculated and systemic leaves. Unlike the N-ARM mutations, substantial deletions of the SPMV CP C-terminus do not affect SPMV RNA binding activity. Interestingly, SPMV CP also binds Panicum mosaic virus genomic RNA via N-ARM-mediated CP:RNA interactions. Mutations of the N-ARM and the C-terminal regions significantly reduce SPMV CP titers and result in symptom attenuation. In contrast, virions were not associated per se with symptom exacerbation or successful SPMV RNA accumulation. The results show the existence of a correlation between N- and C-termini-mediated contributions for CP accumulation, symptom induction, defective-interfering RNA accumulation, and temperature sensitivity of SPMV RNA maintenance. The data provide further evidence that SPMV CP has multiple roles during infection, which might involve the formation of nonvirion CP:RNA complexes whose stability is controlled in a biologically relevant manner by the N- and C-termini of the CP.

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C-Terminal Amino Acids 471-507 of Avian Hepatitis E Virus Capsid Protein Are Crucial for Binding to Avian and Human Cells

PLoS ONE ◽

10.1371/journal.pone.0153723 ◽

2016 ◽

Vol 11 (4) ◽

pp. e0153723 ◽

Cited By ~ 4

Author(s):

Xinquan Zhang ◽

Ivana Bilic ◽

Ana Marek ◽

Martin Glösmann ◽

Michael Hess

Keyword(s):

Amino Acids ◽

Capsid Protein ◽

Hepatitis E Virus ◽

Hepatitis E ◽

Human Cells ◽

Virus Capsid ◽

Terminal Amino ◽

Avian Hepatitis E Virus ◽

Virus Capsid Protein

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Identification of amino acids in auxiliary replicase protein p27 critical for its RNA-binding activity and the assembly of the replicase complex in Red clover necrotic mosaic virus

Virology ◽

10.1016/j.virol.2011.02.017 ◽

2011 ◽

Vol 413 (2) ◽

pp. 300-309 ◽

Cited By ~ 19

Author(s):

Kiwamu Hyodo ◽

Akira Mine ◽

Hiro-oki Iwakawa ◽

Masanori Kaido ◽

Kazuyuki Mise ◽

...

Keyword(s):

Amino Acids ◽

Mosaic Virus ◽

Rna Binding ◽

Red Clover ◽

Binding Activity ◽

Replicase Protein ◽

Replicase Complex

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The Red clover necrotic mosaic virus capsid protein N-terminal lysine-rich motif is a determinant of symptomatology and virion accumulation

Molecular Plant Pathology ◽

10.1111/j.1364-3703.2011.00784.x ◽

2012 ◽

Vol 13 (7) ◽

pp. 744-754 ◽

Cited By ~ 10

Author(s):

SANG-HO PARK ◽

TIM L. SIT ◽

KOOK-HYUNG KIM ◽

STEVEN A. LOMMEL

Keyword(s):

Mosaic Virus ◽

Capsid Protein ◽

Red Clover ◽

Virus Capsid ◽

Virus Capsid Protein

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Analyses of Phosphorylation Events in the Rubella Virus Capsid Protein: Role in Early Replication Events

Journal of Virology ◽

10.1128/jvi.01152-05 ◽

2006 ◽

Vol 80 (14) ◽

pp. 6917-6925 ◽

Cited By ~ 15

Author(s):

LokMan J. Law ◽

Carolina S. Ilkow ◽

Wen-Pin Tzeng ◽

Matthew Rawluk ◽

David T. Stuart ◽

...

Keyword(s):

Capsid Protein ◽

Rubella Virus ◽

Rna Binding ◽

Virus Assembly ◽

Binding Activity ◽

Amino Acid Residues ◽

Direct Role ◽

Virus Capsid ◽

Early Replication ◽

Virus Capsid Protein

ABSTRACT The Rubella virus capsid protein is phosphorylated prior to virus assembly. Our previous data are consistent with a model in which dynamic phosphorylation of the capsid regulates its RNA binding activity and, in turn, nucleocapsid assembly. In the present study, the process of capsid phosphorylation was examined in further detail. We show that phosphorylation of serine 46 in the RNA binding region of the capsid is required to trigger phosphorylation of additional amino acid residues that include threonine 47. This residue likely plays a direct role in regulating the binding of genomic RNA to the capsid. We also provide evidence which suggests that the capsid is dephosphorylated prior to or during virus budding. Finally, whereas the phosphorylation state of the capsid does not directly influence the rate of synthesis of viral RNA and proteins or the assembly and secretion of virions, the presence of phosphate on the capsid is critical for early events in virus replication, most likely the uncoating of virions and/or disassembly of nucleocapsids.

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