Role of RNA structure and RNA binding activity of foot-and-mouth disease virus 3C protein in VPg uridylylation and virus replication

Research output: Contribution to journal › Journal article › Research › peer-review

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Role of RNA structure and RNA binding activity of foot-and-mouth disease virus 3C protein in VPg uridylylation and virus replication. / Nayak, Arabinda; Goodfellow, Ian G; Woolaway, Kathryn E; Birtley, James; Curry, Stephen; Belsham, Graham J.

In: Journal of Virology, Vol. 80, No. 19, 10.2006, p. 9865-75.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Nayak, A, Goodfellow, IG, Woolaway, KE, Birtley, J, Curry, S & Belsham, GJ 2006, 'Role of RNA structure and RNA binding activity of foot-and-mouth disease virus 3C protein in VPg uridylylation and virus replication', Journal of Virology, vol. 80, no. 19, pp. 9865-75. https://doi.org/10.1128/JVI.00561-06

APA

Nayak, A., Goodfellow, I. G., Woolaway, K. E., Birtley, J., Curry, S., & Belsham, G. J. (2006). Role of RNA structure and RNA binding activity of foot-and-mouth disease virus 3C protein in VPg uridylylation and virus replication. Journal of Virology, 80(19), 9865-75. https://doi.org/10.1128/JVI.00561-06

Vancouver

Nayak A, Goodfellow IG, Woolaway KE, Birtley J, Curry S, Belsham GJ. Role of RNA structure and RNA binding activity of foot-and-mouth disease virus 3C protein in VPg uridylylation and virus replication. Journal of Virology. 2006 Oct;80(19):9865-75. https://doi.org/10.1128/JVI.00561-06

Author

Nayak, Arabinda ; Goodfellow, Ian G ; Woolaway, Kathryn E ; Birtley, James ; Curry, Stephen ; Belsham, Graham J. / Role of RNA structure and RNA binding activity of foot-and-mouth disease virus 3C protein in VPg uridylylation and virus replication. In: Journal of Virology. 2006 ; Vol. 80, No. 19. pp. 9865-75.

Bibtex

@article{9e0bcff2398f43e4b08da8036d96db36,
title = "Role of RNA structure and RNA binding activity of foot-and-mouth disease virus 3C protein in VPg uridylylation and virus replication",
abstract = "The uridylylation of the VPg peptide primer is the first stage in the replication of picornavirus RNA. This process can be achieved in vitro using purified components, including 3B (VPg) with the RNA dependent RNA polymerase (3Dpol), the precursor 3CD, and an RNA template containing the cre/bus. We show that certain RNA sequences within the foot-and-mouth disease virus (FMDV) 5' untranslated region but outside of the cre/bus can enhance VPg uridylylation activity. Furthermore, we have shown that the FMDV 3C protein alone can substitute for 3CD, albeit less efficiently. In addition, the VPg precursors, 3B(3)3C and 3B(123)3C, can function as substrates for uridylylation in the absence of added 3C or 3CD. Residues within the FMDV 3C protein involved in interaction with the cre/bus RNA have been identified and are located on the face of the protein opposite from the catalytic site. These residues within 3C are also essential for VPg uridylylation activity and efficient virus replication.",
keywords = "Amino Acid Sequence, Animals, Base Sequence, Binding Sites, Cell Line, Conserved Sequence, Cricetinae, Foot-and-Mouth Disease Virus/classification, Models, Molecular, Molecular Sequence Data, Nucleic Acid Conformation, Protein Binding, Protein Precursors/metabolism, Protein Processing, Post-Translational, Protein Structure, Tertiary, RNA, Viral/chemistry, RNA-Binding Proteins/chemistry, Sequence Alignment, Uridine/metabolism, Viral Proteins/chemistry, Virus Replication",
author = "Arabinda Nayak and Goodfellow, {Ian G} and Woolaway, {Kathryn E} and James Birtley and Stephen Curry and Belsham, {Graham J}",
year = "2006",
month = oct,
doi = "10.1128/JVI.00561-06",
language = "English",
volume = "80",
pages = "9865--75",
journal = "Journal of Virology",
issn = "0022-538X",
publisher = "American Society for Microbiology",
number = "19",

}

RIS

TY - JOUR

T1 - Role of RNA structure and RNA binding activity of foot-and-mouth disease virus 3C protein in VPg uridylylation and virus replication

AU - Nayak, Arabinda

AU - Goodfellow, Ian G

AU - Woolaway, Kathryn E

AU - Birtley, James

AU - Curry, Stephen

AU - Belsham, Graham J

PY - 2006/10

Y1 - 2006/10

N2 - The uridylylation of the VPg peptide primer is the first stage in the replication of picornavirus RNA. This process can be achieved in vitro using purified components, including 3B (VPg) with the RNA dependent RNA polymerase (3Dpol), the precursor 3CD, and an RNA template containing the cre/bus. We show that certain RNA sequences within the foot-and-mouth disease virus (FMDV) 5' untranslated region but outside of the cre/bus can enhance VPg uridylylation activity. Furthermore, we have shown that the FMDV 3C protein alone can substitute for 3CD, albeit less efficiently. In addition, the VPg precursors, 3B(3)3C and 3B(123)3C, can function as substrates for uridylylation in the absence of added 3C or 3CD. Residues within the FMDV 3C protein involved in interaction with the cre/bus RNA have been identified and are located on the face of the protein opposite from the catalytic site. These residues within 3C are also essential for VPg uridylylation activity and efficient virus replication.

AB - The uridylylation of the VPg peptide primer is the first stage in the replication of picornavirus RNA. This process can be achieved in vitro using purified components, including 3B (VPg) with the RNA dependent RNA polymerase (3Dpol), the precursor 3CD, and an RNA template containing the cre/bus. We show that certain RNA sequences within the foot-and-mouth disease virus (FMDV) 5' untranslated region but outside of the cre/bus can enhance VPg uridylylation activity. Furthermore, we have shown that the FMDV 3C protein alone can substitute for 3CD, albeit less efficiently. In addition, the VPg precursors, 3B(3)3C and 3B(123)3C, can function as substrates for uridylylation in the absence of added 3C or 3CD. Residues within the FMDV 3C protein involved in interaction with the cre/bus RNA have been identified and are located on the face of the protein opposite from the catalytic site. These residues within 3C are also essential for VPg uridylylation activity and efficient virus replication.

KW - Amino Acid Sequence

KW - Animals

KW - Base Sequence

KW - Binding Sites

KW - Cell Line

KW - Conserved Sequence

KW - Cricetinae

KW - Foot-and-Mouth Disease Virus/classification

KW - Models, Molecular

KW - Molecular Sequence Data

KW - Nucleic Acid Conformation

KW - Protein Binding

KW - Protein Precursors/metabolism

KW - Protein Processing, Post-Translational

KW - Protein Structure, Tertiary

KW - RNA, Viral/chemistry

KW - RNA-Binding Proteins/chemistry

KW - Sequence Alignment

KW - Uridine/metabolism

KW - Viral Proteins/chemistry

KW - Virus Replication

U2 - 10.1128/JVI.00561-06

DO - 10.1128/JVI.00561-06

M3 - Journal article

C2 - 16973591

VL - 80

SP - 9865

EP - 9875

JO - Journal of Virology

JF - Journal of Virology

SN - 0022-538X

IS - 19

ER -

ID: 257918918