Sequence specificity for uridylylation of the viral peptide linked to the genome (VPg) of enteroviruses

Catherine H. Schein; Mengyi Ye; Aniko V. Paul; M. Steven Oberste; Nora Chapman; Gerbrand J. van der Heden van Noort; Dmitri V. Filippov; Kyung Choi

doi:10.1016/j.virol.2015.05.016

Sequence specificity for uridylylation of the viral peptide linked to the genome (VPg) of enteroviruses

Catherine H. Schein, Mengyi Ye, Aniko V. Paul, M. Steven Oberste, Nora Chapman, Gerbrand J. van der Heden van Noort, Dmitri V. Filippov, Kyung Choi

Pathology & Microbiology

Research output: Contribution to journal › Article › peer-review

12 Scopus citations

Abstract

Enteroviruses (EV) uridylylate a peptide, VPg, as the first step in their replication. VPgpUpU, found free in infected cells, serves as the primer for RNA elongation. The abilities of four polymerases (3D^pol), from EV-species A-C, to uridylylate VPgs that varied by up to 60% of their residues were compared. Each 3D^pol was able to uridylylate all five VPgs using polyA RNA as template, while showing specificity for its own genome encoded peptide. All 3D^pol uridylylated a consensus VPg representing the physical chemical properties of 31 different VPgs. Thus the residues required for uridylylation and the enzymatic mechanism must be similar in diverse EV. As VPg-binding sites differ in co-crystal structures, the reaction is probably done by a second 3D^pol molecule. The conservation of polymerase residues whose mutation reduces uridylylation but not RNA elongation is compared.

Original language	English (US)
Pages (from-to)	80-85
Number of pages	6
Journal	Virology
Volume	484
DOIs	https://doi.org/10.1016/j.virol.2015.05.016
State	Published - Oct 1 2015

Keywords

Coxsackie virus
EV-71
Metal ion dependent phosphotransfer
Nucleotide transfer reaction
PCP-consensus sequence
Peptide priming
Poliovirus
RNA polymerase

ASJC Scopus subject areas

Virology

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10.1016/j.virol.2015.05.016

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@article{a6840e63bf304a1c83e1a499c68465cb,

title = "Sequence specificity for uridylylation of the viral peptide linked to the genome (VPg) of enteroviruses",

abstract = "Enteroviruses (EV) uridylylate a peptide, VPg, as the first step in their replication. VPgpUpU, found free in infected cells, serves as the primer for RNA elongation. The abilities of four polymerases (3Dpol), from EV-species A-C, to uridylylate VPgs that varied by up to 60% of their residues were compared. Each 3Dpol was able to uridylylate all five VPgs using polyA RNA as template, while showing specificity for its own genome encoded peptide. All 3Dpol uridylylated a consensus VPg representing the physical chemical properties of 31 different VPgs. Thus the residues required for uridylylation and the enzymatic mechanism must be similar in diverse EV. As VPg-binding sites differ in co-crystal structures, the reaction is probably done by a second 3Dpol molecule. The conservation of polymerase residues whose mutation reduces uridylylation but not RNA elongation is compared.",

keywords = "Coxsackie virus, EV-71, Metal ion dependent phosphotransfer, Nucleotide transfer reaction, PCP-consensus sequence, Peptide priming, Poliovirus, RNA polymerase",

author = "Schein, {Catherine H.} and Mengyi Ye and Paul, {Aniko V.} and Oberste, {M. Steven} and Nora Chapman and {van der Heden van Noort}, {Gerbrand J.} and Filippov, {Dmitri V.} and Kyung Choi",

note = "Funding Information: Special appreciation and thanks are due to Kaija Maher, CDC, for obtaining the genes for CVA24 and EV-A71 3D pol and staff at FfAME, particularly Ryan Shaw, Lucy Glushacova, Ozlem Yaren, Jennifer Moses, Nicole Leal, Nidhi Sharma, Andrea Bradley and Dianne Rowold for help in establishing the assay methods and Steve Benner for helpful discussions. This work was supported by grants from the NIH to CHS ( 1R21AI105985 ), and in part by grant RO1AI0152235 (PI: Eckard Wimmer). Synthesis of VPgs and VPg-pUs was supported by a VIDI grand from the Netherlands Organisation for Scientific Research (NWO) . Publisher Copyright: {\textcopyright} 2015 Elsevier Inc.",

year = "2015",

month = oct,

day = "1",

doi = "10.1016/j.virol.2015.05.016",

language = "English (US)",

volume = "484",

pages = "80--85",

journal = "Virology",

issn = "0042-6822",

publisher = "Academic Press Inc.",

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TY - JOUR

T1 - Sequence specificity for uridylylation of the viral peptide linked to the genome (VPg) of enteroviruses

AU - Schein, Catherine H.

AU - Ye, Mengyi

AU - Paul, Aniko V.

AU - Oberste, M. Steven

AU - Chapman, Nora

AU - van der Heden van Noort, Gerbrand J.

AU - Filippov, Dmitri V.

AU - Choi, Kyung

N1 - Funding Information: Special appreciation and thanks are due to Kaija Maher, CDC, for obtaining the genes for CVA24 and EV-A71 3D pol and staff at FfAME, particularly Ryan Shaw, Lucy Glushacova, Ozlem Yaren, Jennifer Moses, Nicole Leal, Nidhi Sharma, Andrea Bradley and Dianne Rowold for help in establishing the assay methods and Steve Benner for helpful discussions. This work was supported by grants from the NIH to CHS ( 1R21AI105985 ), and in part by grant RO1AI0152235 (PI: Eckard Wimmer). Synthesis of VPgs and VPg-pUs was supported by a VIDI grand from the Netherlands Organisation for Scientific Research (NWO) . Publisher Copyright: © 2015 Elsevier Inc.

PY - 2015/10/1

Y1 - 2015/10/1

N2 - Enteroviruses (EV) uridylylate a peptide, VPg, as the first step in their replication. VPgpUpU, found free in infected cells, serves as the primer for RNA elongation. The abilities of four polymerases (3Dpol), from EV-species A-C, to uridylylate VPgs that varied by up to 60% of their residues were compared. Each 3Dpol was able to uridylylate all five VPgs using polyA RNA as template, while showing specificity for its own genome encoded peptide. All 3Dpol uridylylated a consensus VPg representing the physical chemical properties of 31 different VPgs. Thus the residues required for uridylylation and the enzymatic mechanism must be similar in diverse EV. As VPg-binding sites differ in co-crystal structures, the reaction is probably done by a second 3Dpol molecule. The conservation of polymerase residues whose mutation reduces uridylylation but not RNA elongation is compared.

AB - Enteroviruses (EV) uridylylate a peptide, VPg, as the first step in their replication. VPgpUpU, found free in infected cells, serves as the primer for RNA elongation. The abilities of four polymerases (3Dpol), from EV-species A-C, to uridylylate VPgs that varied by up to 60% of their residues were compared. Each 3Dpol was able to uridylylate all five VPgs using polyA RNA as template, while showing specificity for its own genome encoded peptide. All 3Dpol uridylylated a consensus VPg representing the physical chemical properties of 31 different VPgs. Thus the residues required for uridylylation and the enzymatic mechanism must be similar in diverse EV. As VPg-binding sites differ in co-crystal structures, the reaction is probably done by a second 3Dpol molecule. The conservation of polymerase residues whose mutation reduces uridylylation but not RNA elongation is compared.

KW - Coxsackie virus

KW - EV-71

KW - Metal ion dependent phosphotransfer

KW - Nucleotide transfer reaction

KW - PCP-consensus sequence

KW - Peptide priming

KW - Poliovirus

KW - RNA polymerase

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DO - 10.1016/j.virol.2015.05.016

M3 - Article

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SN - 0042-6822

VL - 484

SP - 80

EP - 85

JO - Virology

JF - Virology

ER -

Sequence specificity for uridylylation of the viral peptide linked to the genome (VPg) of enteroviruses

Abstract

Keywords

ASJC Scopus subject areas

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