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The RNA-dependent RNA polymerase of the infectious pancreatic necrosis virus is linked to viral mRNA acting as a cap substitute.
González-Catrilelbún, Sebastián; Cartagena, Julio; Vargas, Deborah; Breguel-Serrano, Pamela; Sandino, Ana María; Rivas-Aravena, Andrea.
Afiliação
  • González-Catrilelbún S; Laboratorio de Virología, Facultad de Medicina y Ciencia, Universidad San Sebastián, Santiago, Chile.
  • Cartagena J; Laboratorio de Virología, Centro de Biotecnología Acuícola, Universidad de Santiago de Chile, Santiago, Chile.
  • Vargas D; Laboratorio de Virología, Centro de Biotecnología Acuícola, Universidad de Santiago de Chile, Santiago, Chile.
  • Breguel-Serrano P; Laboratorio de Virología, Facultad de Medicina y Ciencia, Universidad San Sebastián, Santiago, Chile.
  • Sandino AM; Laboratorio de Virología, Centro de Biotecnología Acuícola, Universidad de Santiago de Chile, Santiago, Chile.
  • Rivas-Aravena A; Laboratorio de Virología, Facultad de Medicina y Ciencia, Universidad San Sebastián, Santiago, Chile.
J Gen Virol ; 103(3)2022 03.
Article em En | MEDLINE | ID: mdl-35349401
The infectious pancreatic necrosis virus (IPNV) is responsible for significant economic losses in the aquaculture industry. It is an unenveloped virus with an icosahedral capsid. Its viral genome comprises two dsRNA segments, A and B. Segment A contains a small ORF, which encodes VP5, and a large ORF, which encodes a polyprotein that generates the structural proteins and the viral protease. Segment B encodes the RNA-dependent RNA polymerase (RdRp), called VP1 in this free form, or Vpg when it covalently attaches to the viral RNA. The viral genome does not have cap or poly(A). Instead, each 5' end is linked to the Vpg. Recently, we demonstrated that mRNA-A contains an internal ribosome entry site (IRES) to command polyprotein synthesis. However, the presence of Vpg on IPNV mRNAs and its impact on cellular translation has not been investigated. This research demonstrates that IPNV mRNAs are linked to Vpg and that this protein inhibits cap-dependent translation on infected cells. Also, it is demonstrated that Vpg interacts with eIF4E and that rapamycin treatment partially diminishes the viral protein synthesis. In addition, we determined that an IRES does not command translation of IPNV mRNA-B. We show that VPg serves as a cap substitute during the initiation of IPNV translation, contributing to understanding the replicative cycle of Birnaviruses. Our results indicate that the viral protein VP1/Vpg is multifunctional, having a significant role during IPNV RNA synthesis as the RdRp and the primer for IPNV RNA synthesis and translation as the viral protein genome, acting as a cap substitute.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Vírus da Necrose Pancreática Infecciosa Idioma: En Revista: J Gen Virol Ano de publicação: 2022 Tipo de documento: Article País de afiliação: Chile País de publicação: Reino Unido

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Vírus da Necrose Pancreática Infecciosa Idioma: En Revista: J Gen Virol Ano de publicação: 2022 Tipo de documento: Article País de afiliação: Chile País de publicação: Reino Unido