Structure and Double-Stranded RNA-Binding Activity of the Birnavirus Drosophila X Virus VP3 Protein-Reference-Cited by-同舟云学术

Structure and Double-Stranded RNA-Binding Activity of the Birnavirus Drosophila X Virus VP3 Protein

Published:2021-01-28 Issue:4 Volume:95 Page:
ISSN:0022-538X
Container-title:Journal of Virology
language:en
Short-container-title:J Virol

Author:

Ferrero Diego S.¹²^ORCID,Busnadiego Idoia²^ORCID,Garriga Damià¹³^ORCID,Guerra Pablo¹,Martín María Teresa²,Kremer Leonor²^ORCID,Usón Isabel¹⁴,Rodriguez José Francisco²^ORCID,Verdaguer Nuria¹^ORCID

Affiliation:

1. Structural Biology Unit, Institut de Biologia Molecular de Barcelona, CSIC, Barcelona, Spain

2. Centro Nacional de Biotecnología, CSIC, Madrid, Spain

3. ALBA Synchrotron Light Source, Cerdanyola del Vallès, Spain

4. Institucio Catalana de Recerca i Estudis Avançats, Barcelona, Spain

Abstract

The birnavirus moonlighting protein VP3 plays crucial roles in interacting with the dsRNA genome segments to form stable ribonucleoprotein complexes and controlling host cell immune responses, presumably by binding to and shielding the dsRNA from recognition by the host silencing machinery. The structural, biophysical, and functional data presented in this work identified the N-terminal domain of VP3 as being responsible for the dsRNA-binding and silencing suppression activities of the protein in drosophila X virus.

Funder

Spanish Ministry of Science and Innovation

Publisher

American Society for Microbiology

Subject

Virology,Insect Science,Immunology,Microbiology

Link

https://journals.asm.org/doi/pdf/10.1128/JVI.02166-20

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