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Journal of Virology, February 2003, p. 1757-1763, Vol. 77, No. 3
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.3.1757-1763.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Rotavirus Nonstructural Protein NSP5 Interacts with Major Core Protein VP2

Mabel Berois,1,2* Catherine Sapin,3 Inge Erk,2 Didier Poncet,2 and Jean Cohen2

Seccion Virologia, Facultad de Ciencias, Montevideo 11400, Uruguay,1 UMR CNRS-INRA Virologie Moléculaire et Structurale, 91198 Gif-sur-Yvette Cedex,2 INSERM U 538, Université Pierre et Marie Curie, 75012 Paris, France3

Received 18 July 2002/ Accepted 28 October 2002

Rotavirus is a nonenveloped virus with a three-layered capsid. The inner layer, made of VP2, encloses the genomic RNA and two minor proteins, VP1 and VP3, with which it forms the viral core. Core assembly is coupled with RNA viral replication and takes place in definite cellular structures termed viroplasms. Replication and encapsidation mechanisms are still not fully understood, and little information is available about the intermolecular interactions that may exist among the viroplasmic proteins. NSP2 and NSP5 are two nonstructural viroplasmic proteins that have been shown to interact with each other. They have also been found to be associated with precore replication intermediates that are precursors of the viral core. In this study, we show that NSP5 interacts with VP2 in infected cells. This interaction was demonstrated with recombinant proteins expressed from baculovirus recombinants or in bacterial systems. NSP5-VP2 interaction also affects the stability of VP6 bound to VP2 assemblies. The data presented showed evidence, for the first time, of an interaction between VP2 and a nonstructural rotavirus protein. Published data and the interaction demonstrated here suggest a possible role for NSP5 as an adapter between NSP2 and the replication complex VP2-VP1-VP3 in core assembly and RNA encapsidation, modulating the role of NSP2 as a molecular motor involved in the packaging of viral mRNA.

* Corresponding author. Mailing address: UMR CNRS-INRA Virologie Moléculaire et Structurale, Domaine de Vilvert, 78352 Jouy en Josas, France. Phone: 33-0-1-34-65-26-11. Fax: 33-0-1-34-65-26-21. E-mail: berois{at}jouy.inra.fr.

Journal of Virology, February 2003, p. 1757-1763, Vol. 77, No. 3
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.3.1757-1763.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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