| Journal of General Virology |
| First posted online 12 December 2001 | REVIEW ARTICLE |
| DOI: 10.1099/vir.0.18133-0 |
Agustín Portela1 and Paul Digard2
1 División de Productos
Biológicos y Biotecnología, Agencia Española del
Medicamento, Majadahonda 28220, Madrid, Spain
2 Division of Virology, Department of Pathology, University of
Cambridge, Tennis Court Road, Cambridge CB2 1QP, UK
All viruses with negative-sense RNA genomes encode a single-strand RNA-binding nucleoprotein (NP). The primary function of NP is to encapsidate the virus genome for the purposes of RNA transcription, replication and packaging. The purpose of this review is to illustrate using the influenza virus NP as a well-studied example that the molecule is much more than a structural RNA-binding protein, but also functions as a key adapter molecule between virus and host cell processes. It does so through the ability to interact with a wide variety of viral and cellular macromolecules, including RNA, itself, two subunits of the viral RNA-dependent RNA polymerase and the viral matrix protein. NP also interacts with cellular polypeptides, including actin, components of the nuclear import and export apparatus and a nuclear RNA helicase. The evidence for the existence of each of these activities and their possible roles in transcription, replication and intracellular trafficking of the virus genome is considered.
© 2002 SGM
This article is now available in the April 2002 print issue of JGV (vol. 83, 723734). The complete issue of the journal may be seen in electronic form on JGV Online.