Nucleic Acids Research, Vol 25, Issue 21 4271-4277, Copyright © 1997 by Oxford University Press
RM Marion, T Aragon, A Beloso, A Nieto and J Ortin
A collection of C-terminal deletion mutants of the influenza A virus NS1
gene has been used to define the regions of the NS1 protein involved in its
functionality. Immunofluorescence analyses showed that the NS1 protein
sequences downstream from position 81 are not required for nuclear
transport. The capacity of these mutants to bind RNA was studied by in
vitro binding tests using a model vRNA probe. These experiments showed that
the N-terminal 81 amino acids of NS1 protein are sufficient for RNA binding
activity. The collection of mutants also served to map the NS1 sequences
required for nuclear retention of mRNA and for stimulation of viral mRNA
translation, using the NP gene as reporter. The results obtained indicated
that the N-terminal 113 amino acids of NS1 protein are sufficient for
nuclear retention of mRNA and stimulation of viral mRNA translation. The
possibility that this region of the protein may be sufficient for virus
viability is discussed in relation to the sequences of NS1 genes of field
isolates and to the phenotype of known viral mutants affected in the NS1
gene.
ARTICLES
The N-terminal half of the influenza virus NS1 protein is sufficient for nuclear retention of mRNA and enhancement of viral mRNA translation
Centro Nacional de Biotecnologia (CSIC), Cantoblanco, 28049 Madrid, Spain.
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