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J Virol, June 1998, p. 5307-5312, Vol. 72, No. 6
School of Animal and Microbial Sciences,
University of Reading, Reading RG6 6AJ, United Kingdom
Received 16 December 1997/Accepted 17 March 1998
The nucleoprotein (NP) of influenza B virus is 50 amino acids
longer at the N-terminus than influenza A virus NP and lacks homology
to the A virus protein over the first 69 residues. We have deleted the
N-terminal 51 and 69 residues of the influenza B/Ann Arbor/1/66 virus
NP and show that nuclear accumulation of the protein is unaffected.
This indicates that the nuclear localization signal is not located at
the extreme N terminus, as in influenza A virus NP. To determine if the
N-terminal mutants could support the expression and replication of a
model influenza B virus RNA, the genes encoding the subunits of the
viral RNA-dependent RNA polymerase (PA, PB1, and PB2) were cloned.
Coexpression of NP and the P proteins in 293 cells was found to permit
the expression and replication of a transfected model RNA based on
segment 4 of B/Maryland/59, in which the hemagglutinin-coding region
was replaced by a chloramphenicol acetyltransferase gene. The
expression and replication of the synthetic RNA were not affected by
the replacement of NP with NP mutants lacking the N-terminal 51 or 69 residues, indicating that the N-terminal extension is not required for
transcription or replication of the viral RNA. In addition, we report
that the influenza B virus NP cannot be functionally replaced by type A
virus NP in this system.
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
The N-Terminal Extension of the Influenza B Virus
Nucleoprotein Is Not Required for Nuclear Accumulation or the
Expression and Replication of a Model RNA
*
Corresponding author. Mailing address: School of Animal
and Microbial Sciences, University of Reading, Reading RG6 6AJ, United Kingdom. Phone: 44 (1189) 316368. Fax: 44 (1189) 316671. E-mail: w.s.barclay{at}reading.ac.uk.
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