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Journal of Virology, January 2000, p. 156-163, Vol. 74, No. 1
Centro Nacional de Biotecnología
(CSIC), Campus de Cantoblanco, 28049 Madrid, Spain
Received 15 July 1999/Accepted 17 September 1999
Influenza virus ribonucleoproteins (RNPs) were reconstituted in
vivo from cloned cDNAs expressing the three polymerase subunits, the
nucleoprotein (NP), and short template RNAs. The structure of purified
RNPs was studied by electron microscopy and image processing. Circular
and elliptic structures were obtained in which the NP and the
polymerase complex could be defined. Comparison of the structure of
RNPs of various lengths indicated that each NP monomer interacts with
approximately 24 nucleotides. The analysis of the amplification of RNPs
with different lengths showed that those with the highest replication
efficiency contained an even number of NP monomers, suggesting that the
NP is incorporated as dimers into newly synthesized RNPs.
0022-538X/0/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Ultrastructural and Functional Analyses of
Recombinant Influenza Virus Ribonucleoproteins Suggest Dimerization of
Nucleoprotein during Virus Amplification
*
Corresponding author. Mailing address: Centro Nacional
de Biotecnologia, Campus de Cantoblanco, 28049 Madrid, Spain. Phone: 34-91-585-4557. Fax: 34-91-585-4506. E-mail:
jortin{at}cnb.uam.es.
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