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Ultrastructural and functional analyses of recombinant influenza virus ribonucleoproteins suggest dimerization of nucleoprotein during virus amplification

AutorOrtega, Joaquín; Martín-Benito, Jaime; Zürcher, Thomas; Valpuesta, José M.; Carrascosa, José L.; Ortín, Juan
Fecha de publicaciónene-2000
EditorAmerican Society for Microbiology
CitaciónJournal of Virology 74(1): 156-163 (2000)
ResumenInfluenza 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.
Descripción8 pages, 7 figures.-- PMID: 10590102 [PubMed].-- PMCID: PMC111524.
Full-text version available Open Access at PebMed Central: http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=10590102
Versión del editorhttp://jvi.asm.org/cgi/content/abstract/74/1/156?ck=nck
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