Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/15449
Share/Export:
logo share SHARE BASE
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE
Title

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

AuthorsOrtega, Joaquín; Martín-Benito, Jaime; Zürcher, Thomas; Valpuesta, José M. CSIC ORCID ; Carrascosa, José L.; Ortín, Juan
Issue DateJan-2000
PublisherAmerican Society for Microbiology
CitationJournal of Virology 74(1): 156-163 (2000)
AbstractInfluenza 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.
Description8 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
Publisher version (URL)http://jvi.asm.org/cgi/content/abstract/74/1/156?ck=nck
URIhttp://hdl.handle.net/10261/15449
ISSN0022-538X
E-ISSN1098-5514
Appears in Collections:(CNB) Artículos

Show full item record
Review this work

PubMed Central
Citations

55
checked on May 7, 2022

SCOPUSTM   
Citations

101
checked on May 12, 2022

WEB OF SCIENCETM
Citations

100
checked on May 13, 2022

Page view(s)

310
checked on May 15, 2022

Google ScholarTM

Check

Dimensions



WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.