Three-dimensional reconstruction of a recombinant influenza virus ribonucleoprotein particle.
A three-dimensional structural model of an influenza virus ribonucleoprotein particle reconstituted in vivo from recombinant proteins and a model genomic vRNA has been generated by electron microscopy. It shows a circular shape and contains nine nucleoprotein monomers, two of which are connected with the polymerase complex. The nucleoprotein monomers show a curvature that may be responsible for the formation of helical structures in the full-size viral ribonucleoproteins. The monomers show distinct contact boundaries at the two sides of the particle, suggesting that the genomic RNA may be located in association with the nucleoprotein at the base of the ribonucleoprotein complex. Sections of the three-dimensional model show a trilobular morphology in the polymerase complex that is consistent with the presence of its three subunits.
Martín-Benito
J
J
Centro Nacional de Biotecnología (CSIC), Campus de Cantoblanco, 28049 Madrid, Spain.
Area
E
E
Ortega
J
J
Llorca
O
O
Valpuesta
J M
JM
Carrascosa
J L
JL
Ortín
J
J
D007091:Image Processing, Computer-Assisted; D008854:Microscopy, Electron; D009975:Orthomyxoviridae / Q000737:chemistry*; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry; D012261:Ribonucleoproteins / Q000737:chemistry*
D011994:Recombinant Proteins; D012261:Ribonucleoproteins