Organization of turnip yellow mosaic virus investigated by neutron small angle scattering at 80 K: an intermediate state preceding decapsidation of the virion?
The organization of turnip yellow mosaic virus has been investigated by neutron small angle scattering at 300 K and 80 K in buffers containing various amounts of D2O. We confirm that in native virions, no substantial part of the RNA is located at a radius larger than ca. 100-110 A, i.e., that there is very little interpretation of the RNA into the capsid. At 80 K, scattering curves do not depend much upon contrast, from 40% D2O to 100% D2O buffers, but are strongly affected by interparticle interference. We could, however, show that it is not the case for the subsidiary intensity maximum at q approximately 0.06 A-1. From the position of this maximum, we conclude that upon freezing, the radius of the capsid expands by c.a. 3.5% and the RNA penetrates deeply into the protein shell. Biological implications of this conformational change immediately preceding decapsidation are discussed.
Witz
J
J
Département d'Immunochimie des Peptides et Virus, Institut de Biologie Moléculaire et Cellulaire du C.N.R.S., Strasbourg, France.
Timmins
P A
PA
Adrian
M
M
D002213:Capsid / Q000648:ultrastructure; D005615:Freezing; D009502:Neutrons; D012367:RNA, Viral / Q000648:ultrastructure; D012542:Scattering, Radiation; D017806:Tymovirus / Q000648:ultrastructure*; D014771:Virion / Q000648:ultrastructure*
D012367:RNA, Viral