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Conformational flexibility in measles virus nucleocapsids visualized.
2004 SEP 1 - (NewsRx.com & NewsRx.net) -- Scientists have visualized conformational flexibility in recombinant measles virus nucleocapsids by cryo-negative stain electron microscopy and real-space helical reconstruction.
"Measles virus is a highly contagious virus that, despite the existence of an effective vaccine, is a major cause of illness and mortality worldwide. The virus has a negative-sense, single-stranded RNA genome that is encapsidated by the nucleocapsid protein (N) to form a helical ribonucleoprotein complex known as the nucleocapsid. This structure serves as the template for both transcription and replication. Paramyxovirus nucleocapsids are flexible structures, a trait that has hitherto hampered structural analysis even at low resolution," scientists in Scotland report.
"We have investigated the extent of this structural plasticity, using real-space methods to calculate three-dimensional reconstructions of recombinant nucleocapsids from cryo-negative stain transmission electron micrographs," said David Bhella and colleagues at the Medical Research Council Virology Unit in Glasgow. "Images of short sections of helix were sorted according to both pitch (the axial rise per turn) and twist (the number of subunits per turn). Our analysis indicates that there is extensive conformational flexibility within these structures, ranging in pitch from 50 to 66 angstroms, while twist varies from at least 13.04 to 13.44 with a greater number of helices comprising around 13.1 subunits per turn."
"We have also investigated the influence of the C terminus of N on helix conformation, ...
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