Anatomy of Venezuelan Equine Encephalomyelitis Virus
FORT DETRICK FREDERICK MD
Pagination or Media Count:
Virions of Venezuelan equine encephalomyelitis virus purified by gradient centrifugation procedure were disrupted with Tween and ether and then centrifuged in equillibrium cesium chloride density gradient. Fine structures of the resulting fractions of hemagglutinin HA and ribonucleoprotein RNP were examined in the electron microscope. The HA had a shape of a hollow cylinder 55 - 60 A long and 45 - 50 A in diameter. RNP looked like a strand 15 - 17 A thick. It is assumed that RNP is packed within the virion in such a way that loops of the external part of the nucleoid interact with each other like capsomerss in the cubic type of symmetry thereby determining the quasi- icosahedral form of nucleoids. Information about the relatively fine structure of hemaglutinin HA and ribonucleoproteins RNP of the VEE virus and the architecture of virions is discussed.