Incorporation of lipid precursors into cytoplasmic membranes of poliovirus-infected HeLa cells.
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Biomedical subjects
Publications and source records attributed to L A Caliguiri.
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Helical nucleocapsids of each of the paramyxoviruses simian virus 5 (SV5), Newcastle disease virus (NDV), and Sendai virus have been isolated in two different forms. One form contains larger protein subunits and is obtained from mature virions or infected cells dispersed by ethylenediaminetetraacetic acid. The other form possesses smaller subunits and is obtained from infected cells dispersed by trypsin. The estimated molecular weights of the larger subunits in the three viruses are similar: SV5, 61,000; Sendai virus, 60,000; NDV, 56,000. The smaller nucleocapsid subunits are also very similar: SV5, 43,000; Sendai virus, 46,000; NDV, 47,000. The helical nucleocapsid composed of the smaller subunit appears to be less flexible and more stable than that formed by the larger subunit. There is suggestive evidence that conversion of the larger subunit to the smaller by proteolytic cleavage may occur intracellularly. The possibility that such a mechanism could be involved in the accumulation of nucleocapsid in cells persistently infected with paramyxoviruses is discussed.
Poliovirus RNA and proteins are synthesized in association with distinct membranous structures that were separated by means of Isopycnic centrifugation of cytoplasmic extracts in discontinuous sucrose-density gradients. Viral RNA is replicated in a structure that contains rapidly labeled replicative intermediate RNA and viral RNA polymerase associated with the smooth membrane fraction. In sucrose gradients this viral RNA replication complex is distributed at densities in the range of 1.12 to 1.18 grams per cubic centimeter. Viral proteins are synthesized on polyribosomes bound to membranes and sediment with polyribosomes at densities of less than 1.25 grams per cubic centimeter.
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