Radioiodination of the envelope proteins of Newcastle disease virus.
Lactoperoxidase-catalyzed iodination selectively labels the two glycoproteins (VP1 and VP2) of Newcastle disease virus. The low-molecular-weight, nonglycosylated major viral protein, VP6, was not iodinated in the intact virus but was iodinated in disrupted virions, suggesting a localization on the inner, rather than the outer, envelope surface. Studies on the distribution of virion proteins labeled with 125-I and 3-H-isoleucine between detergent-soluble and detergent-insoluble fractions show that the virion proteins VP4, VP5, and VP6 are solubilized to a much lesser extent than are VP1 and VP2.
D000818:Animals; D002499:Centrifugation, Density Gradient; D055598:Chemical Phenomena; D002621:Chemistry; D002642:Chick Embryo; D004591:Electrophoresis, Polyacrylamide Gel; D006023:Glycoproteins; D007457:Iodine Radioisotopes; D007784:Lactoperoxidase; D009522:Newcastle disease virus / Q000254:growth & development / Q000648:ultrastructure; D012967:Sodium Dodecyl Sulfate; D012995:Solubility; D014764:Viral Proteins / Q000302:isolation & purification; D014779:Virus Replication
D006023:Glycoproteins; D007457:Iodine Radioisotopes; D014764:Viral Proteins; D012967:Sodium Dodecyl Sulfate; D007784:Lactoperoxidase