Radioiodination of the envelope proteins of Newcastle disease virus

J Supramol Struct. 1975;3(1):51-60. doi: 10.1002/jss.400030106.

Abstract

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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Centrifugation, Density Gradient
  • Chemical Phenomena
  • Chemistry
  • Chick Embryo
  • Electrophoresis, Polyacrylamide Gel
  • Glycoproteins
  • Iodine Radioisotopes
  • Lactoperoxidase
  • Newcastle disease virus* / growth & development
  • Newcastle disease virus* / ultrastructure
  • Sodium Dodecyl Sulfate
  • Solubility
  • Viral Proteins* / isolation & purification
  • Virus Replication

Substances

  • Glycoproteins
  • Iodine Radioisotopes
  • Viral Proteins
  • Sodium Dodecyl Sulfate
  • Lactoperoxidase