Isolation and characterization of mouse FM3A cell mutants which are devoid of Newcastle disease virus receptors

J Virol. 1989 Jan;63(1):182-8. doi: 10.1128/JVI.63.1.182-188.1989.


A method was developed to select host cell mutants which did not permit the replication of Newcastle disease virus (NDV), and 14 isolates of NDV-nonpermissive mutants of mouse FM3A cells were obtained. All these isolates were judged to be deficient in NDV receptors, since their ability to adsorb 3H-labeled NDV virions was markedly decreased. They were tested for genetic complementation in pairs by cell fusion and shown to fall into a single recessive complementation group, which was designated as Had-1. Vesicular stomatitis virus was able to replicate in this mutant to produce infectious progeny, but the glycoprotein of the released virion was abnormal in size, suggesting a defective processing of the asparagine-linked carbohydrate chains in the mutant cell. The Had-1 mutant was resistant to wheat germ agglutinin, but sensitive to a Griffonia simplicifolia lectin, GS-II, which recognizes terminal N-acetylglucosamine residues. The altered sensitivity to these plant lectins compared with that of the parental FM3A cells indicates that sialylated sugar chains on the cell surface are almost absent from the Had-1 cells, thereby rendering the cells NDV receptor deficient.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Adhesion
  • Cell Line
  • Chick Embryo
  • Genetic Complementation Test
  • Hemadsorption
  • Lectins / metabolism
  • Mammary Neoplasms, Experimental
  • Membrane Glycoproteins / biosynthesis
  • Mutation
  • Newcastle disease virus / metabolism*
  • Newcastle disease virus / physiology
  • Receptors, Virus / genetics*
  • Tumor Cells, Cultured
  • Vesicular stomatitis Indiana virus / physiology
  • Viral Envelope Proteins / biosynthesis
  • Viral Proteins / biosynthesis
  • Virus Replication


  • G protein, vesicular stomatitis virus
  • Lectins
  • Membrane Glycoproteins
  • Receptors, Virus
  • Viral Envelope Proteins
  • Viral Proteins