Reduced temperature prevents transfer of a membrane glycoprotein to the cell surface but does not prevent terminal glycosylation

Cell. 1983 Aug;34(1):233-43. doi: 10.1016/0092-8674(83)90154-x.

Abstract

The transport kinetics of the influenza virus hemagglutinin from its site of synthesis to the apical plasma membrane of Madin-Darby canine kidney cells, a polarized epithelial cell line, were studied by a sensitive tryptic assay. Hemagglutinin acquired terminal sugars, as judged by sensitivity to endo-beta-N-acetylglucosaminidase H, 10-15 min after synthesis, and first appeared on the apical domain 15 min later. None of the pulse-labeled hemagglutinin accumulated on the basolateral domain. At 20 degrees C, terminal glycosylation continued, but no hemagglutinin was detected on the cell surface within 2 hr. If the incubation temperature was raised from 20 degrees C to 37 degrees C, hemagglutinin was quickly externalized, demonstrating that the inhibition at low temperature was reversible.

MeSH terms

  • Animals
  • Biological Transport
  • Cell Line
  • Cell Membrane / metabolism*
  • Dogs
  • Hemagglutinins, Viral*
  • Influenza A virus / metabolism*
  • Kinetics
  • Oligosaccharides / metabolism*
  • Temperature
  • Viral Envelope Proteins
  • Viral Proteins / metabolism*

Substances

  • Hemagglutinins, Viral
  • Oligosaccharides
  • Viral Envelope Proteins
  • Viral Proteins