title: Reduced temperature prevents transfer of a membrane glycoprotein to the cell surface but does not prevent terminal glycosylation.
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: D000818:Animals; D001692:Biological Transport; D002460:Cell Line; D002462:Cell Membrane / Q000378:metabolism*; D004285:Dogs; D006389:Hemagglutinins, Viral; D009980:Influenza A virus / Q000378:metabolism*; D007700:Kinetics; D009844:Oligosaccharides / Q000378:metabolism*; D013696:Temperature; D014759:Viral Envelope Proteins; D014764:Viral Proteins / Q000378:metabolism*
chemical_list: D006389:Hemagglutinins, Viral; D009844:Oligosaccharides; D014759:Viral Envelope Proteins; D014764:Viral Proteins