Inhibition of N-linked oligosaccharide trimming does not interfere with surface expression of certain integral membrane proteins.
The effects of 1-deoxynojirimycin (dNM) and 1-deoxymannojirimycin (dMM), inhibitors of oligosaccharide trimming glucosidase I and mannosidase I, respectively, on the biosynthesis of vesicular stomatitis virus G protein, influenza virus hemagglutinin, and human class I histocompatibility antigens were investigated. Although the oligosaccharides of these membrane glycoproteins were greatly altered, neither dNM nor dMM interferred with their surface expression, as determined by a variety of assays, including accessibility to proteases and antibodies; neither did these drugs inhibit production of infectious virus particles.
D017485:1-Deoxynojirimycin; D000818:Animals; D002460:Cell Line; D006224:Cricetinae; D004285:Dogs; D005944:Glucosamine / Q000031:analogs & derivatives / Q000494:pharmacology; D005959:Glucosidases / Q000037:antagonists & inhibitors; D006023:Glycoproteins / Q000096:biosynthesis*; D006680:HLA Antigens / Q000096:biosynthesis; D006389:Hemagglutinins, Viral / Q000096:biosynthesis; D008361:Mannosidases / Q000037:antagonists & inhibitors; D008565:Membrane Proteins / Q000096:biosynthesis*; D011499:Protein Processing, Post-Translational
D006023:Glycoproteins; D006680:HLA Antigens; D006389:Hemagglutinins, Viral; D008565:Membrane Proteins; D017485:1-Deoxynojirimycin; D005959:Glucosidases; D008361:Mannosidases; D005944:Glucosamine