Glycosylation requirements for intracellular transport and function of the hemagglutinin of influenza virus.

摘要: The contribution of each the seven asparagine-linked oligosaccharide side chains on hemagglutinin A/Aichi/68 (X31) strain influenza virus was assessed with respect to its effect folding, intracellular transport, and biological activities molecule. Twenty mutant hemagglutinins were constructed expressed, which had one or more glycosylation sites removed. Investigations these indicated that (i) no individual chain is necessary sufficient for function molecule, (ii) at least five are required X31 molecule move along exocytic pathway plasma membrane, (iii) having less than form aggregates retained in endoplasmic reticulum. Images