The action of partly purified neuraminidase (NA) of influenza A virus, a mixture of detergent solubilized NA and haemagglutinin (HA) and of intact virions on gangliosides GTlb, gdla, GDlb, gmlwas studied. The viral NA transformed gtlbmainly into GDlbWith formation of only minor amounts of GMl. HA was found to inhibit the hydrolysis activity of viral NA. At the same time viral NA transformed GDlaquantitatively into gmlwhich was not hydrolyzed by the enzyme. These results suggest that the function of NA is to transfer the 'primary' receptor (such as GTlb) into the proper carbohydrate sequence (GDlb-like) which is proposed to serve as the minimal structure required for influenza virus reception. © 1985.
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