Regulation of receptor binding affinity of influenza virus hemagglutinin by its carbohydrate moiety.

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摘要：

The (HA) of the () strain of has two N-linked attached to Asn123 and Asn149 in the vicinity of the site. The effect of these carbohydrate side chains on the of HA to -containing receptors has been analyzed. When the were deleted by site-specific , HA expressed from a vector showed enhanced hemadsorbing activity. was so strong under these conditions that erythrocytes were no longer released by viral and that release was significantly reduced when from was used. Similarly, when these were removed selectively from purified by N-glycosidase F, such were unable to elute from receptors, although they retained activity. Thus, release of from cell receptors depends on the presence of the HA at Asn123 and Asn149. On the other hand, was abolished when these were sialylated after expression in the absence of (M. Ohuchi, A. Feldmann, R. Ohuchi, and H.-D. Klenk, Virology 212:77-83, 1995). These observations indicate that the receptor affinity of HA is controlled by adjacent to the site.

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Animals Dogs Erythrocytes Cells, Cultured Cell Line Influenza A virus Virion Hemagglutinin Glycoproteins, Influenza Virus Glycosylation Binding Sites