Slepushkin V A, Bukrinskaya A G, Prokazova N V, Zhigis L S, Reshetov P D, Shaposhnikova J I, Bergelson L D
FEBS Lett. 1985 Mar 25;182(2):273-7. doi: 10.1016/0014-5793(85)80314-8.
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 GT1b, GD1a, GD1b, GM1 was studied. The viral NA transformed GT1b mainly into GD1b with formation of only minor amounts of GM1. HA was found to inhibit the hydrolysis activity of viral NA. At the same time viral NA transformed GD1a quantitatively into GM1 which was not hydrolyzed by the enzyme. These results suggest that the function of NA is to transfer the 'primary' receptor (such as GT1b) into the proper carbohydrate sequence (GD1b-like) which is proposed to serve as the minimal structure required for influenza virus reception.
研究了甲型流感病毒部分纯化的神经氨酸酶(NA)、去污剂溶解的NA与血凝素(HA)混合物以及完整病毒粒子对神经节苷脂GT1b、GD1a、GD1b、GM1的作用。病毒NA主要将GT1b转化为GD1b,仅生成少量GM1。发现HA可抑制病毒NA的水解活性。同时,病毒NA将GD1a定量转化为GM1,而GM1不会被该酶水解。这些结果表明,NA的功能是将“初级”受体(如GT1b)转化为合适的碳水化合物序列(类GD1b),该序列被认为是流感病毒受体所需的最小结构。