ACTION OF ORTHOMYXOVIRUS AND PARAMYXOVIRUS NEURAMINIDASE ON GANGLIOSIDES - HYDROLYSIS OF GANGLIOSIDE GM1 BY SENDAI VIRUS NEURAMINIDASE

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  • 1 January 1980
    • journal article
    • research article
    • Vol. 619  (3) , 632-639
Abstract
The action of neuraminidase of influenza A virus, Sendai virus and Newcastle disease virus particles on bovine brain ganglioside GM1 and the properties of Sendai virus neuraminidase for GM1 were studied. With Sendai virus, GM1 was hydrolyzed to asialo-GM1 (GA1) and N-acetylneuraminic acid even in the absence or surfactant or other additives, while the hydrolysis of GM1 by Newcastle disease virus or influenza A virus was very low or undetectable under the same conditions. The formation of GA1 by Sendai virus neuraminidase was confirmed by TLC and immunodiffusion test using anti-GA1 antiserum. The apparent Km of Sendai virus neuraminidase for GM1 hydrolysis was 2.67 .cntdot. 10-4 M and the optimum pH was 5.6. GM3, GM2 and oligosaccharide of GM1 were hydrolyzed more effectively than GM1 in the absence of surfactant (GM3 > GM2 > oligosaccharide of GM1 > GM1). The hydrolysis of GM1 by the Sendai virus enzyme was stimulated by the addition of sodium cholate or sodium taurocholate, but was inhibited by divalent cations (10 mM), Ca2+, Mg2+, Zn2+, Fe2+ and Cu2+. In the absence of the surfactant, Sendai virus neuraminidase hydrolyzed GM1 more efficiently than Arthobacter ureafaciens neuraminidase which was reported recently as being an adequate enzyme to hydrolyze ganglioside GM1 as a substrate.