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Action of influenza virus neuraminidase on gangliosides
Author(s) -
Slepushkin V.A.,
Bukrinskaya A.G.,
Prokazova N.V.,
Zhigis L.S.,
Reshetov P.D.,
Shaposhnikova J.I.,
Bergelson L.D.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80314-8
Subject(s) - neuraminidase , virology , action (physics) , virus , h5n1 genetic structure , chemistry , covid-19 , biology , medicine , physics , disease , quantum mechanics , infectious disease (medical specialty)
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 G Tlb , g dla , G Dlb , g ml was studied. The viral NA transformed g tlb mainly into G Dlb With formation of only minor amounts of G Ml . HA was found to inhibit the hydrolysis activity of viral NA. At the same time viral NA transformed G Dla quantitatively into g ml which was not hydrolyzed by the enzyme. These results suggest that the function of NA is to transfer the ‘primary’ receptor (such as G Tlb ) into the proper carbohydrate sequence (G Dlb ‐like) which is proposed to serve as the minimal structure required for influenza virus reception.