Action of influenza virus neuraminidase on gangliosides. Haemagglutinin inhibits viral neuraminidase. 1985

V A Slepushkin, and A G Bukrinskaya, and N V Prokazova, and L S Zhigis, and P D Reshetov, and J I Shaposhnikova, and L D Bergelson

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.

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
D009439 Neuraminidase An enzyme that catalyzes the hydrolysis of alpha-2,3, alpha-2,6-, and alpha-2,8-glycosidic linkages (at a decreasing rate, respectively) of terminal sialic residues in oligosaccharides, glycoproteins, glycolipids, colominic acid, and synthetic substrate. (From Enzyme Nomenclature, 1992) Sialidase,Exo-alpha-Sialidase,N-Acylneuraminate Glycohydrolases,Oligosaccharide Sialidase,Exo alpha Sialidase,Glycohydrolases, N-Acylneuraminate,N Acylneuraminate Glycohydrolases,Sialidase, Oligosaccharide
D009980 Influenza A virus The type species of the genus ALPHAINFLUENZAVIRUS that causes influenza and other diseases in humans and animals. Antigenic variation occurs frequently between strains, allowing classification into subtypes and variants. Transmission is usually by aerosol (human and most non-aquatic hosts) or waterborne (ducks). Infected birds shed the virus in their saliva, nasal secretions, and feces. Alphainfluenzavirus influenzae,Avian Orthomyxovirus Type A,FLUAV,Fowl Plague Virus,Human Influenza A Virus,Influenza Virus Type A,Influenza Viruses Type A,Myxovirus influenzae-A hominis,Myxovirus influenzae-A suis,Myxovirus pestis galli,Orthomyxovirus Type A,Orthomyxovirus Type A, Avian,Orthomyxovirus Type A, Human,Orthomyxovirus Type A, Porcine,Pestis galli Myxovirus,Fowl Plague Viruses,Influenza A viruses,Myxovirus influenzae A hominis,Myxovirus influenzae A suis,Myxovirus, Pestis galli,Myxoviruses, Pestis galli,Pestis galli Myxoviruses,Plague Virus, Fowl,Virus, Fowl Plague
D005677 G(M1) Ganglioside A specific monosialoganglioside that accumulates abnormally within the nervous system due to a deficiency of GM1-b-galactosidase, resulting in GM1 gangliosidosis. GM1 Ganglioside,Monosialosyl Tetraglycosyl Ceramide,GM1a Monosialoganglioside,Ceramide, Monosialosyl Tetraglycosyl,Ganglioside, GM1,Monosialoganglioside, GM1a,Tetraglycosyl Ceramide, Monosialosyl
D005732 Gangliosides A subclass of ACIDIC GLYCOSPHINGOLIPIDS. They contain one or more sialic acid (N-ACETYLNEURAMINIC ACID) residues. Using the Svennerholm system of abbrevations, gangliosides are designated G for ganglioside, plus subscript M, D, or T for mono-, di-, or trisialo, respectively, the subscript letter being followed by a subscript arabic numeral to indicated sequence of migration in thin-layer chromatograms. (From Oxford Dictionary of Biochemistry and Molecular Biology, 1997) Ganglioside,Sialoglycosphingolipids
D006389 Hemagglutinins, Viral Specific hemagglutinin subtypes encoded by VIRUSES. Viral Hemagglutinin,Viral Hemagglutinins,Hemagglutinin, Viral

Related Publications

V A Slepushkin, and A G Bukrinskaya, and N V Prokazova, and L S Zhigis, and P D Reshetov, and J I Shaposhnikova, and L D Bergelson
January 2002, Reviews in medical virology,
V A Slepushkin, and A G Bukrinskaya, and N V Prokazova, and L S Zhigis, and P D Reshetov, and J I Shaposhnikova, and L D Bergelson
February 2009, Antiviral research,
V A Slepushkin, and A G Bukrinskaya, and N V Prokazova, and L S Zhigis, and P D Reshetov, and J I Shaposhnikova, and L D Bergelson
June 2009, Biologicals : journal of the International Association of Biological Standardization,
V A Slepushkin, and A G Bukrinskaya, and N V Prokazova, and L S Zhigis, and P D Reshetov, and J I Shaposhnikova, and L D Bergelson
March 1970, The Journal of general virology,
V A Slepushkin, and A G Bukrinskaya, and N V Prokazova, and L S Zhigis, and P D Reshetov, and J I Shaposhnikova, and L D Bergelson
September 1980, Biochimica et biophysica acta,
V A Slepushkin, and A G Bukrinskaya, and N V Prokazova, and L S Zhigis, and P D Reshetov, and J I Shaposhnikova, and L D Bergelson
October 1968, Biochimica et biophysica acta,
V A Slepushkin, and A G Bukrinskaya, and N V Prokazova, and L S Zhigis, and P D Reshetov, and J I Shaposhnikova, and L D Bergelson
May 2008, Journal of virology,
V A Slepushkin, and A G Bukrinskaya, and N V Prokazova, and L S Zhigis, and P D Reshetov, and J I Shaposhnikova, and L D Bergelson
March 1989, Acta virologica,
V A Slepushkin, and A G Bukrinskaya, and N V Prokazova, and L S Zhigis, and P D Reshetov, and J I Shaposhnikova, and L D Bergelson
June 1976, Postgraduate medical journal,
V A Slepushkin, and A G Bukrinskaya, and N V Prokazova, and L S Zhigis, and P D Reshetov, and J I Shaposhnikova, and L D Bergelson
July 1963, Journal of neurochemistry,
Copied contents to your clipboard!