Recognition by human A and B influenza viruses of 8- and 7-carbon analogues of sialic acid modified in the polyhydroxyl side chain.
To evaluate the recognition by influenza viruses of the C9-C7 polyhydroxylated moiety of sialic acid (SA) receptor determinant a novel assay has been developed based on the assessment of binding by the solid-phase immobilized virus of the enzyme-labeled sialyglycoprotein fetuin treated by periodate or periodate/borohydride to contain an 8-carbon aldehyde, 7-carbon aldehyde, or corresponding hydroxyl analogues of SA. Some features of recognition by human influenza viruses of these SA analogues were type and subtype specific, especially marked differences being found between type A and type B viruses. At the same time a significant diversity was observed among virus strains belonging to the same subtype. The assay described provides a new tool for the differentiation of influenza viruses according to receptor binding properties and for an investigation of molecular interactions in the receptor binding site of the virus.
Matrosovich
M N
MN
Institute of Poliomyelitis and Viral Encephalitides, USSR Academy of Medical Sciences, Moscow Region.
Gambaryan
A S
AS
Reizin
F N
FN
Chumakov
M P
MP
D066298:In Vitro Techniques; D019158:N-Acetylneuraminic Acid; D009975:Orthomyxoviridae / Q000378:metabolism*; D010084:Oxidation-Reduction; D010504:Periodic Acid / Q000737:chemistry; D011991:Receptors, Virus / Q000378:metabolism*; D012794:Sialic Acids / Q000737:chemistry / Q000378:metabolism*; D013329:Structure-Activity Relationship; D000509:alpha-Fetoproteins / Q000378:metabolism
D011991:Receptors, Virus; D012794:Sialic Acids; D000509:alpha-Fetoproteins; D010504:Periodic Acid; D019158:N-Acetylneuraminic Acid