Enterovirus Hemagglutination: Inhibition by Aldoses and a Possible Mechanism

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Abstract
Summary: Aldoses, but not their polyhydroxyl counterparts, were active in inhibiting enterovirus HA. The fewer the number of carbon atoms in the aliphatic chain, the broader (in terms of the number of enteroviruses which are inhibited from HA) the blocking capacity of the compound. Thus glycerylaldehyde was much less specific and more active than D-galactose, D-mannose or D-ribose. Formaldehyde inhibited the HA of all of the viruses which were tested, namely echoviruses type 3, 7, 11, 12 and 19; coxsackieviruses group B, type 1 and 5; and reovirus type 2. The carbonyl group of these aldoses is thus implicated as the necessary reactive site in these blocking reactions. A number of L-amino acids were tested similarly for their ability to block enterovirus-red blood cell union. They were remarkably inactive. Pretreatment of erythrocytes with D, L-glycerylaldehyde rendered them much less agglutinable by echoviruses, type 3, 11 and 19; reovirus type 2; and coxsackievirus group B, type 1. Similarly treated red blood cells were not altered in their agglutinability by echoviruses type 7 and 12. The active aldoses attach firmly to erythrocytes, but not to virus. Enterovirus HA may involve the binding of a carbonyl group of a terminal sugar from an oligosaccharide side chain on the virus capsid to a specific receptor on the red cell surface.

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