Arch Virol. 1991;120(3-4):289-96.

Intraepidemic variants of influenza virus H3 hemagglutinin differing in the number of carbohydrate side chains.

Seidel W, Künkel F, Geisler B, Garten W, Herrmann B, Döhner L, Klenk HD.

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Institut für medizinische Mikrobiologie, Ernst-Moritz-Arndt-Universität, Greifswald, Federal Republic of Germany.

Abstract

During the epidemic outbreak in the region of Greifswald in the winter 1974/75, we found influenza virus variants which showed differences in the electrophoretic mobility of HA. Among the 25 isolates 13 were of slower and 12 of higher mobility. HA1 of 6 isolates was studied by determining the number of the carbohydrate side chains and by direct sequencing of vRNA. Evidence is presented that variants showing a slower electrophoretic mobility of HA1 had consistently acquired a seventh carbohydrate side chain at Asn 126 in epitope A. All the isolates differed from the reference strain A/Port Chalmers/1/73 by the loss of the oligosaccharide at Asn 81. The field strain A/Dresden/3/71 possessed only 5 oligosaccharides in HA1. These results suggest that changes in glycosylation are an important mechanism in the structural variation underlying antigenic drift of HA.

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