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. 2002 Nov 12;27(2):147–160. doi: 10.1016/0168-1702(93)90078-2

A H1 hemagglutinin of a human influenza A virus with a carbohydrate-modulated receptor binding site and an unusual cleavage site

I Günther a, B Glatthaar b, G Döller b, W Garten a,∗
PMCID: PMC7133948  PMID: 8460527

Abstract

Two receptor binding variants of the influenza virus A/Tübingen/12/85 (H1N1) were separated by their different plaque formation in MDCK cells. Hemagglutination of variant I was restricted to red blood cells of guinea pigs, whereas variant II also hemagglutinated chicken cells. The variants differed also in their ability to bind to α2,6-linked sialic acid. Evidence is presented that this difference is determined by a complex carbohydrate side chain at asparagine131 near the receptor binding site which is absent in variant II. With both variants, the arginine found at the cleavage site of all other human isolates analyzed so far was replaced by lysine.

Keywords: Influenza A virus variant, H1 hemagglutinin, Receptor binding site, Cleavage site

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