HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Jackson, D. C. Articles by White, D. O. Search for Related Content PubMed PubMed Citation Articles by Jackson, D. C. Articles by White, D. O. Agricola Articles by Jackson, D. C. Articles by White, D. O.

Antigenic Determinants of Influenza Virus Haemagglutinin. VI. Antigenic Characterization of the Oligosaccharide Sidechains from HA₁ of Influenza Virus Haemagglutinins

Department of Microbiology University of Melbourne, Parkville, Victoria, 3052, Australia

The oligosaccharide sidechains attached to the major polypeptide, HA₁ of the haemagglutinin of influenza virus were examined for antigenic activity using a solid-phase radioimmunoassay. Cross-reactivity between the HA₁ of different human subtypes was clearly demonstrable with IgG raised against purified virus but was abrogated if anti-carbohydrate antibodies were first removed by passage of the IgG through an immunoadsorbent column containing haemagglutinin (HA) from an unrelated avian influenza strain. Antibodies eluted from the column were found to cross-react with the HA₁ of all subtypes tested. ‘Host antigen’ extracted from chick chorioallantoic membrane and coupled to Sepharose was also able to remove cross-reactive antibodies from antiviral sera, while antibodies raised against host antigen bound to the HA₁ isolated from each subtype tested. It is concluded that, although there are qualitative and quantitative differences between the oligosaccharide sidechains of influenza haemagglutinins, the antigenically active side-chains are cross-reactive.

Received 12 June 1980; accepted 22 July 1980.