Host antigen as the sulphated moiety of influenza virus haemagglutinin
JC Downie - Journal of General Virology, 1978 - microbiologyresearch.org
JC Downie
Journal of General Virology, 1978•microbiologyresearch.orgInorganic sulphate (35S) was incorporated into the haemagglutinin molecule of
A/Memphis/1/71 (H3N2) influenza virus when a keratosulphate-like host antigen was also
incorporated into the glycoproteins of virus grown in the chorioallantoic membrane of the
embryonated hen's egg. Little or no 35S-sulphate was incorporated when this host antigen
was not present in the glycoproteins of virus grown in chick embryo kidney cells or in the
chorioallantoic membrane of embryonated duck eggs. The presence of the keratosulphate …
A/Memphis/1/71 (H3N2) influenza virus when a keratosulphate-like host antigen was also
incorporated into the glycoproteins of virus grown in the chorioallantoic membrane of the
embryonated hen's egg. Little or no 35S-sulphate was incorporated when this host antigen
was not present in the glycoproteins of virus grown in chick embryo kidney cells or in the
chorioallantoic membrane of embryonated duck eggs. The presence of the keratosulphate …
Summary
Inorganic sulphate (35S) was incorporated into the haemagglutinin molecule of A/Memphis/1/71 (H3N2) influenza virus when a keratosulphate-like host antigen was also incorporated into the glycoproteins of virus grown in the chorioallantoic membrane of the embryonated hen’s egg. Little or no 35S-sulphate was incorporated when this host antigen was not present in the glycoproteins of virus grown in chick embryo kidney cells or in the chorioallantoic membrane of embryonated duck eggs.
The presence of the keratosulphate-like host antigen was required for the stability of the haemagglutinin molecule in sodium dodecyl sulphate (SDS). The haemagglutinin molecules from virus grown in hens’ eggs were stable in SDS, whereas those from virus grown in duck eggs or in chick embryo kidney cells were not and could not be isolated on cellulose acetate.
Chemical analysis showed that there were 87 glucosamine residues and three molecules of sulphate per haemagglutinin subunit as calculated for a trimer molecule having a mol. wt. of 200000. There was one sulphate molecule per HA1 polypeptide chain and this was associated with the slowest migrating carbohydrate-protein complex of an HA1 tryptic digest separated by polyacrylamide gel electrophoresis.
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