Abstract
Summary: During the purification of GDVII virus from infected mouse brains by red cell adsorption and elution it was found that haemagglutination with human red cells occurred at both 4 C and at room temperature. This reaction had previously been reported to take place only at the former temperature and the present work demonstrated that different rates of adsorption of virus on erythrocytes existed for the purified virus and the crude saline suspensions of infected mouse brain. These observations are discussed as a possible explanation of the mechanism of non-specific inhibition of GDVII virus haemagglutination by normal mouse brain extracts described elsewhere. An investigation of the mechanism of haemagglutination by the GDVII virus disclosed that in a salt-free medium adsorption of haemagglutinins was complete at 4 C and partial at 18 C. Once virus-red cell combination had taken place elution occurred only into an electrolyte-containing solution. While the haemagglutinin titre was not materially influenced by the presence of different electrolytes at a static molarity, a study of the adsorption and elution rates revealed considerable variation among the salts tested. Of particular interest was the observation that elution of adsorbed virus was considerably retarded by calcium ions. These findings have been compared and contrasted with corresponding reactions exhibited by members of the influenza group of viruses.