No abstract

Transmissible gastroenteritis virus grown in primary swine kidney cell cultures agglutinated erythrocytes from chicken, guinea pig and cattle but not erythrocytes from mouse and goose. The optimal incubation temperature was at 4 degrees C. The hemagglutination (HA) reaction was inhibited by specific antiserum. Some factors involved in the HA and HA-inhibition (HI) were investigated and standard HA and HI tests were established. HI antibody titers of individual pig sera showed a significant positive correlation with their neutralizing antibody titers.

Transmissible gastroenteritis virus was readily adsorbed onto chicken erythrocytes at 4 degrees C. The hemagglutinin thus adsorbed could be eluted from the erythrocytes by incubating in phosphate buffered saline at 37 degrees C. The receptor on chicken erythrocytes for the hemagglutinin was inactivated by neuraminidase and potassium periodate, but not by trypsin, 2-mercaptoethanol and formalin. The hemagglutinin was inactivated by trypsin, papain, pepsin, alpha-amylase, phospholipase C, neuraminidase, formalin, 2-mercaptoethanol, potassium periodate, ethyl ether, chloroform, Tween-80 and beta-propiolactone, but not by sodium deoxycholate and trichlorotrifluoroethane, suggesting that the active component of the hemagglutinin involved glycoproteins. The hemagglutinin was stable at 37 degrees C or lower temperatures but not at 60 degrees C or higher temperatures. The hemagglutinin activity was resistant to ultraviolet irradiation, while the infectivity was very susceptible. The hemagglutinin and the infectivity were readily sedimented by ultracentrifugation at 45,000 x g for 60 minutes. In rate zonal centrifugation of the hemagglutinin preparation on a sucrose density gradient, the hemagglutinin activity showed a sharp peak at 1.19 g/ml coinciding with the peak of infectivity. The activity in the peak fraction seemed to be structurally associated with virus particles.

No abstract

No abstract