レクチンによる狂犬病ウイルスの凝集
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概要
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Wheat germ agglutinin (WGA), concanavalin-A (con A) and ricinus communis agglutinin (RCA_60) were used to study agglutination of purified HEP-Flury strain of rabies virus. The degree of agglutination was estimated by determining the recovery of infectivity, HA activity and CF activity of the resulting virus-lectin aggregates after incubation of the virus with lectins for 60 min. at room temperature. The aggregates were reversed by N-acetyl-glucosamine for WGA aggregates, by α-methyl-mannoside for Con A aggregates and by galactose for RCA_<60> aggregates before assaying biological activities of the virus. The results showed that the maximum virus agglutination occurred when the WGA and Con A were used at a final concentration of 500μg/ml, and the recovery of the infectivity was 99.98% and 93.3%, respectively. However, when RCA_<60> was used at a final concentration of 250μg/ml, the recovery of the infectivity was as low as 1.1%. The solubilization of the virus glycoprotein was attempted with three different detergents (Triton X-100, NP-40 and saponin) using 3H-glucosamine labelled virus. Treatment of the virus with Triton X-100 at final concentrations of 0.25% and 2% and with NP-40 at a final concentration of 0.25% resulted in the disruption of more than 85% of the virion, as indicated by the release of radioactive virion subunits. Saponin was not effective in solubilizing the glycoprotein, at least in the present test conditions. These results appear to indicate that the rabies virus glycoprotein may be isolated from the virion either with Triton X-100, or with NP-40, and purified by WGA or Con A affinity column chromatography.
- 1979-12-28
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