PURIFICATION OF THE RECEPTOR FOR JAPANESE ENCEPHALITIS VIRUS PREPARED FROM MOUSE BRAIN TISSUE AND SOME OF ITS PROPERTIES

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Purification of the receptor for Japanese encehaplitis virus (JEV) prepared from mouse brain tissue was performed successfully by differential centrifugation, digestion with trypsin, precipitation by streptomycin and centrifugation in D2O.The receptor, which was purified about 2, 000 times from crude extract, had a single peak with a S20°W of about 110 Svedberg units and a buoyant density of 1.06. The purified receptor was found to be composed of lipid and small amounts of carbohydrate and protein.Receptor activity was inactivated by phospholipase C and D, but not proteolytic enzymes such as trypsin and α-chymotrypsin. Interaction of the receptor with JEV proceeded in two stages, reversible and then irreversible. Reversibly attached virus could be dissociated from the receptor by treatment with streptomycin or hydrogen bond dissociating agents such as LiCl and NaCl.The action of the purified receptor was highly specific in a sense that it was effective in inhibiting hemagglutination or infectivity of Arboviruses, but not other viruses so far examined.
日本ウイルス学会の論文