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J Gen Virol 69 (1988), 2797-2807; DOI 10.1099/0022-1317-69-11-2797
© 1988 Society for General Microbiology
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Low pH-induced Conformational Change of Rubella Virus Envelope Proteins

Shigetaka Katow and A. Sugiura

Department of Measles Virus, National Institute of Health, 4-9-1 Gakuen, Musashi-Murayama, Tokyo 190-12, Japan

Fusion of rubella virus-infected cells was induced by their brief treatment at pH below 6.0. Exposure of rubella virus to pH 5 caused an irreversible conformational change of the viral envelope glycoproteins, E1 and E2. The change was manifested in the marked reduction in both infectivity and haemagglutinating activity of the virus, the increased resistance of E1 and decreased resistance of E2 polypeptides to proteolytic digestion with trypsin, and the acquisition of liposome-binding activity of the virus. The above changes are presumed to mimic the events occurring in the acidic environment within endosomes following endocytosis of the virus.

Keywords: rubella virus, envelope proteins, liposome-binding

Received 29 March 1988; accepted 25 July 1988.


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