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1 Center for Disease Control and Prevention, Division of Vector-Borne Infectious Diseases, Dengue Laboratory, 2 Calle Casia, San Juan, Puerto Rico 00921-3200
2 Division of Vector-Borne Infectious Diseases, Fort Collins, Colorado, U.S.A.
and3 School of Biological Sciences, University of Surrey, Guildford GU2 5XH, U.K.
The glycosylation patterns of the envelope (E) glycoprotein of several naturally occurring strains of St Louis encephalitis (SLE) virus were investigated. SLE viruses were found that contained both glycosylated and non-glycosylated E proteins, and one isolate (Tr 9464) that lacks N-linked glycosylation sites on its E protein was identified. SLE virus monoclonal antibodies that define E protein B cell epitopes and demonstrate biological activities reacted essentially to the same extent with glycosylated and non-glycosylated virions. These results indicate that glycosylation is not essential for epitope conformation or recognition. However, failure to glycosylate the E protein was associated with possible morphogenetic differences as manifested by reduced virus yields and differences in specific infectivity.
Received 25 November 1992;
accepted 15 July 1993.
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