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• W1457757497 endingPage "168" @default.
• W1457757497 startingPage "103" @default.
• W1457757497 abstract "The vast majority of monoclonal antibodies to flaviviruses produced so far are specific for the E glycoprotein; therefore, this chapter deals with the characteristics of epitopes on this immunologically dominant protein. In addition, recent studies with NV3-specific monoclonal antibodies provide evidence that this nonstructural glycoprotein may play an important role in mounting a protective immune response. These new aspects have been emphasized. The analysis of flavivirus structural glycoproteins with monoclonal antibodies revealed a serological complexity that goes far beyond that established by polyclonal sera. At the epitope level, antigenic relationships are strongly determined by the assay system used, and differing patterns of cross-reactivities are obtained when different functional tests are applied. For the tick-borne encephalitis (TBE) virus system, it has been shown that increased binding is due to up to six-fold enhancement of antibody avidity. The structural characteristics of monoclonal antibody-defined epitopes have been determined for TBE virus. Epitopes in both major domains appear to be strongly conformational dependent, with the difference that domain A is very labile and easily denatured, whereas domain B is strongly stabilized by disulfide bridges. For all flaviviruses analyzed with monoclonal antibodies, the dissociation of different functional activities is apparent at the epitope level. All types of different qualitative and quantitative combinations can be observed." @default.
• W1457757497 created "2016-06-24" @default.
• W1457757497 creator A5080446878 @default.
• W1457757497 date "1986-01-01" @default.
• W1457757497 modified "2023-10-14" @default.
• W1457757497 title "Epitope Mapping of Flavivirus Glycoproteins" @default.
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