Novel anti‐dengue monoclonal antibody recognizing conformational structure of the prM‐E heterodimeric complex of dengue virus

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Abstract
An interaction between the premembrane (prM) and envelope (E) glycoproteins as prM‐E heterodimer is required for proper folding and transport of E during the formation and release of new flaviviral progeny. More evidence, however, is needed to confirm this interaction of prM and E during dengue virus replication. In this study, 2E11, a mouse monoclonal antibody (Mab) that specifically recognizes dengue prM‐E heterodimeric complex in either intracellular or secreted dengue virions, was generated and characterized. In immunofluorescence and immuno‐pull down assays, the Mab 2E11 recognized an epitope present in 293T transfectants that co‐expressed prM and the full‐length form of E in cis and in trans, but it failed to react with prM or E protein expressed individually. The reactivity of Mab 2E11 was diminished in transfected cells that co‐express prM together with a truncated form of E lacking the 84‐residue stretch at the C‐terminal transmembrane region, presumably essential for prM and E interaction. The Mab 2E11 described in this study is a novel Mab with a unique capability in detecting the conformational structure of prM‐E heterodimeric complex of dengue virus. It will be a new biological tool for identification and characterization of dengue prM‐E heterodimer as well as virus maturation and export. J. Med. Virol. 80:125–133, 2008.

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