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Novel anti‐dengue monoclonal antibody recognizing conformational structure of the prM‐E heterodimeric complex of dengue virus
Author(s) -
Puttikhunt Chunya,
Keelapang Poonsook,
Khemnu Nuanpan,
Sittisombut Nopporn,
Kasinrerk Watchara,
Malasit Prida
Publication year - 2008
Publication title -
journal of medical virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 121
eISSN - 1096-9071
pISSN - 0146-6615
DOI - 10.1002/jmv.21047
Subject(s) - virology , dengue virus , dengue fever , monoclonal antibody , virus , antibody , flavivirus , dengue vaccine , biology , immunology
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. © 2007 Wiley‐Liss, Inc.