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Targeted Antibody Blocking by a Dual-Functional Conjugate of Antigenic Peptide and Fc-III Mimetics (DCAF)
Published on: September 17, 2019
Novel anti-dengue monoclonal antibody recognizing conformational structure of the prM-E heterodimeric complex of
Chunya Puttikhunt1, Poonsook Keelapang, Nuanpan Khemnu
1Medical Biotechnology Unit, National Center for Genetic Engineering and Biotechnology, National Science and Technology Development Agency, Bangkok, Thailand.
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.
Insights
A new monoclonal antibody, 2E11, specifically detects the dengue virus premembrane-envelope (prM-E) heterodimer. This antibody is a valuable tool for studying flavivirus maturation and export processes.
Area of Science:
- Virology
- Structural Biology
- Immunology
Background:
- Flavivirus assembly requires interaction between premembrane (prM) and envelope (E) glycoproteins.
- The precise nature of the prM-E heterodimer interaction during dengue virus replication needs further elucidation.
Purpose of the Study:
- To generate and characterize a novel mouse monoclonal antibody (Mab) 2E11.
- To confirm the prM-E heterodimer interaction in dengue virus.
Main Methods:
- Generation and characterization of Mab 2E11.
- Immunofluorescence assays.
- Immuno-pull down assays.
- Analysis of transfected cells expressing full-length and truncated E proteins.
Main Results:
- Mab 2E11 specifically recognizes the dengue prM-E heterodimeric complex.
- The antibody binds to prM-E expressed in cis and in trans but not to individual prM or E proteins.
- Reactivity of Mab 2E11 was reduced when a truncated E protein lacking the C-terminal transmembrane region was used.
Conclusions:
- Mab 2E11 is a novel tool for detecting the conformational structure of the dengue virus prM-E heterodimer.
- This antibody can aid in the identification and characterization of the prM-E heterodimer.
- Mab 2E11 will facilitate research into flavivirus maturation and export.
