Development of anti-dengue virus D8 neutralizing monoclonal antibody production in Nicotiana benthamiana
Issued Date
2026-03-01
Resource Type
eISSN
2215017X
Scopus ID
2-s2.0-105030886064
Journal Title
Biotechnology Reports
Volume
49
Rights Holder(s)
SCOPUS
Bibliographic Citation
Biotechnology Reports Vol.49 (2026)
Suggested Citation
Niyompun G., Rattanapisit K., Jaratsittisin J., Suwanchaikasem P., Sootichote R., Sittikul P., Pitaksajjakul P., Ramasoota P., Phoolcharoen W. Development of anti-dengue virus D8 neutralizing monoclonal antibody production in Nicotiana benthamiana. Biotechnology Reports Vol.49 (2026). doi:10.1016/j.btre.2026.e00951 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/115495
Title
Development of anti-dengue virus D8 neutralizing monoclonal antibody production in Nicotiana benthamiana
Author's Affiliation
Corresponding Author(s)
Other Contributor(s)
Abstract
Dengue is a life-threatening mosquito-borne viral disease ranging from mild symptoms to severe hemorrhagic fever. In this study, a recombinant anti-dengue D8 monoclonal antibody was produced in Nicotiana benthamiana and characterized for protein integrity and glycosylation by LC-MS. The plant-derived antibody lacked plant-specific β1,2-xylose and core α1,3-fucose residues, displaying a mammalian-like glycan profile. Functional evaluation showed potent cross-neutralizing activity against all four dengue virus serotypes (DENV1–DENV4), with the strongest activity against DENV4 (FRNT50 ' 1 µg/mL), followed by DENV2 (5.82 µg/mL), DENV3 (9.49 µg/mL), and DENV1 (28.68 µg/mL), comparable to the mammalian-produced counterpart. The antibody also bound strongly to NS1 proteins of all serotypes, especially DENV2, and demonstrated higher reactivity than mammalian-derived anti-NS1 antibodies. Collectively, our results provide proof-of-concept that a glycoengineered plant platform can generate a functional D8 antibody with mammalian-like glycosylation, robust NS1 binding, and cross-neutralizing activity against DENV1–4, prompting further evaluation in Fc-dependent assays and in vivo models.