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Peer-reviewedCC BY-NC-ND 4.0Virologica Sinica

A dual-glycoprotein-targeting bispecific nanoantibody confers potent neutralization against Nipah virus

  • Shengdong Wang1,2
  • Xinghai Zhang1
  • Haiwei Zhang1
  • Guibo Rao1
  • Yanfeng Yao1
  • Guihong Tian1,2
  • Ge Gao1
  • Yun Peng1
  • Wujian Li3,4,5
  • Sheng Cao1
  • Sandra Chiu3,4,5
  • Rui Gong1,2
1 more authors
  • Li Chen1
5 affiliations
  1. 1State Key Laboratory of Virology and Biosafety, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, China
  2. 2University of Chinese Academy of Sciences, Beijing 100049, China
  3. 3Department of Infectious Disease, The First Affiliated Hospital of USTC, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei 230027, China
  4. 4Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei 230027, China
  5. 5Key Laboratory of Anhui Province for Emerging and Reemerging Infectious Diseases, Hefei 230027, China
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Abstract

Nipah virus (NiV) is a biosafety level 4 pathogen that has consistently posed a significant threat to public health. The two envelope proteins on the viral surface, the receptor-binding protein (RBP) and the fusion (F) protein, are the primary targets of neutralizing antibodies. However, the use of antibodies targeting a single viral antigen often leads to the emergence of resistant strains. Here, by panning phage display library, we obtained a C-type nanoantibody (C-Nab), G-3-1, targeting the head domain of RBP. The half-life-extended G-3-1-HLE effectively protected hamsters against authentic NiV challenge. Furthermore, we constructed a fusion protein, 2A1-3-8-(AP)12-G-3-1, by linking G-3-1 to the F-targeting nanobody 2A1-3-8 via a rigid (AP)12 linker. This fusion protein exhibited improved and balanced neutralizing activity. In addition, the in vivo prophylactic efficacy of 2A1-3-8-(AP)12-G-3-1 was validated in a mouse model of NiV pseudovirus infection. Collectively, this study on a dual-envelope-protein-targeting bispecific antibody not only provides a promising antiviral candidate, but also offers an important design strategy for next-generation antibody optimization.

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Cite

BibTeXRIS
BibTeX
@article{wang2026dualglycoproteintargeting,
  title = {{A dual-glycoprotein-targeting bispecific nanoantibody confers potent neutralization against Nipah virus}},
  author = {Shengdong Wang and Xinghai Zhang and Haiwei Zhang and Guibo Rao and Yanfeng Yao and Guihong Tian and Ge Gao and Yun Peng and Wujian Li and Sheng Cao and Sandra Chiu and Rui Gong and Li Chen},
  journal = {Virologica Sinica},
  year = {2026},
  month = oct,
  doi = {10.1016/j.virs.2026.09.014},
  url = {https://doi.org/10.1016/j.virs.2026.09.014},
  note = {CC BY-NC-ND 4.0},
}
RIS
TY  - JOUR
TI  - A dual-glycoprotein-targeting bispecific nanoantibody confers potent neutralization against Nipah virus
AU  - Shengdong Wang
AU  - Xinghai Zhang
AU  - Haiwei Zhang
AU  - Guibo Rao
AU  - Yanfeng Yao
AU  - Guihong Tian
AU  - Ge Gao
AU  - Yun Peng
AU  - Wujian Li
AU  - Sheng Cao
AU  - Sandra Chiu
AU  - Rui Gong
AU  - Li Chen
PY  - 2026
DA  - 2026/10/09
JO  - Virologica Sinica
DO  - 10.1016/j.virs.2026.09.014
UR  - https://doi.org/10.1016/j.virs.2026.09.014
AB  - Nipah virus (NiV) is a biosafety level 4 pathogen that has consistently posed a significant threat to public health. The two envelope proteins on the viral surface, the receptor-binding protein (RBP) and the fusion (F) protein, are the primary targets of neutralizing antibodies. However, the use of antibodies targeting a single viral antigen often leads to the emergence of resistant strains. Here, by panning phage display library, we obtained a C-type nanoantibody (C-Nab), G-3-1, targeting the head domain of RBP. The half-life-extended G-3-1-HLE effectively protected hamsters against authentic NiV challenge. Furthermore, we constructed a fusion protein, 2A1-3-8-(AP)12-G-3-1, by linking G-3-1 to the F-targeting nanobody 2A1-3-8 via a rigid (AP)12 linker. This fusion protein exhibited improved and balanced neutralizing activity. In addition, the in vivo prophylactic efficacy of 2A1-3-8-(AP)12-G-3-1 was validated in a mouse model of NiV pseudovirus infection. Collectively, this study on a dual-envelope-protein-targeting bispecific antibody not only provides a promising antiviral candidate, but also offers an important design strategy for next-generation antibody optimization.
SN  - 1674-0769
SN  - 1995-820X
ER  -