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Peer-reviewedCC BY-NC-ND 4.0Nature Communications

Reoviridae-derived short trimerization domain for stabilizing homo-trimerization of vaccine immunogens and therapeutic proteins

  • Min Wei1,2
  • Qingfang Bu1,2
  • Jin Xiao1,2
  • Lunzhi Yuan1,2
  • Jinmiao Shi1,2
  • Huilin Guo1,2
  • Yang Huang1,2
  • Hui Sun1,2
  • Kai Wang1,2
  • Zonglin Li1,2
  • Min Lin1,2
  • Zhaoming Lu1,2
25 more authors
  • Chen Zheng1,2
  • Jijing Chen1,2
  • Jiahua Gao1,2
  • Zikang Wang1,2
  • Zehong Huang1,2
  • Ruojing Bai1,2
  • Ying Liu1,2
  • Jian Ma1,2
  • Yunda Hong1,2
  • Youfeng Wang1,2
  • Jiayi Wu1,2
  • Yifan Yin1,2
  • Shengxiang Ge1,2
  • Zizheng Zheng1,2
  • Yixin Chen1,2
  • Yi Guan3,4
  • Hai Yu1,2
  • Tianying Zhang1,2
  • Jun Zhang1,2
  • Shaojuan Wang1,2
  • Qingbing Zheng1,2
  • Yangtao Wu1,2
  • Ningshao Xia1,2
  • Yali Zhang1,2
  • Quan Yuan1,2
4 affiliations
  1. 1State Key Laboratory of Vaccines for Infectious Diseases, Xiang An Biomedicine Laboratory, School of Public Health, School of Life Sciences, Xiamen University, Xiamen, PR China
  2. 2National Institute of Diagnostics and Vaccine Development in Infectious Diseases, Collaborative Innovation Center of Biologic Products, National Innovation Platform for Industry-Education Integration in Vaccine Research, Xiamen University, Xiamen, PR China
  3. 3State Key Laboratory of Emerging Infectious Diseases, The University of Hong Kong, Hong Kong, PR China
  4. 4Joint Institute of Virology (Shantou University and The University of Hong Kong), Guangdong-Hongkong Joint Laboratory of Emerging Infectious Diseases, Shantou University, Shantou, PR China
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Abstract

Trimerization motifs play pivotal roles in structural biology and therapeutic protein engineering. Here, we describe a short trimerization motif (rFd1303) derived from the Reoviridae family reovirus σ1 protein. Compared with the widely used T4-Foldon, the rFd1303 increased recombinant protein yields. The rFd1303-fused immunogens of SARS-CoV-2 spike and influenza hemagglutinin elicited antibody responses comparable to T4-Foldon-fused controls in mice. Using this tag, we engineered a trimeric ACE2-Ig fusion protein (TriACE2-Ig) that remained stable after 30 days at room temperature and neutralized a broad range of ACE2-utilizing sarbecoviruses, including 19 SARS-CoV-2 variants, SARS-CoV, and pangolin coronaviruses GD and GX, with higher potency than monomeric ACE2-Ig. In the hamster model challenged with various SARS-CoV-2 variants, our data demonstrated that intranasal TriACE2-Ig administration markedly reduced viral loads, virus-induced body-weight loss, lung pathology, and decreased within-cage virus transmission. These findings highlight rFd1303 as a versatile trimerization platform for vaccine and therapeutic protein development.

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Cite

BibTeXRIS
BibTeX
@article{wei2026reoviridaederived,
  title = {{Reoviridae-derived short trimerization domain for stabilizing homo-trimerization of vaccine immunogens and therapeutic proteins}},
  author = {Min Wei and Qingfang Bu and Jin Xiao and Lunzhi Yuan and Jinmiao Shi and Huilin Guo and Yang Huang and Hui Sun and Kai Wang and Zonglin Li and Min Lin and Zhaoming Lu and Chen Zheng and Jijing Chen and Jiahua Gao and Zikang Wang and Zehong Huang and Ruojing Bai and Ying Liu and Jian Ma and Yunda Hong and Youfeng Wang and Jiayi Wu and Yifan Yin and Shengxiang Ge and Zizheng Zheng and Yixin Chen and Yi Guan and Hai Yu and Tianying Zhang and Jun Zhang and Shaojuan Wang and Qingbing Zheng and Yangtao Wu and Ningshao Xia and Yali Zhang and Quan Yuan},
  journal = {Nature Communications},
  year = {2026},
  month = sep,
  doi = {10.1038/s41467-026-77926-x},
  url = {https://doi.org/10.1038/s41467-026-77926-x},
  note = {CC BY-NC-ND 4.0},
}
RIS
TY  - JOUR
TI  - Reoviridae-derived short trimerization domain for stabilizing homo-trimerization of vaccine immunogens and therapeutic proteins
AU  - Min Wei
AU  - Qingfang Bu
AU  - Jin Xiao
AU  - Lunzhi Yuan
AU  - Jinmiao Shi
AU  - Huilin Guo
AU  - Yang Huang
AU  - Hui Sun
AU  - Kai Wang
AU  - Zonglin Li
AU  - Min Lin
AU  - Zhaoming Lu
AU  - Chen Zheng
AU  - Jijing Chen
AU  - Jiahua Gao
AU  - Zikang Wang
AU  - Zehong Huang
AU  - Ruojing Bai
AU  - Ying Liu
AU  - Jian Ma
AU  - Yunda Hong
AU  - Youfeng Wang
AU  - Jiayi Wu
AU  - Yifan Yin
AU  - Shengxiang Ge
AU  - Zizheng Zheng
AU  - Yixin Chen
AU  - Yi Guan
AU  - Hai Yu
AU  - Tianying Zhang
AU  - Jun Zhang
AU  - Shaojuan Wang
AU  - Qingbing Zheng
AU  - Yangtao Wu
AU  - Ningshao Xia
AU  - Yali Zhang
AU  - Quan Yuan
PY  - 2026
DA  - 2026/09/24
JO  - Nature Communications
DO  - 10.1038/s41467-026-77926-x
UR  - https://doi.org/10.1038/s41467-026-77926-x
AB  - Trimerization motifs play pivotal roles in structural biology and therapeutic protein engineering. Here, we describe a short trimerization motif (rFd1303) derived from the Reoviridae family reovirus σ1 protein. Compared with the widely used T4-Foldon, the rFd1303 increased recombinant protein yields. The rFd1303-fused immunogens of SARS-CoV-2 spike and influenza hemagglutinin elicited antibody responses comparable to T4-Foldon-fused controls in mice. Using this tag, we engineered a trimeric ACE2-Ig fusion protein (TriACE2-Ig) that remained stable after 30 days at room temperature and neutralized a broad range of ACE2-utilizing sarbecoviruses, including 19 SARS-CoV-2 variants, SARS-CoV, and pangolin coronaviruses GD and GX, with higher potency than monomeric ACE2-Ig. In the hamster model challenged with various SARS-CoV-2 variants, our data demonstrated that intranasal TriACE2-Ig administration markedly reduced viral loads, virus-induced body-weight loss, lung pathology, and decreased within-cage virus transmission. These findings highlight rFd1303 as a versatile trimerization platform for vaccine and therapeutic protein development.
SN  - 2041-1723
ER  -