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

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. In this study, the authors engineer a short trimerization tag for vaccine and therapeutic protein development. The tag enables a trimeric ACE2 decoy that exhibits broad neutralizing activity against coronaviruses and confers protection in animal models.

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Journal
Nature Communications
Published
2026-09-24
DOI
https://doi.org/10.1038/s41467-026-77926-x
Primary Topic
SARS-CoV-2 and COVID-19 Research
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article
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Reoviridae-derived short trimerization domain for stabilizing homo-trimerization of vaccine immunogens and therapeutic proteins

Tianying Zhang, Yangtao Wu, Shengxiang Ge, Zehong Huang et al.
Nature Communications
SARS-CoV-2 and COVID-19 Research
article

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

Tianying Zhang, Yangtao Wu, Shengxiang Ge, Zehong Huang, Qingbing Zheng, Jijing Chen, Shaojuan Wang, Zikang Wang, Ruojing Bai, Yunda Hong, Yi Guan, Hai Jing Yu, Lunzhi Yuan, Zizheng Zheng, Ningshao Xia, Quan Yuan, Jiahua Gao, Jun Zhang, Min Wei, Hui Sun, Huilin Guo, Yuehua Chen, Zhaoming Lu, Yifan Yin, Jinmiao Shi, Qingfang Bu, Youfeng Wang, Jin Xiao, Chen Zheng, Jiayi Wu, Yali Zhang, Min Lin, Ying Liu, Jian Ma, Yang Huang, Zonglin Li, Kai Wang
article en

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. In this study, the authors engineer a short trimerization tag for vaccine and therapeutic protein development. The tag enables a trimeric ACE2 decoy that exhibits broad neutralizing activity against coronaviruses and confers protection in animal models.

Nature Communications
Xiamen University (CN), Shantou University (CN), University of Hong Kong (HK)
Good health and well-being
Openalex Percentile: Top 12%
SARS-CoV-2 and COVID-19 Research
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