Molecular basis of host recognition of human coronavirus 229E

Yu-Xi Tsai, Yu-Chun Chien, Min-Feng Hsu, Kay-Hooi Khoo and Shang-Te Danny Hsu (sthsu@gate.sinica.edu.tw)
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Yu-Xi Tsai: Academia Sinica
Yu-Chun Chien: Academia Sinica
Min-Feng Hsu: Academia Sinica
Kay-Hooi Khoo: Academia Sinica
Shang-Te Danny Hsu: Academia Sinica

Nature Communications, 2025, vol. 16, issue 1, 1-15

Abstract: Abstract Human coronavirus 229E (HCoV-229E) is the earliest CoV found to infect humans. It binds to the human aminopeptidase N (hAPN) through the receptor binding domain (RBD) of its spike (S) protein to achieve host recognition. We present the cryo-electron microscopy structure of two HCoV-229E S protein in complex with a dimeric hAPN to provide structural insights on how the HCoV-229E S protein opens up its RBD to engage with its host receptor, information that is currently missing among alphacoronaviruses to which HCoV-229E belong. We quantitatively profile the glycosylation of HCoV-229E S protein and hAPN to deduce the glyco-shielding effects pertinent to antigenicity and host recognition. Finally, we present an atomic model of fully glycosylated HCoV-229E S in complex with hAPN anchored on their respective membrane bilayers to recapitulate the structural basis of the first step of host infection by HCoV-229E.

Date: 2025
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DOI: 10.1038/s41467-025-57359-8

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