Molecular basis for receptor recognition and broad host tropism for merbecovirus MjHKU4r-CoV-1.
EMBO Rep
; 25(7): 3116-3136, 2024 Jul.
Article
en En
| MEDLINE
| ID: mdl-38877169
ABSTRACT
A novel pangolin-origin MERS-like coronavirus (CoV), MjHKU4r-CoV-1, was recently identified. It is closely related to bat HKU4-CoV, and is infectious in human organs and transgenic mice. MjHKU4r-CoV-1 uses the dipeptidyl peptidase 4 (DPP4 or CD26) receptor for virus entry and has a broad host tropism. However, the molecular mechanism of its receptor binding and determinants of host range are not yet clear. Herein, we determine the structure of the MjHKU4r-CoV-1 spike (S) protein receptor-binding domain (RBD) complexed with human CD26 (hCD26) to reveal the basis for its receptor binding. Measuring binding capacity toward multiple animal receptors for MjHKU4r-CoV-1, mutagenesis analyses, and homology modeling highlight that residue sites 291, 292, 294, 295, 336, and 344 of CD26 are the crucial host range determinants for MjHKU4r-CoV-1. These results broaden our understanding of this potentially high-risk virus and will help us prepare for possible outbreaks in the future.
Palabras clave
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Unión Proteica
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Receptores Virales
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Dipeptidil Peptidasa 4
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Tropismo Viral
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Especificidad del Huésped
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Glicoproteína de la Espiga del Coronavirus
Límite:
Animals
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Humans
Idioma:
En
Año:
2024
Tipo del documento:
Article