Abstract
The protein capsid of noroviruses is composed of a protruding (P) domain and a shell that encases the genomic RNA. Bile salts enhance receptor (CD300lf) binding to the mouse norovirus (MNV) P domain and collapse the highly mobile P domain onto the shell surface. Williams et al. (e00176-21) determined the high-resolution cryo-electron microscopy (cryo-EM) structure of the P domain complexed with a neutralizing Fab and demonstrate that bile salts cause allosteric conformational changes that block antibody recognition to the top of the P domain. Therefore, MNV hijacks the host’s own bile to escape antibody-mediated neutralization while enhancing cell attachment.
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