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| Main Authors: | , , , , , |
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| Format: | Artículo científico |
| Language: | en |
| Published: |
Archives of virology
2025
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| Subjects: | |
| Online Access: | https://pubmed.ncbi.nlm.nih.gov/40169405/ |
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Table of Contents:
- Identification of a recombinant GII.13[P21] norovirus strain: molecular dynamic simulations indicate that gene mutations shifted its spectrum of binding to host receptor glycans. Chen, Yunfei Zhou, Zexian Dong, Lei Jin, Miao Wang, Yongjie Yu, Yongxin Norovirus Molecular Dynamics Simulation Humans Caliciviridae Infections Blood Group Antigens Mutation Polysaccharides Genome, Viral Gastroenteritis Protein Binding Feces Human norovirus is a pervasive pathogen that causes global outbreaks of viral gastroenteritis. Previous studies have suggested that histo-blood group antigens (HBGAs) can interact with human norovirus, facilitating its entry of host cells and significantly affecting its evolution. In this study, the complete genome sequence of recombinant GII.13[P21] norovirus from fecal samples was analyzed. Molecular dynamics simulations of GII.13 norovirus P proteins from 1978 to 2019 showed changes in their capacity to bind to HBGAs. Initially, GII.13 proteins bound A or B/H-type HBGAs, but subsequent mutations resulted in a loss of this binding capacity, favoring binding to the HBGA type I precursor (Lewis c) over A or B/H and Lewis antigens.