ArticleJournal of molecular modeling2019
HBGA binding modes and selectivity in noroviruses upon mutation: a docking and molecular dynamics study.
Article in Journal of molecular modeling, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 15 citations in OpenAlex.
- Development of a broad-spectrum therapeutic Fc-nanobody for human noroviruses.Journal of virology · 2024Article
- Benchmarking ANI potentials as a rescoring function and screening FDA drugs for SARS-CoV-2 MJournal of computer-aided molecular design · 2024Article
- Revisiting MMPBSA by Adoption of MC-Based Surface Area/Volume, ANI-ML Potentials, and Two-Valued Interior Dielectric Constant.The journal of physical chemistry. B · 2023Article
- Accurate Binding Free Energy Method from End-State MD Simulations.Journal of chemical information and modeling · 2022Article
- Gut Microbiota and Transcriptomics Reveal the Effect of Human Norovirus Bioaccumulation on Oysters (Crassostrea gigas).Microbiology spectrum · 2022Article
- The endemic GII.4 norovirus-like-particle induced-antibody lacks of cross-reactivity against the epidemic GII.17 strain.Journal of medical virology · 2021Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Norovirus, also called winter vomiting bug, is the most common cause for gastroenteritis and severe childhood diarrhea disease. High mutation rates cause drug resistance and thus complicate the development of an effective therapeutics against virus infection. The virus protein enters the host cell via the interaction with histo-blood group antigens (HBGAs), formed by oligosaccharides. To date, the crystal structures of numerous complexes of virus proteins with different antigens have been reported. The HBGAs bind to the two distinct regions of the virus proteins. Herein, the affinity of different variants of virus protein to some common glycans has been computationally analyzed. Molecular docking studies as combination of docking scores and rmsd values revealed that the binding region 1 is more attractive for the ligands in variants of categories 1-5, but selectivity is drastically shifted to region 2 due to in category 6. In addition, molecular dynamics simulations were unraveled when the region 1 is hindered (in category 6); the blocking loop has less fluctuation than that of unblocked in other categories.
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