ArticleNature communications2019
A post-translational modification of human Norovirus capsid protein attenuates glycan binding.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
What it found
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Who cites it
35 citing papers in PubMed.
- Insights into the role of internal catalysts in asparagine-to-succinimide conversion in a hyperthermophilic glutamine amidotransferase.The Journal of biological chemistry · 2026Article
- Advanced NMR Characterization and Sensitive Detection of Isoaspartate in Proteins.Analytical chemistry · 2026Article
- Medical Gas Plasma Inactivates Adenoviruses via Capsid Oxidation.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
- Structural basis for sequence context-independent single-stranded DNA cytosine deamination by the bacterial toxin SsdA.Nature communications · 2025Article
- An integrated proteomics approach identifies phosphorylation sites on viral and host proteins that regulate West Nile virus infection.Cell reports · 2025Article
- Semisynthesis of Isomerized Histone H4 Reveals Robustness and Vulnerability of Chromatin toward Molecular Aging.Journal of the American Chemical Society · 2025Article
- Virus-Glycan Interactions Studied by Solute NMR.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Genomic characterization of norovirus and Sapovirus from a diarrhea outbreak in a school linked to heavy rainfall.Frontiers in microbiology · 2025Article
- Conformational Flexibility in Capsids Encoded by theViruses · 2024Review
- Probing effects of site-specific aspartic acid isomerization on structure and stability of GB1 through chemical protein synthesis.Protein science : a publication of the Protein Society · 2024Article
- Evolutionary Spread of Distinct O-methyltransferases Guides the Discovery of Unique Isoaspartate-Containing Peptides, Pamtides.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Article
- Elucidating the Implications of NorovirusViruses · 2023Review
- Conformational Control of Fast Asparagine Deamidation in a Norovirus Capsid Protein.Biochemistry · 2023Article
- Distinct dissociation rates of murine and human norovirus P-domain dimers suggest a role of dimer stability in virus-host interactions.Communications biology · 2022Article
- Assignment of Ala, Ile, LeuBiomolecular NMR assignments · 2022Article
- Norovirus-glycan interactions - how strong are they really?Biochemical Society transactions · 2022Article
- Physicochemical tools for studying virus interactions with targeted cell membranes in a molecular and spatiotemporally resolved context.Analytical and bioanalytical chemistry · 2021Review
- Mass Spectrometry-Based System for Identifying and Typing Norovirus Major Capsid Protein VP1.Viruses · 2021Article
- Protein Secondary Structure Affects Glycan Clustering in Native Mass Spectrometry.Life (Basel, Switzerland) · 2021Article
Corrections and comments
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Authors and funding
12 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Attachment of human noroviruses to histo blood group antigens (HBGAs) is essential for infection, but how this binding event promotes the infection of host cells is unknown. Here, we employ protein NMR experiments supported by mass spectrometry and crystallography to study HBGA binding to the P-domain of a prevalent virus strain (GII.4). We report a highly selective transformation of asparagine 373, located in an antigenic loop adjoining the HBGA binding site, into an iso-aspartate residue. This spontaneous post-translational modification (PTM) proceeds with an estimated half-life of a few days at physiological temperatures, independent of the presence of HBGAs but dramatically affecting HBGA recognition. Sequence conservation and the surface-exposed position of this PTM suggest an important role in infection and immune recognition for many norovirus strains.
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