ArticlePLoS pathogens2019
Unraveling the role of the secretor antigen in human rotavirus attachment to histo-blood group antigens.
Article in PLoS pathogens, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 60 citations in OpenAlex.
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- Factors contributing to the frequent interspecies transmission of G4P[6]Microbial genomics · 2026Article
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- Infant gut anellovirus composition associates with early life factors and childhood atopic disease.Nature communications · 2025Article
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- Specific binding of human P[28] rotavirus VP8* protein to blood group ABH antigens on type 1 chains.PLoS pathogens · 2025Article
- Human milk oligosaccharide secretion dynamics during breastfeeding and its antimicrobial role: A systematic review.World journal of clinical pediatrics · 2025Article
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- Human Rotaviruses of Multiple Genotypes Acquire Conserved VP4 Mutations during Serial Passage.Viruses · 2024Article
- Synthesis of fucosyllactose using α-L-fucosidases GH29 from infant gut microbial metagenome.Applied microbiology and biotechnology · 2024Article
- Infant Non-Secretor Histoblood Group Antigen Phenotype Reduces Susceptibility to Both Symptomatic and Asymptomatic Rotavirus Infection.Pathogens (Basel, Switzerland) · 2024Article
- Culture of Human Rotaviruses in Relevant Models Shows Differences in Culture-Adapted and Nonculture-Adapted Strains.International journal of molecular sciences · 2023Article
- Gut Microbial Sialidases and Their Role in the Metabolism of Human Milk Sialylated Glycans.International journal of molecular sciences · 2023Review
- Diverse Sensory Repertoire of Paralogous Chemoreceptors Tlp2, Tlp3, and Tlp4 inMicrobiology spectrum · 2022Article
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- Infant Gut Microbial Metagenome Mining of α-l-Fucosidases with Activity on Fucosylated Human Milk Oligosaccharides and Glycoconjugates.Microbiology spectrum · 2022Article
- Novel fold of rotavirus glycan-binding domain predicted by AlphaFold2 and determined by X-ray crystallography.Communications biology · 2022Article
- Human Milk Oligosaccharides: Potential Applications in COVID-19.Biomedicines · 2022Review
- Milk lactose protects against porcine group A rotavirus infection.Frontiers in microbiology · 2022Article
- The Role of Host Glycobiology and Gut Microbiota in Rotavirus and Norovirus Infection, an Update.International journal of molecular sciences · 2021Review
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Rotavirus is the leading agent causing acute gastroenteritis in young children, with the P[8] genotype accounting for more than 80% of infections in humans. The molecular bases for binding of the VP8* domain from P[8] VP4 spike protein to its cellular receptor, the secretory H type-1 antigen (Fuc-α1,2-Gal-β1,3-GlcNAc; H1), and to its precursor lacto-N-biose (Gal-β1,3-GlcNAc; LNB) have been determined. The resolution of P[8] VP8* crystal structures in complex with H1 antigen and LNB and site-directed mutagenesis experiments revealed that both glycans bind to the P[8] VP8* protein through a binding pocket shared with other members of the P[II] genogroup (i.e.: P[4], P[6] and P[19]). Our results show that the L-fucose moiety from H1 only displays indirect contacts with P[8] VP8*. However, the induced conformational changes in the LNB moiety increase the ligand affinity by two-fold, as measured by surface plasmon resonance (SPR), providing a molecular explanation for the different susceptibility to rotavirus infection between secretor and non-secretor individuals. The unexpected interaction of P[8] VP8* with LNB, a building block of type-1 human milk oligosaccharides, resulted in inhibition of rotavirus infection, highlighting the role and possible application of this disaccharide as an antiviral. While key amino acids in the H1/LNB binding pocket were highly conserved in members of the P[II] genogroup, differences were found in ligand affinities among distinct P[8] genetic lineages. The variation in affinities were explained by subtle structural differences induced by amino acid changes in the vicinity of the binding pocket, providing a fine-tuning mechanism for glycan binding in P[8] rotavirus.
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