ArticleJournal of virology1994
Assay for evaluation of rotavirus-cell interactions: identification of an enterocyte ganglioside fraction that mediates group A porcine rotavirus recognition.
Article in Journal of virology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
22 citing papers in PubMed, 67 citations in OpenAlex.
- Fatty acid 2-hydroxylase facilitates rotavirus uncoating and endosomal escape.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Whey Protein Lipid Concentrate High in Milk Fat Globule Membrane Components Inhibit Porcine and Human RotavirusFrontiers in pediatrics · 2021Article
- Sialoglycovirology of Lectins: Sialyl Glycan Binding of Enveloped and Non-enveloped Viruses.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Glycosphingolipid-Protein Interaction in Signal Transduction.International journal of molecular sciences · 2016Review
- Solar and temperature treatments affect the ability of human rotavirus wa to bind to host cells and synthesize viral RNA.Applied and environmental microbiology · 2015Article
- Influence of Epicuticular Physicochemical Properties on Porcine Rotavirus Adsorption to 24 Leafy Green Vegetables and Tomatoes.PloS one · 2015Article
- Carbohydrate recognition by rotaviruses.Journal of structural and functional genomics · 2014Review
- Gangliosides have a functional role during rotavirus cell entry.Journal of virology · 2013Article
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- Role of sialic acids in rotavirus infection.Glycoconjugate journal · 2006Review
- Microbial adhesion of Cryptosporidium parvum sporozoites: purification of an inhibitory lipid from bovine mucosa.The Journal of parasitology · 2004Article
- Evolution of cell recognition by viruses: a source of biological novelty with medical implications.Advances in virus research · 2003Review
- Oligosaccharides as receptors for JC virus.Journal of virology · 2002Article
- Initial interaction of rotavirus strains with N-acetylneuraminic (sialic) acid residues on the cell surface correlates with VP4 genotype, not species of origin.Journal of virology · 2002Article
- Glycosphingolipid binding specificities of rotavirus: identification of a sialic acid-binding epitope.Journal of virology · 2001Article
- Biochemical characterization of rotavirus receptors in MA104 cells.Journal of virology · 2000Article
- Structure and function of a ganglioside receptor for porcine rotavirus.Journal of virology · 1998Article
- Characterization of the interaction between VP8 of bovine rotavirus C486 and cellular components on MA-104 cells and erythrocytes.Canadian journal of veterinary research = Revue canadienne de recherche veterinaire · 1998Article
- Rotavirus is released from the apical surface of cultured human intestinal cells through nonconventional vesicular transport that bypasses the Golgi apparatus.Journal of virology · 1997Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A virus-host cell-binding assay was developed and used to investigate specific binding between group A porcine rotavirus and MA-104 cells or porcine enterocytes. A variety of glycoconjugates and cellular components were screened for their ability to block rotavirus binding to cells. During these experiments a crude ganglioside mixture was observed to specifically block rotavirus binding. On the basis of these results, enterocytes were harvested from susceptible piglets and a polar lipid fraction was isolated by solvent extraction and partitioning. Throughout subsequent purification of this fraction by Sephadex partition, ion-exchange, silicic acid, and thin-layer chromatography, blocking activity behaved as a monosialoganglioside (GMX) that displayed a thin-layer chromatographic mobility between those of GM2 and GM3. The blocking activity of GMX was inhibited by treatment with neuraminidase and ceramide glycanase but not by treatment with protease or heat (100 degrees C). Further purification of GMX by high-pressure liquid chromatography resulted in the resolution of two monosialogangliosides, GMX and a band which comigrated with GM1 on thin-layer chromatography. These data suggest that a cell surface monosialoganglioside or family of monosialogangliosides may function as an in vivo relevant receptor for group A porcine rotavirus and that sialic acid is a required epitope for virus-binding activity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.