N -Glycolyl GM1 Ganglioside as a Receptor for Simian Virus 40 (original) (raw)
Related papers
N-Glycolyl GM1 Ganglioside as a Receptor for Simian Virus 40
Journal of Virology, 2007
Carbohydrate microarrays have emerged as powerful tools in analyses of microbe-host interactions. Using a microarray with 190 sequence-defined oligosaccharides in the form of natural glycolipids and neoglycolipids representative of diverse mammalian glycans, we examined interactions of simian virus 40 (SV40) with potential carbohydrate receptors. While the results confirmed the high specificity of SV40 for the ganglioside GM1, they also revealed that N-glycolyl GM1 ganglioside [GM1(Gc)], which is characteristic of simian species and many other nonhuman mammals, is a better ligand than the N-acetyl analog [GM1(Ac)] found in mammals, including humans. After supplementing glycolipid-deficient GM95 cells with GM1(Ac) and
Nature of the Sendai virus receptor: glycoprotein versus ganglioside
Journal of Virology, 1980
Gangliosides were compared with glycoproteins as potential receptors for Sendai virus by incorporating measured amounts of the glycoconjugates into lecithin-cholesterol liposomes and measuring binding by a hemagglutination assay with sheep erythrocytes. HeLa cell gangliosides showed no binding activity toward the virus up to 15 micrograms of sialic acid per 5 mumol of lecithin-cholesterol, whereas HeLa cell glycoproteins incorporated into similar liposomes caused avid virus binding below 1 microgram of sialic acid. These sialoglycoproteins could be separated from the bulk of cell proteins by multiple chloroform-methanol extractions. Purified rat brain gangliosides at a level of 120 micrograms of sialic acid in liposomes did not bind virus, whereas chloroform-methanol-extracted rat brain proteins caused only marginal binding. Bovine brain gangliosides differed slightly from the rat brain mixture in showing weak binding properties. Our results thus indicate that glycoproteins, rather ...
Recognition of the GM3 Ganglioside Glycan by Rhesus Rotavirus Particles
Angewandte Chemie International Edition, 2011
Rotaviruses are a major cause of severe infantile gastroenteritis in humans and animals worldwide, producing a childhood mortality exceeding 650 000 annually. Mapping host cell glycan-virus interactions to define a viral glycointeractome is invaluable in providing new directions for the discovery of novel broad-spectrum drugs and vaccines. In that context we have recently reported the first NMR-based structural analysis of the interaction of GD1a (1) and GM1
Turning the spotlight on the oligosaccharide chain of GM1 ganglioside
Glycoconjugate Journal
It is well over a century that glycosphingolipids are matter of interest in different fields of research. The hydrophilic oligosaccharide and the lipid moiety, the ceramide, both or separately have been considered in different moments as the crucial portion of the molecule, responsible for the role played by the glycosphingolipids associated to the plasma-membranes or to any other subcellular fraction. Glycosphingolipids are a family of compounds characterized by thousands of structures differing in both the oligosaccharide and the ceramide moieties, but among them, the nervous system monosialylated glycosphingolipid GM1, belonging to the group of gangliosides, has gained particular attention by a multitude of Scientists. In recent years, a series of studies have been conducted on the functional roles played by the hydrophilic part of GM1, its oligosaccharide, that we have named “OligoGM1”. These studies allowed to shed new light on the mechanisms underlying the properties of GM1 de...
Glycoconjugate Journal, 1993
The structures of gangliosides from human granulocytes were elucidated by fast atom bombardment mass spectrometry and by gas chromatography/mass spectrometry as their partially methylated alditol acetates. In human granulocytes besides GM3 (II3Neu5Ac-LacCer), neolacto-series gangliosides (IV3Neu5Ac-nLcOse4Cer, IV6Neu5Ac-nLcOsegCer and VI3Neu5Ac-nLcOse6Cer) containing C24:1, and to some extent C22:o; and C16:o fatty acid in their respective ceramide portions, were identified as major components. In this study we demonstrate that gangliosides from human granulocytes, the second most abundant cells in peripheral blood, can serve as receptors for influenza viruses A/PR/8/34 (H 1N1), A/X-31 (H3N2), and a parainfluenza virus Sendai virus (HNF1, Z-strain). Viruses were found to exhibit specific adhesion to terminal Neu5Ac~2-3Gal and/or Neu5Acct2-6Gal sequences as well as depending on the chain length of ganglioside carbohydrate backbones from human granulocytes, these important effector cells which represent the first line of defence in immunologically mediated reactions.
Novel Structural Insights into Rotavirus Recognition of Ganglioside Glycan Receptors
Journal of Molecular Biology, 2011
Rotaviruses ubiquitously infect children under the age of 5, being responsible for more than half a million diarrhoeal deaths each year worldwide. Host cell oligosaccharides containing sialic acid(s) are critical for attachment by rotaviruses. However, to date, no detailed three-dimensional atomic model showing the exact rotavirus interactions with these glycoconjugate receptors has been reported. Here, we present the first crystallographic structures of the rotavirus carbohydrate-recognizing protein VP8 ⁎ in complex with ganglioside G M3 glycans. In combination with assessment of the inhibition of rotavirus infectivity by N-acetyl and Nglycolyl forms of this ganglioside, our results reveal key details of rotavirusganglioside G M3 glycan recognition. In addition, they show a direct correlation between the carbohydrate specificities exhibited by VP8 ⁎ from porcine and by monkey rotaviruses and the respective infectious virus particles. These novel results also indicate the potential binding interactions of rotavirus VP8 ⁎ with other sialic acid-containing gangliosides.
Conformation of the Oligosaccharide Chain of GM1 Ganglioside in a Carbohydrate-Enriched Surface
Biophysical Journal, 1998
The solution structure of ganglioside G M1 carbohydrate moiety at the surface of a 102-kDa lipid-modified-G M1 micelle is investigated by high-resolution 1 H-NMR in H 2 O. The micellar surface can be considered a cluster-like lateral distribution of the gangliosides, each single monomer being anchored in a carbohydrate-enriched model membrane matrix. 1 H NOESY measurements at short mixing times reveal a rigid trisaccharide core--GalNAc-(1-4)-[␣-Neu5Ac-(2-3)]--Galand a more flexible -Gal-(1-3)--GalNActerminal glycosidic bond. In the lipid-modified G M1 ganglioside micellar system, there is no evidence that intermolecular side-by-side carbohydrate interactions modulate, or alter in any way, the head-group spatial arrangement. Possible intermonomer interactions at the level of the branched trisaccharide portion were further investigated on mixed micelles of natural N-glycolyl-and N-acetylneuraminic acid containing G M1 in D 2 O, taking advantage of the different NMR features of N-glycolyl-and N-acetylneuraminic acids, which allow discrimination between sialic acid ring proton signals. Measurements of the water/ganglioside-OH proton chemical exchange rates suggest hydroxyl group involvement at position 8 of sialic acid in strong intramolecular interaction processes.
Journal of Virology, 2012
Human norovirus infections are the most common cause of acute nonbacterial gastroenteritis in humans worldwide, and glycan binding plays an important role in the susceptibility to these infections. However, due to the lack of an efficient cell culture system or small animal model for human noroviruses, little is known about the biological role of glycan binding during infection. Murine noroviruses (MNV) are also enteric viruses that bind to cell surface glycans, but in contrast to their human counterparts, they can be grown in tissue culture and a small animal host. In this study, we determined glycan-binding specificities of the MNV strains MNV-1 and CR3 in vitro, identified molecular determinants of glycan binding, and analyzed infection in vivo. We showed that unlike MNV-1, CR3 binding to murine macrophages was resistant to neuraminidase treatment and glycosphingolipid depletion. Both strains depended on N-linked glycoproteins for binding, while only MNV-1 attachment to macrophages was sensitive to O-linked glycoprotein depletion. In vivo, CR3 showed differences in tissue tropism compared to MNV-1 by replicating in the large intestine. Mapping of a glycan-binding site in the MNV-1 capsid by reverse genetics identified a region topologically similar to the histo-blood group antigen (HBGA)-binding sites of the human norovirus strain VA387. The recombinant virus showed distinct changes in tissue tropism compared to wild-type virus. Taken together, our data demonstrate that MNV strains evolved multiple strategies to bind different glycan receptors on the surface of murine macrophages and that glycan binding contributes to tissue tropism in vivo.
Gangliosides as binding sites in SA-11 rotavirus infection of LLC-MK2 cells
Journal of General Virology, 1991
The chemical nature of receptors involved in the attachment of simian rotavirus (SA-11) to a monkey kidney cell line (LLC-MK2) was investigated. Enzymic treatment of cells before virus infection indicated that membrane proteins and phospholipids are not involved in virus attachment, whereas sialic acid and galactose participate in the receptor structure to differing extents. Incubation of SA-11 with bovine brain gangliosides before infection strongly reduced its ability to bind to cell membranes. Similar experiments with individual purified gangliosides from bovine brain showed that virus infection was prevented by preincubation with GM1. Moreover, desialylated cells regained susceptibility to virus infection when coated with whole gangliosides or GM1 immediately after Clostridium perfringens neuraminidase treatment. The binding of SA-11 to whole gangliosides or GM1 was quantified by an ELISA procedure. The results suggest that gangliosides, mainly GM1, are part of the receptor structure for SA-11 of susceptible LLC-MK2 cells.
Journal of Virology, 2009
Updated information and services can be found at: These include: REFERENCES http://jvi.asm.org/content/83/9/4092#ref-list-1 at: This article cites 65 articles, 34 of which can be accessed free CONTENT ALERTS more» articles cite this article), Receive: RSS Feeds, eTOCs, free email alerts (when new http://journals.asm.org/site/misc/reprints.xhtml Information about commercial reprint orders: http://journals.asm.org/site/subscriptions/ To subscribe to to another ASM Journal go to: