The alpha-anomeric form of sialic acid is the minimal receptor determinant recognized by reovirus.
A series of synthetic sialosides were evaluated for their ability to interact with reovirus serotype 3. It was found that sialosides with terminal N-acetylneuraminic acid (NeuNAc) linked in either an alpha 2,3 or alpha 2,6 configuration effectively blocked the binding of reovirus to mouse L fibroblasts, in contrast to a monosaccharide mixture containing the oligosaccharide constituents. Direct binding of reovirus to the sialosides was also demonstrable using sialosides conjugated to bovine serum albumin as ligands in a solid phase binding system. Of particular significance was the finding that the conjugate containing alpha-sialic acid alone (linked to bovine serum albumin) was capable of being recognized by reovirus at a level comparable to that of the other sialoside conjugates. Virus binding was abrogated by pretreating such conjugates with neuraminidase. These results suggest that the alpha-anomeric form of sialic acid is the minimal receptor determinant for reovirus recognition.
Department of Microbiology and Infectious Diseases, University of Calgary Health Sciences Centre, Alberta, Canada.
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Paul
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Choi
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Lee
D002240:Carbohydrate Sequence; D008969:Molecular Sequence Data; D015394:Molecular Structure; D011991:Receptors, Virus / Q000502:physiology*; D012087:Reoviridae / Q000502:physiology*; D012794:Sialic Acids / Q000502:physiology*; D012795:Sialoglycoproteins / Q000502:physiology*; D013329:Structure-Activity Relationship
D011991:Receptors, Virus; D012794:Sialic Acids; D012795:Sialoglycoproteins