Affinity of lectins for rabies virus: Partial structural analysis of oligosaccharides and virus purification
Review articleOpen access
1981/10/01 Full-length article DOI: 10.1016/S0769-2617(81)80035-4
Journal: Annales de l'Institut Pasteur / Virologie
SummaryLectins (PHA-Els, WGA, RcA, LcA and in a lesser extent ConA) interact with rabies virus through specific binding to external polysaccharides, in vitro leading to the appearance of large aggregates, detectable by absorbance. On the other hand, no aggregation was recorded using limulin, while PNA only aggregated desialated particles. On the basis of the known specificity of each lectin and their specific affinity towards viral carbohydrate moieties (evaluated from the initial rates of the in vitro aggregation reactions) it may be concluded that sugar moiety could correspond to the following sequence: NeuNAc-Gal-GlcNAc-Man…Morevoer, since the WGA aggregation may be easily reversed by specific ligand, we deviced an affinity chromatographic method useful to purify rabies virus. Our results indicate that the whole virus may be specifically retained by the immobilized lectin, while soluble glycoconjugates (glycoprotein or glycopeptides) do not lead to the formation of stable complexes.
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