Formation and activity of covalent conjugates of poliovirus and ligands binding to cell surface structures
Identifieur interne : 001565 ( Main/Exploration ); précédent : 001564; suivant : 001566Formation and activity of covalent conjugates of poliovirus and ligands binding to cell surface structures
Auteurs : Christin Munkebye Aarnes [Norvège] ; Inger Helene Madshus [Norvège] ; Jean Claude Guillemot [Norvège] ; Kirsten Sandvig [Norvège] ; Sjur Olsnes [Norvège]Source :
- Experimental Cell Research [ 0014-4827 ] ; 1987.
English descriptors
- Teeft :
- Ammonium acetate, Apical side, Asialoglycoprotein receptor, Biotin, Biotinylated, Biotinylated cells, Buoyant density, Cell surface, Cellular receptor, Cona, Conformational change, Conjugate, Diphtheria toxin, Free streptavidin, Hela, Hela ohio cells, Hydrophobic domains, Intact conjugate, Large number, Lysate, Microtitre plates, Natural poliovirus receptors, Olsnes, Poliovirus, Poliovirus receptors, Proc natl acad, Productive infection, Radioactive material, Receptor, Same buffer, Sandvig, Sendai virus, Specific binding, Streptavidin, Unbound conjugate, Unmodified, Unmodified cells, Unmodified virus, Unreacted streptavidin, Unreacted virus, Virus, Virus entry, Virus particle, Virus particles, Virus receptor, Virus surface.
Abstract
Abstract: Disulfide-linked conjugates of poliovirus with streptavidin or concanavalin A were formed and the binding of the conjugates to mouse L cells that lack natural poliovirus receptors was studied. The conjugate with streptavidin was specifically bound to biotinylated L cells, but not to unmodified L cells. The conjugate with conA was bound to L cells in the absence of, but not in the presence of α-methyl mannoside. Incubation of L cells with bound conjugates did not produce virus, although the conjugates were highly infectious in HeLa cells, containing natural poliovirus receptors. This suggests that the artificially bound virus was unable to penetrate the L cells and start replication. The possibility that binding of the virus to the natural receptor is required for efficient infection is discussed.
Url:
DOI: 10.1016/0014-4827(87)90322-3
Affiliations:
Links toward previous steps (curation, corpus...)
- to stream Istex, to step Corpus: 000553
- to stream Istex, to step Curation: 000533
- to stream Istex, to step Checkpoint: 000703
- to stream Main, to step Merge: 001588
- to stream Main, to step Curation: 001565
Le document en format XML
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<term>Biotinylated</term>
<term>Biotinylated cells</term>
<term>Buoyant density</term>
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<term>Cellular receptor</term>
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<term>Conformational change</term>
<term>Conjugate</term>
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<term>Free streptavidin</term>
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<term>Intact conjugate</term>
<term>Large number</term>
<term>Lysate</term>
<term>Microtitre plates</term>
<term>Natural poliovirus receptors</term>
<term>Olsnes</term>
<term>Poliovirus</term>
<term>Poliovirus receptors</term>
<term>Proc natl acad</term>
<term>Productive infection</term>
<term>Radioactive material</term>
<term>Receptor</term>
<term>Same buffer</term>
<term>Sandvig</term>
<term>Sendai virus</term>
<term>Specific binding</term>
<term>Streptavidin</term>
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<term>Unmodified</term>
<term>Unmodified cells</term>
<term>Unmodified virus</term>
<term>Unreacted streptavidin</term>
<term>Unreacted virus</term>
<term>Virus</term>
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<term>Virus particle</term>
<term>Virus particles</term>
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<front><div type="abstract" xml:lang="en">Abstract: Disulfide-linked conjugates of poliovirus with streptavidin or concanavalin A were formed and the binding of the conjugates to mouse L cells that lack natural poliovirus receptors was studied. The conjugate with streptavidin was specifically bound to biotinylated L cells, but not to unmodified L cells. The conjugate with conA was bound to L cells in the absence of, but not in the presence of α-methyl mannoside. Incubation of L cells with bound conjugates did not produce virus, although the conjugates were highly infectious in HeLa cells, containing natural poliovirus receptors. This suggests that the artificially bound virus was unable to penetrate the L cells and start replication. The possibility that binding of the virus to the natural receptor is required for efficient infection is discussed.</div>
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