Comparative antirhinoviral activities of soluble intercellular adhesion molecule-1 (sICAM-1) and chimeric ICAM-1/immunoglobulin A molecule.
We conducted a comparative study of the antirhinovirus activities of soluble intercellular adhesion molecule-1 (sICAM-1) and a chimeric ICAM-1/immunoglobulin A (IgA) molecule (ICI-5D/IgA) for nine major receptor group human rhinovirus (HRV) serotypes and for a variant of HRV-39 relatively resistant to inhibition by sICAM-1. ICI-5D/IgA inhibited the infectivity of eight of the nine wild-type HRVs and the resistant HRV-39 variant and was 60 to 170 times more potent than sICAM-1 on a molar basis. In contrast to sICAM-1, ICI-5D/IgA directly neutralized the infectivity of the representative HRVs by approximately 1 log10. These results expand on the antirhinovirus spectrum of ICI-5D/IgA, confirm that dimeric forms of sICAM-1 have a higher antirhinoviral potency than monomeric sICAM-1, and indicate that cross-linking of two adjacent receptor binding sites on the virus capsid by a divalent receptor enhances the direct inactivation of viral infectivity.
Crump
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CE
Department of Internal Medicine, University of Virginia School of Medicine, Charlottesville 22908.
Arruda
E
E
Hayden
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FG
D000998:Antiviral Agents / Q000494:pharmacology*; D015815:Cell Adhesion Molecules / Q000494:pharmacology*; D006367:HeLa Cells; D006801:Humans; D007070:Immunoglobulin A / Q000494:pharmacology*; D018799:Intercellular Adhesion Molecule-1; D011993:Recombinant Fusion Proteins / Q000494:pharmacology*; D012229:Rhinovirus / Q000187:drug effects*
D000998:Antiviral Agents; D015815:Cell Adhesion Molecules; D007070:Immunoglobulin A; D011993:Recombinant Fusion Proteins; D018799:Intercellular Adhesion Molecule-1