A defense against rhinoviruses might nonetheless succeed by exploiting hidden similarities among the rhinovirus strains. For example, most rhinovirus strains bind to the same kind of molecule on a cells surface when they attack human cells. Colonno, taking advantage of these common receptors, devised a strategy for blocking the attachment of rhinoviruses to their appropriate receptors. Rather than fruitlessly searching for an antibody that would bind to all rhinoviruses, Colonno realized that an antibody binding to the common receptors of a human cell would prevent rhinoviruses from initiating an infection. Because human cells normally do not develop antibodies to components of their own cells, Colonno injected human cells into mice, which did produce an antibody to the common receptor. In isolated human cells, this antibody proved to be extraordinarily effective at thwarting the rhinovirus. Moreover, when the antibody was given to chimpanzees, it inhibited rhinoviral growth, and in humans it lessened both the severity and duration of cold symptoms.
Another possible defense against rhinoviruses was proposed by Rossman, who described rhinoviruses detailed molecular structure. Rossman showed that protein sequences common to all rhinovirus strains lie at the base of a deep canyon scoring each face of the capsid. The narrow opening of this canyon possibly prevents the relatively large antibody molecules from binding to the common sequence, but smaller molecules might reach it. Among these smaller, nonantibody molecules, some might bind to the common sequence, lock the nucleic acid in its coat, and thereby prevent the virus from reproducing.
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