Abstract
Rotavirus, strain SA11, glycoprotein VP7 that was expressed by a recombinant herpes simplex virus-1 or contained in purified rotavirus particles lost reactivity with the neutralizing monoclonal antibody (mAb) 159, but not with nonneutralizing mAbs, upon chelation of calcium by EGTA. Exposing VP7, but not the neutralizing mAbs, to a transient excess of EGTA over calcium eliminated VP7 neutralizing epitopes. Therefore, a calcium chelation-induced conformational change in VP7, not in the neutralizing mAbs, caused the epitope loss. Addition of excess calcium or strontium, but not magnesium or barium, to EGTA-treated VP7 restored its 159 epitope. These results suggest that VP7 binds calcium in the absence of other rotavirus proteins and that the calcium chelation-induced conformational change in VP7 may mediate uncoating of double-shelled rotavirus particles.
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