Abstract
Monoclonal antibodies (MAbs) that neutralized human cytomegalovirus (HCMV) were produced by ten hybrid cells lines, generated from BALB/c mice immunized with HCMV-infected human fibroblasts. By immunoblot technique six antibodies detected a set of HCMV glycosylated polypeptides which, when separated under reducing conditions, migrated with apparent molecular weights (m.wt.) of 47.5K, 51K, 54K, 58K, and 60-69K. One other antibody reacted only with the 47.5 and 51K polypeptides and the 60-69K broad band. Under nonreducing conditions, these antibodies showed no reactivity with any polypeptide. The three remaining MAbs reacted with two high-m.wt. polypeptides of approximately 200K and greater than 200K when separated under nonreducing conditions. One of these antibodies showed no clear reactivity with the polypeptides, one detected a 58K and 92-94K species and one detected a 58K and 130K species, when separated under reducing conditions.
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