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A monoclonal antibody (MAb), N2, neutralized human cytomegalovirus (HCMV) infectivity in the absence of complement and recognized a normal cell protein. By immunofluorescence, MAb N2 detected antigens in uninfected human cells, but not in cells of non-human origin. Antigens were present at the membrane and were dispersed diffusely within the cytoplasm. MAb N2 immunoprecipitated a glycoprotein with an M r of 94K from uninfected and infected cells. In infected cells only, it also recognized a protein of M r 34K which was not linked to the 94K M r glycoprotein by disulphide bonds. N2 neutralized both laboratory and field isolates of HCMV. A study of the distribution of the N2 neutralization epitope recognized among fresh isolates of HCMV showed that only 67% of the isolates could be neutralized by this antibody. There was no correlation between the number of in vitro passages and the level of neutralization. The 34K M r polypeptide was present in cells infected by all isolates. It thus appears that, during virus assembly, HCMV acquires a normal cell protein that bears a neutralization epitope.
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