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1 Institut für Klinische und Molekulare Virologie, Friedrich-Alexander-Universität Erlangen-Nürnberg, Loschgestrasse 7, 8520 Erlangen, Germany
2 Department of Virology, National Bacteriological Laboratory and Karolinska Institute, Stockholm, Sweden
and3 Division of Oral Biology, School of Dentistry, University of California San Francisco, San Francisco, California 94143, U.S.A.
Glycoprotein gp116 of human cytomegalovirus (HCMV) is a target for neutralizing antibodies. Gp116 is a component of the gCI complex which consists of gp58 and gp116. Like its homologue, glycoprotein B of herpes simplex virus type 1, gp116 contains a highly antigenic region in the N-terminal part of the molecule, between amino acids 28 and 84. Prokaryotic expression plasmids and synthetic peptides were used to define binding sites for mouse and human monoclonal antibodies (MAbs) as well as HCMV convalescent sera. Site I, located between amino acids 68 and 77, contains an epitope recognized by the human MAb C23, which is capable of neutralizing HCMV independently of complement and the site is conserved between HCMV strains. Of HCMV-positive human sera, 53% recognized site I. Site II was mapped using mouse MAbs as well as human sera. It is located between residues 50 and 54, an area which is not conserved between strains AD169 and Towne, the two laboratory strains of known sequence. Strain-specific antibodies were detected in 25% of human sera. Site II-specific antibodies, purified from human sera by affinity chromatography, were found to be incapable of neutralizing HCMV in tissue culture.
Received 6 February 1992;
accepted 20 May 1992.
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