%0 Journal Article %A Banks, Theresa %A Huo, Bin %A Kousoulas, Konstantin %A Spaete, Richard %A Pachl, Carol %A Pereira, Lenore %T A Major Neutralizing Domain Maps within the Carboxyl-terminal Half of the Cleaved Cytomegalovirus B Glycoprotein %D 1989 %J Journal of General Virology, %V 70 %N 4 %P 979-985 %@ 1465-2099 %R https://doi.org/10.1099/0022-1317-70-4-979 %K epitope mapping %K glycoprotein B %K CMV %I Microbiology Society, %X SUMMARY Cytomegalovirus (CMV) encodes several glycoproteins reported to be structural homologues of glycoproteins encoded by herpes simplex virus type 1 (HSV-1). To map the antigenic and functional domains on the 907 amino acid CMV glycoprotein B (gB), we cloned and expressed a subfragment of BamHI fragment R of the CMV (Towne) genome into an expression vector and reacted the resulting gene product with a panel of monoclonal antibodies. Our results showed that the DNA fragment encodes related glycoproteins which we previously designated gA and which others have reported to be homologous to HSV-1 gB in CMV (AD169). Analyses of the processing of CMV gB transiently expressed in eukaryotic cells showed that glycosylation occurred independently of viral infection. Ten antibodies with complement-dependent and independent neutralizing activity reacted with a truncated derivative of gB that contained 619 amino-terminal residues but lacked the transmembrane and intracellular regions of the molecule. Twelve additional antibodies reacted with a CHO cell line expressing a 680 amino-terminal derivative of gB. All of the reactive antibodies precipitated the 447 residue carboxy-terminal cleavage product of gB from extracts of CMV-infected cells. These results showed that the neutralizing epitopes map in at least two domains of gB which are located in a discontinuous segment of 219 amino acids between residues 461 and 680 from the amino terminus of the molecule. %U https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-70-4-979