B. Kropff et M. Mach, IDENTIFICATION OF THE GENE CODING FOR RHESUS CYTOMEGALOVIRUS GLYCOPROTEIN-B AND IMMUNOLOGICAL ANALYSIS OF THE PROTEIN, Journal of General Virology, 78, 1997, pp. 1999-2007
The nucleotide sequence of the gene encoding glycoprotein B (gB) of rh
esus cytomegalovirus (RhCMV) was determined and the protein characteri
zed. The open reading frame of gB encoded a protein of 854 amino acids
with 60% identity and 75% similarity at the amino acid level to human
cytomegalovirus (HCMV) gB. Cysteine residues in the extraluminal part
of the protein are perfectly conserved. Out of the 16 potential N-lin
ked glycosylation sites present in HCMV gB, 15 are conserved in RhCMV
gB. Immunoblot analyses with antisera detected three bands of 150 kDa,
90-110 kDa and 55 kDa representing the full-length gB as well as the
proteolytic cleavage products. Cross-reactivity and cross-neutralizati
on of a number of HCMV gB-specific monoclonal antibodies with RhCMV gB
indicated sharing of immunogenic epitopes between the two molecules.
The RhCMV gB regions corresponding to antigenic domains AD-1, 2 and 3
of HCMV gB were immunogenic during natural RhCMV infection with the AD
-1 region being the immunodominant domain. The data indicate that RhCM
V might represent a useful model to investigate pathogenesis and immun
e surveillance of cytomegaloviruses.