HCMV Glycoprotein B (R457T, K459Q, R460T mutant, recombinant)

Human cytomegalovirus (HCMV) is a large, enveloped dsDNA virus and member of the Betaherpesvirinae subfamily. HCMV infection in immunocompetent individuals is asymptomatic or causes mild flu-like symptoms but can lead to severe complications in immunocompromised individuals. HCMV infection is also a leading cause of viral congenital birth defects. HCMV glycoprotein B (gB) is a heavily glycosylated type I envelope protein encoded by HCMV open reading frame UL55. It is composed of a large ectodomain, a hydrophobic membrane proximal region (MRP), a transmembrane domain, and an intraviral C-terminal domain. The full-length HCMV gB precursor protein contains a furin cleavage site at the arginine in position 460, where cleavage results in two polypeptides that stay linked by disulfide bonds. It forms a complex with gN on the virion surface and tethers the host cell by interacting with heparan sulfate proteoglycans. HCMV gB is involved in membrane fusion and host cell entry via complex interactions with a variety of host cell receptors on multiple cell types and is also involved in cell-to-cell spread. It contains several antigenic domains, of which two have been identified as the primary HCMV gB targets for neutralizing antibodies. Cayman's HCMV Glycoprotein B (R457T, K459Q, R460T mutant, recombinant) protein can be used for binding assays. This protein is a disulfide-linked homodimer that contains furin cleavage site mutations. The reduced monomer, composed of HCMV glycoprotein B (amino acids 25-700, 777-907) fused to human IgG1 Fc at its C-terminus, consists of 1,045 amino acids, has a calculated molecular weight of 118 kDa, and a predicted N-terminus of Asn25 after signal peptide cleavage. As a result of glycosylation, the monomer migrates at approximately 160-170 kDa by SDS-PAGE under reducing conditions.