United Kingdom (UK)
Recombinant monoclonal antibody to gB. Manufactured using AbAb’s Recombinant Platform with variable regions (i.e. specificity) from the hybridoma 1G2.
UniProt Accession Number of Target Protein: P13201
Alternative Name(s) of Target: Envelope glycoprotein B; UL55; Ab-50
Immunogen: The original antibody was isolated from EBV transformed human peripheral blood derived B cells derived from hCMV-infected donors.
Specificity: This antibody is specific for a surface epitope in antigenic domain 5 (AD-5), also termed Domain I (Dom I), of Human cytomegalovirus (hCMV) (strain Towne), also called Human herpesvirus 5 (HHV-5). Dom I resides between amino acid residues 133 to 343 of the gB of hCMV strain AD169 and has the following sequence: IVAHTFKVRVYQKVLTFRRSYAYIYTTYLLGSNTEYVAPPMWEIHHINKFAQCYSSYSRVIG
GTVFVAYHRDSYENKTMQLIPDDYSNTHSTRYVTVKDQWHSRGSTWLYRETCNLNCMLT
ITTARSKYPYHFFATSTGDVVYISPFYNGTNRNASYFGENADKFFIFPNYTIVSDFGRPNAA
PETHRLVAFLERADSVISWDIQDEKNVT. The exact epitope lies between Tyr280-Phe300, or: Y-NGTNRNASYFGENADKFFIF-P.
Application Notes: The original version of the antibody was used in a neutralization assay against human cytomegalovirus (hCMV). It was found to neutralize hCMV with high potency — it neutralized the virus with an IC50 of 0.1 μg/ml and an IC90 of 0.4 μg/ml (US9346874B2). The Fab version of this antibody was generated and its structure in complex with hCMV gB was explored using crystallography. It was also used in neutralization assays, surface staining of full-length gB in flow cytometry, and gB immunoprecipitation (Chandramouli et al., 2015; PMID: 26365435).
Antibody first published in:
Pötzsch et al. B cell repertoire analysis identifies new antigenic domains on glycoprotein B of human cytomegalovirus which are target of neutralizing antibodies. PLoS Pathog. 2011 Aug;7(8):e1002172. doi: 10.1371/journal.ppat.1002172. PMID:21852946
Note on publication:
The original publication investigates the B-cell response to glycoprotein B (gB) of human cytomegalovirus (HCMV) in healthy infected individuals, identifying new antigenic domains (AD-4 and AD-5) targeted by neutralizing antibodies, which could inform vaccine design and antibody therapies.