@article{mbs:/content/journal/jgv/10.1099/0022-1317-83-8-2001, author = "Lantto, Johan and Fletcher, Jean M. and Ohlin, Mats", title = "A divalent antibody format is required for neutralization of human cytomegalovirus via antigenic domain 2 on glycoprotein B", journal= "Journal of General Virology", year = "2002", volume = "83", number = "8", pages = "2001-2005", doi = "https://doi.org/10.1099/0022-1317-83-8-2001", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-83-8-2001", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", abstract = "Glycoprotein B (gB) of human cytomegalovirus (HCMV) is the dominating protein in the envelope of this virus and gives rise to virus-neutralizing antibodies in most infected individuals. We have previously isolated a neutralizing human antibody specific for antigenic domain 2 (AD-2) on gB, a poorly immunogenic epitope, which nevertheless is capable of eliciting potent neutralizing antibodies. In order to define parameters important for the neutralization of HCMV via gB, we have investigated the virus-neutralizing capacity and the kinetics of the interaction with AD-2 of the monomeric and dimeric forms of a single chain variable fragment (scFv) corresponding to this antibody. We demonstrate here that neutralization of HCMV via AD-2 on gB can be mediated by dimeric scFv, while monomeric fragments cannot mediate neutralization of the virus, despite a slow dissociation from the intact glycoprotein. This finding is discussed in the context of possible mechanisms for antibody-mediated virus neutralization.", }