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A divalent antibody format is required for neutralization of human cytomegalovirus via antigenic domain 2 on glycoprotein B

Department of Immunotechnology, Lund University, PO Box 7031, S-220 07 Lund, Sweden¹
Department of Immunology, Royal Free and University College Medical School, Royal Free Campus, London NW3 2PF, UK²

Author for correspondence: Mats Ohlin. Fax +46 46 2224200. e-mail mats.ohlin{at}immun.lth.se

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.

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