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Binding Characteristics Determine the Neutralizing Potential of Antibody Fragments Specific for Antigenic Domain 2 on Glycoprotein B of Human Cytomegalovirus

Lantto, Johan LU ; Fletcher, Jean M. and Ohlin, Mats LU (2003) In Virology 305(1). p.201-209
Abstract
Site I of antigenic domain 2 (AD-2) on human cytomegalovirus glycoprotein B (gB) is poorly immunogenic in both man and mouse and knowledge about antibody repertoires reactive with this epitope is thus limited. Here we have characterized a phage display-derived repertoire of antibody fragments specific for this epitope in terms of antigen recognition, fine-specificity, and virus-neutralizing capacity. Our results show that the functional properties within a closely related repertoire may differ widely and that the effectiveness of the members of the repertoire to neutralize the virus is determined by the fine-specificity and kinetics of the interaction with the antigen. The half-life of the interaction between monomeric antibody fragments... (More)
Site I of antigenic domain 2 (AD-2) on human cytomegalovirus glycoprotein B (gB) is poorly immunogenic in both man and mouse and knowledge about antibody repertoires reactive with this epitope is thus limited. Here we have characterized a phage display-derived repertoire of antibody fragments specific for this epitope in terms of antigen recognition, fine-specificity, and virus-neutralizing capacity. Our results show that the functional properties within a closely related repertoire may differ widely and that the effectiveness of the members of the repertoire to neutralize the virus is determined by the fine-specificity and kinetics of the interaction with the antigen. The half-life of the interaction between monomeric antibody fragments and gB seems to be particularly critical for the neutralizing capacity. We also demonstrate that sequence variation within gB allows virus variants to escape at least a part of the AD-2-specific neutralizing antibody repertoire, apparently without preventing antibody binding to the epitope. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Virology
volume
305
issue
1
pages
201 - 209
publisher
Elsevier
external identifiers
  • wos:000180214200019
  • pmid:12504553
  • scopus:0037227411
ISSN
1096-0341
DOI
10.1006/viro.2002.1752
language
English
LU publication?
yes
id
5721d956-624a-4ea2-a341-e4f337d3f028 (old id 134333)
date added to LUP
2007-07-06 14:24:55
date last changed
2017-01-01 07:22:48
@article{5721d956-624a-4ea2-a341-e4f337d3f028,
  abstract     = {Site I of antigenic domain 2 (AD-2) on human cytomegalovirus glycoprotein B (gB) is poorly immunogenic in both man and mouse and knowledge about antibody repertoires reactive with this epitope is thus limited. Here we have characterized a phage display-derived repertoire of antibody fragments specific for this epitope in terms of antigen recognition, fine-specificity, and virus-neutralizing capacity. Our results show that the functional properties within a closely related repertoire may differ widely and that the effectiveness of the members of the repertoire to neutralize the virus is determined by the fine-specificity and kinetics of the interaction with the antigen. The half-life of the interaction between monomeric antibody fragments and gB seems to be particularly critical for the neutralizing capacity. We also demonstrate that sequence variation within gB allows virus variants to escape at least a part of the AD-2-specific neutralizing antibody repertoire, apparently without preventing antibody binding to the epitope.},
  author       = {Lantto, Johan and Fletcher, Jean M. and Ohlin, Mats},
  issn         = {1096-0341},
  language     = {eng},
  number       = {1},
  pages        = {201--209},
  publisher    = {Elsevier},
  series       = {Virology},
  title        = {Binding Characteristics Determine the Neutralizing Potential of Antibody Fragments Specific for Antigenic Domain 2 on Glycoprotein B of Human Cytomegalovirus},
  url          = {http://dx.doi.org/10.1006/viro.2002.1752},
  volume       = {305},
  year         = {2003},
}