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Novel antibody specificities targeting glycoprotein B of cytomegalovirus identified by molecular library technology

Carlsson, Fredrika LU ; Persson, Jonas LU ; Moreau, Emmanuel ; Côté, Marie-Hélène ; Lamarre, Alain and Ohlin, Mats LU orcid (2009) In New Biotechnology 25(6). p.429-436
Abstract
Antibodies provide some protection against cytomegalovirus-mediated disease. All aspects of antibody recognition of important viral antigens are however not fully appreciated. Glycoprotein B (gB), a key protein in the viral membrane, participates in viral infection and it is a component of prototype vaccines. By using combinatorial antibody library and selection technology, novel antibody specificities targeting gB have now been isolated. We define a monoclonal antibody fragment able to recognize site I of antigenic domain (AD) 2, a poorly immunogenic epitope targeted by potent virus-neutralizing antibodies, in a way that is different from the binding of antibodies induced by infection but similar to those induced by vaccination. We also... (More)
Antibodies provide some protection against cytomegalovirus-mediated disease. All aspects of antibody recognition of important viral antigens are however not fully appreciated. Glycoprotein B (gB), a key protein in the viral membrane, participates in viral infection and it is a component of prototype vaccines. By using combinatorial antibody library and selection technology, novel antibody specificities targeting gB have now been isolated. We define a monoclonal antibody fragment able to recognize site I of antigenic domain (AD) 2, a poorly immunogenic epitope targeted by potent virus-neutralizing antibodies, in a way that is different from the binding of antibodies induced by infection but similar to those induced by vaccination. We also describe the existence of a novel epitope overlapping site I of AD-2 and AD-1, the immunodominant epitope of gB. These specificities, derived by molecular engineering, will be useful for the future assessment of humoral immune responses against this opportunistic viral infection. (Less)
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author
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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
New Biotechnology
volume
25
issue
6
pages
429 - 436
publisher
Elsevier
external identifiers
  • wos:000270772100011
  • scopus:70449532221
  • pmid:19464399
ISSN
1876-4347
DOI
10.1016/j.nbt.2009.05.003
language
English
LU publication?
yes
id
76b368e2-927f-443c-b936-30e655fc3203 (old id 1394515)
date added to LUP
2016-04-01 12:03:42
date last changed
2022-01-26 22:13:00
@article{76b368e2-927f-443c-b936-30e655fc3203,
  abstract     = {{Antibodies provide some protection against cytomegalovirus-mediated disease. All aspects of antibody recognition of important viral antigens are however not fully appreciated. Glycoprotein B (gB), a key protein in the viral membrane, participates in viral infection and it is a component of prototype vaccines. By using combinatorial antibody library and selection technology, novel antibody specificities targeting gB have now been isolated. We define a monoclonal antibody fragment able to recognize site I of antigenic domain (AD) 2, a poorly immunogenic epitope targeted by potent virus-neutralizing antibodies, in a way that is different from the binding of antibodies induced by infection but similar to those induced by vaccination. We also describe the existence of a novel epitope overlapping site I of AD-2 and AD-1, the immunodominant epitope of gB. These specificities, derived by molecular engineering, will be useful for the future assessment of humoral immune responses against this opportunistic viral infection.}},
  author       = {{Carlsson, Fredrika and Persson, Jonas and Moreau, Emmanuel and Côté, Marie-Hélène and Lamarre, Alain and Ohlin, Mats}},
  issn         = {{1876-4347}},
  language     = {{eng}},
  number       = {{6}},
  pages        = {{429--436}},
  publisher    = {{Elsevier}},
  series       = {{New Biotechnology}},
  title        = {{Novel antibody specificities targeting glycoprotein B of cytomegalovirus identified by molecular library technology}},
  url          = {{http://dx.doi.org/10.1016/j.nbt.2009.05.003}},
  doi          = {{10.1016/j.nbt.2009.05.003}},
  volume       = {{25}},
  year         = {{2009}},
}