RT info:eu-repo/semantics/article
T1 Clonal repertoire diversification of a neutralizing cytomegalovirus glycoprotein B-specific antibody results in variants with diverse anti-viral properties
A1 Barrios del Pino, Yvelise
A1 Knör, Susanne
A1 Lantto, Johan
A1 Mach, Michael
A1 Ohlin, Mats
K1 Antibody
K1 Cytomegalovirus
K1 Phagedisplay
K1 Repertoire
K1 Virus neutralization
AB Cytomegalovirus induces a chronic infection that in normal individuals is controlled by the immune system. In the case of humoral immunity, epitopes, in particular antigenic domain-1, in glycoprotein B have proven to be important for the induction of virus-neutralizing activity. Such antibodies can exert potent virus-neutralizing activity but can also block neutralizing antibodies from binding. Furthermore, these antibodies differ in their fine recognition of antigenic domain-1 as determined by epitope mapping. By using combinatorial library and phage display technologies we have now isolated a large array of clonally related antibody fragments to understand the origin of this diversity. This procedure allowed us to demonstrate that much of the diversity in functional activity (virus neutralization) and epitope recognition can arise from a single parental molecule through somatic mutation processes. We have thus demonstrated that the clonal diversification of a single antigen-specific clone can account for much of the diversity in antibody anti-viral activity. These findings have implications on the development of a gB-based subunit vaccine, as an effective vaccine preparation need not only to recruit appropriate clones into the immune response but also to evolve them properly so as to maintain an appropriate biological function. © 2006 Elsevier Ltd. All rights reserved.
SN 0161-5890
YR 2007
FD 2007
LK http://riull.ull.es/xmlui/handle/915/34891
UL http://riull.ull.es/xmlui/handle/915/34891
LA en
DS Repositorio institucional de la Universidad de La Laguna
RD 19-nov-2024