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Affinity and Epitope Profiling of Mouse Anti-CD40 Monoclonal Antibodies

Malmborg Hager, Ann-Christin LU ; Ellmark, Peter LU ; Borrebaeck, Carl LU and Furebring, Christina LU (2003) In Scandinavian Journal of Immunology 57(6). p.517-524
Abstract
The CD40-CD40L interaction plays a critical role in both humoral and cellular immune responses and interfering antibodies have been suggested as an effective approach for the treatment of lymphomas and autoimmune diseases. In this study we have profiled a panel of mouse antihuman CD40 monoclonal antibodies (MoAbs), regarding their CD40 binding affinity and epitope-specificity relative to the CD40L binding in relation to their cellular activating potential. Despite a rather similar domain-recognition profile, the MoAbs blocked the CD40L binding to a varying degree, with MoAb 5C3 being the poorest inhibitor. There was no correlation between affinity and cellular activation potential. In contrast, a correlation between the ability to block... (More)
The CD40-CD40L interaction plays a critical role in both humoral and cellular immune responses and interfering antibodies have been suggested as an effective approach for the treatment of lymphomas and autoimmune diseases. In this study we have profiled a panel of mouse antihuman CD40 monoclonal antibodies (MoAbs), regarding their CD40 binding affinity and epitope-specificity relative to the CD40L binding in relation to their cellular activating potential. Despite a rather similar domain-recognition profile, the MoAbs blocked the CD40L binding to a varying degree, with MoAb 5C3 being the poorest inhibitor. There was no correlation between affinity and cellular activation potential. In contrast, a correlation between the ability to block CD40L-binding and activation potential could be seen. We believe that this analysis of several mouse anti-CD40 antibodies can be used to develop strategies for producing new human anti-CD40 antibodies that can more effectively induce or block B-cell proliferation. (Less)
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author
; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Scandinavian Journal of Immunology
volume
57
issue
6
pages
517 - 524
publisher
Wiley-Blackwell
external identifiers
  • wos:000183367900003
  • pmid:12791089
  • scopus:0038040565
ISSN
1365-3083
DOI
10.1046/j.1365-3083.2003.01271.x
language
English
LU publication?
yes
id
4c6c4f5d-06e0-43e8-96d6-6944b4c5c749 (old id 134310)
date added to LUP
2016-04-01 17:13:36
date last changed
2022-01-29 01:17:06
@article{4c6c4f5d-06e0-43e8-96d6-6944b4c5c749,
  abstract     = {{The CD40-CD40L interaction plays a critical role in both humoral and cellular immune responses and interfering antibodies have been suggested as an effective approach for the treatment of lymphomas and autoimmune diseases. In this study we have profiled a panel of mouse antihuman CD40 monoclonal antibodies (MoAbs), regarding their CD40 binding affinity and epitope-specificity relative to the CD40L binding in relation to their cellular activating potential. Despite a rather similar domain-recognition profile, the MoAbs blocked the CD40L binding to a varying degree, with MoAb 5C3 being the poorest inhibitor. There was no correlation between affinity and cellular activation potential. In contrast, a correlation between the ability to block CD40L-binding and activation potential could be seen. We believe that this analysis of several mouse anti-CD40 antibodies can be used to develop strategies for producing new human anti-CD40 antibodies that can more effectively induce or block B-cell proliferation.}},
  author       = {{Malmborg Hager, Ann-Christin and Ellmark, Peter and Borrebaeck, Carl and Furebring, Christina}},
  issn         = {{1365-3083}},
  language     = {{eng}},
  number       = {{6}},
  pages        = {{517--524}},
  publisher    = {{Wiley-Blackwell}},
  series       = {{Scandinavian Journal of Immunology}},
  title        = {{Affinity and Epitope Profiling of Mouse Anti-CD40 Monoclonal Antibodies}},
  url          = {{https://lup.lub.lu.se/search/files/4913606/624423.pdf}},
  doi          = {{10.1046/j.1365-3083.2003.01271.x}},
  volume       = {{57}},
  year         = {{2003}},
}