Tamir Ding
Structural biology of antibody recognition of carbohydrate epitopes and potential uses for targeted cancer immunotherapies
Ding, Tamir; Spendlove, Ian; Durrant, Lindy G.; Scott, Andrew M.; Yuriev, Elizabeth; Ramsland, Paul A.
Authors
Dr IAN SPENDLOVE IAN.SPENDLOVE@NOTTINGHAM.AC.UK
ASSOCIATE PROFESSOR
Lindy G. Durrant
Andrew M. Scott
Elizabeth Yuriev
Paul A. Ramsland
Abstract
Monoclonal antibodies represent the most successful class of biopharmaceuticals for the treatment of cancer. Mechanisms of action of therapeutic antibodies are very diverse and reflect their ability to engage in antibody-dependent effector mechanisms, internalize to deliver cytotoxic payloads, and display direct effects on cells by lysis or by modulating the biological pathways of their target antigens. Importantly, one of the universal changes in cancer is glycosylation and carbohydrate-binding antibodies can be produced to selectively recognize tumor cells over normal tissues. A promising group of cell surface antibody targets consists of carbohydrates presented as glycolipids or glycoproteins. In this review, we outline the basic principles of antibody-based targeting of carbohydrate antigens in cancer. We also present a detailed structural view of antibody recognition and the conformational properties of a series of related tissue-blood group (Lewis) carbohydrates that are being pursued as potential targets of cancer immunotherapy.
Citation
Ding, T., Spendlove, I., Durrant, L. G., Scott, A. M., Yuriev, E., & Ramsland, P. A. (2015). Structural biology of antibody recognition of carbohydrate epitopes and potential uses for targeted cancer immunotherapies. Molecular Immunology, 67(2, Pt. A), 75-88. https://doi.org/10.1016/j.molimm.2015.02.028
Journal Article Type | Article |
---|---|
Acceptance Date | Feb 19, 2015 |
Online Publication Date | Mar 7, 2015 |
Publication Date | Oct 31, 2015 |
Deposit Date | Jun 7, 2018 |
Electronic ISSN | 1872-9142 |
Publisher | Elsevier |
Peer Reviewed | Peer Reviewed |
Volume | 67 |
Issue | 2, Pt. A |
Pages | 75-88 |
DOI | https://doi.org/10.1016/j.molimm.2015.02.028 |
Public URL | https://nottingham-repository.worktribe.com/output/1112439 |
Publisher URL | https://www.sciencedirect.com/science/article/pii/S0161589015000772?via%3Dihub |
PMID | 25757815 |
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