TY - JOUR
T1 - MAbTope
T2 - A Method for Improved Epitope Mapping
AU - Bourquard, Thomas
AU - Musnier, Astrid
AU - Tahir, Shifa
AU - Ayoub, Mohammed Akli
AU - Boulo, Thomas
AU - Gallay, Nathalie
AU - Bruneau, Gilles
AU - Reiter, Eric
AU - Crépieux, Pascale
AU - Poupon, Anne
N1 - Funding Information:
This work was supported by the French National Research Agency (ANR) under the program Investissements d’Avenir Grant Agreement (LabEx MabImprove: ANR-10-LABX-53), and by ANR (Contract ANR-2011–1619 01), ARTE2, MODUPHAC, MAbSilico, and ARD 2020 Biomédicament grants from Région Centre.
Publisher Copyright:
Copyright © 2018 by The American Association of Immunologists, Inc. All rights reserved
PY - 2018/11/15
Y1 - 2018/11/15
N2 - are very efficient drugs, 70 of them are already approved for medical use, over 500 are in clinical development, and many more are in preclinical development. One important step in the characterization and protection of a therapeutic Ab is the determination of its cognate epitope. The gold standard is the three-dimensional structure of the Ab/Ag complex by crystallography or nuclear magnetic resonance spectroscopy. However, it remains a tedious task, and its outcome is uncertain. We have developed MAbTope, a docking-based prediction method of the epitope associated with straightforward experimental validation procedures. We show that MAbTope predicts the correct epitope for each of 129 tested examples of Ab/Ag complexes of known structure. We further validated this method through the successful determination, and experimental validation (using human embryonic kidney cells 293), of the epitopes recognized by two therapeutic Abs targeting TNF-a: certolizumab and golimumab. The Journal of Immunology, 2018, 201: 3096-3105.
AB - are very efficient drugs, 70 of them are already approved for medical use, over 500 are in clinical development, and many more are in preclinical development. One important step in the characterization and protection of a therapeutic Ab is the determination of its cognate epitope. The gold standard is the three-dimensional structure of the Ab/Ag complex by crystallography or nuclear magnetic resonance spectroscopy. However, it remains a tedious task, and its outcome is uncertain. We have developed MAbTope, a docking-based prediction method of the epitope associated with straightforward experimental validation procedures. We show that MAbTope predicts the correct epitope for each of 129 tested examples of Ab/Ag complexes of known structure. We further validated this method through the successful determination, and experimental validation (using human embryonic kidney cells 293), of the epitopes recognized by two therapeutic Abs targeting TNF-a: certolizumab and golimumab. The Journal of Immunology, 2018, 201: 3096-3105.
UR - http://www.scopus.com/inward/record.url?scp=85056262103&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85056262103&partnerID=8YFLogxK
U2 - 10.4049/jimmunol.1701722
DO - 10.4049/jimmunol.1701722
M3 - Article
C2 - 30322966
AN - SCOPUS:85056262103
SN - 0022-1767
VL - 201
SP - 3096
EP - 3105
JO - Journal of Immunology
JF - Journal of Immunology
IS - 10
ER -