RT Journal Article
SR Electronic
T1 Antibody binding epitope Mapping (AbMap) of two hundred antibodies in a single run
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 739342
DO 10.1101/739342
A1 Huan Qi
A1 Mingliang Ma
A1 Chuansheng Hu
A1 Zhao-wei Xu
A1 Fan-lin Wu
A1 Nan Wang
A1 Dan-yun Lai
A1 Yang Li
A1 Shu-juan Guo
A1 Xiaodong Zhao
A1 Hua Li
A1 Sheng-ce Tao
YR 2019
UL http://biorxiv.org/content/early/2019/08/19/739342.abstract
AB Epitope mapping is essential for the understanding how an antibody works. Given millions of antibodies short of epitope information, there is an urgent need for high-throughput epitope mapping. Here we combined a commercial phage displayed random peptide library of 109 diversity with next generation sequencing to develop Antibody binding epitope Mapping (AbMap) technology. Over two hundred antibodies were analyzed in a single test and epitopes were determined for >50% of them. Strikingly, the antibodies were able to recognize different proteins from multiple species with similar epitopes. We successfully identified the epitopes of 14 anti-PD-1 antibodies, including Sintilimab (i.e., L128, A129 and P130), and confirmed that the binding epitopes of Nivolumab and Sintilimab are very close to the binding interface of PD-1 and PD-L1. The predicted conformational epitopes of Pembrolizumab and Nivolumab are consistent with their antibody-antigen co-crystal structures. AbMap is the first technology enables high-throughput epitope mapping.HighlightsThe first technology enables epitope mapping of two hundred antibodies in a single runLinear epitope was determined for >50% of the antibodiesDistinct epitopes of 14 anti-PD-1 antibodies, including Sintilimab, were determinedThe predicted conformational epitopes of Pembrolizumab and Nivolumab are consistent with the known antibody-antigen co-crystal structures