IVIS 2025
Conference dates: August 11-14, 2025
Stand: 4
Location: Vienna, Austria
Poster session
Poster Title: Accelerate Kinetic Screening and Epitope Characterization of Antibody Libraries with High Throughput SPR
Location:
Presenter: Andrew Goodhead, PhD, Carterra
Abstract: Throughput, speed, resolution, and sample consumption are typically key limiting factors for performing detailed kinetic and epitope characterization of monoclonal antibody (mAb) libraries destined for use as therapeutics. In addition, mAb immune responses can be used to survey the epitope landscape of pathogens and inform the design of more effective immunogens for vaccines. Here, we demonstrate three core applications of high throughput SPR: capture kinetics, epitope binning, and epitope mapping, that together provide a comprehensive characterization of your mAb library with minimal sample consumption, enabling more confident decisions to be made earlier in the research process and obviating the need for preliminary ELISA screening. We show that high throughput SPR can facilitate the generation of high-quality kinetic data from 384 mAbs in parallel, using < 1 μg per mAb and only 2 μg of antigen. Epitope binning in a 384-mAb array format allows for a rapid assessment of the depth and breadth of your library’s epitope diversity, providing exquisite resolution between near-identical clones, using < 5 μg per mAb and about 100 μg antigen. Finally, a large panel of mAbs can be mapped against a 384-peptide library, if their epitopes can be (partially) recapitulated on peptides, using 1 μg per mAb and <0.1 μg per peptide.
Speaking session
Title: A cross-reactive neutralising epitope of foot-and-mouth disease virus (FMDV)
Presenter: Abigail Hay, PhD, The Pirbright Institute
Date: Wednesday, August 13
Time: 14:00
Location: Session 2.3a – Vaccine Development
Abstract: Foot-and-mouth disease virus (FMDV) causes a devastating disease in livestock and poses a continuous threat to food security worldwide. FMDV protection is primarily mediated by neutralising antibodies but controlling the disease is challenging due to short-term protection elicited by current vaccines and limited cross-serotype protection. To investigate cross-serotype reactive/neutralising antibody epitopes, we sequentially vaccinated cattle with FMDV antigens from four serotypes (O, A, Asia 1, and SAT2). Isolation of antigen-specific B-cells and production of selected antibodies yielded three antibodies capable of neutralising 23 strains across four of the seven FMDV serotypes (O, A, Asia 1, and C). An additional 41 strains from the same four serotypes showed reactivity by ELISA.
Western Blot analysis revealed that the cross-serotype specific epitope was predominantly a linear epitope. Peptide scanning by ELISA and surface plasmon resonance mapped the epitope to a region of VP1 with previously unknown immunogenicity. Crystallography and Cryo-EM confirmed the linear epitope and identified its location within a dynamic pocket of the FMDV capsid. Sequence analysis revealed that the key residues involved in the epitope-paratope interaction are conserved in some SAT strains that are not neutralised. Combined with structural data, this suggests that epitope accessibility may be influencing antibody binding and serotype specificity. Ongoing analysis aims to further understand the mechanisms of serotype specificity and neutralisation to further inform development of improved broad-spectrum vaccines.