Engineering Antibodies track banner

The field of antibody and protein engineering is at an exciting point, with the pandemic bringing new attention to the discovery and development of antibody and other therapeutic approaches to treat SARS-CoV-2, while continuing to focus on engineering novel modalities, and strengthening the structure-function, affinity and maturation of existing antibody therapeutics. CHI’s 6th Annual Engineering Antibodies conference at PEGS Europe invites scientists to showcase their novel approaches to developing next-generation antibody and protein therapeutics for oncology, SARS-CoV-2 and beyond.

Wednesday, 3 November

07:15 Registration and Morning Coffee



Chairperson's Opening Remarks

Bryan Briney, PhD, Assistant Professor, Immunology & Microbial Science, Scripps Research Institute

Naturally Occurring Antibodies from the Repertoires of Resilient Individuals

Ralph Minter, PhD, Vice President, Research, Alchemab Therapeutics

At Alchemab, we are harnessing the power of the immune system to counter complex diseases. By mining the antibody repertoires of individuals who demonstrate exceptional resilience to disease we are able to pinpoint antibodies which are linked to improved outcomes. Selected antibodies are characterised by function and target specificity before entering preclinical disease models. We will show examples to illustrate the platform’s applicability across disease areas, including Infection, Oncology and Neurodegeneration.


Isolation of SARS-CoV-2 nAbs (Including Cross-Reactivity with Emerging Variants) Using Single Cell Genomics Techniques

Bryan Briney, PhD, Assistant Professor, Immunology & Microbial Science, Scripps Research Institute
Jonathan Didier, Field Application Specialist, Berkeley Lights, Inc.

This presentation will introduce Berkeley Lights’ Opto™ Plasma B Discovery 4.0 workflow that enables recovery of 1000s of hits by screening up to 100,000 plasma cells, down-selection of lead candidates by functional screening, and sequencing and re-expression of >1000 functionally-characterized antibodies all in 1 week. By maximizing the diversity of antibodies through direct functional profiling of plasma cells, the OPBD 4.0 workflow allows users to tackle even the most challenging targets.


10:00 Session Break and Transition into Plenary Keynote



Plenary Keynote Introduction

Janine Schuurman, PhD, Senior Vice President, Antibody Research & Technology, Research & Innovation, Genmab BV

New Modes of T Cell Recognition and Novel Broadly-Expressed T Cell Epitopes by Dissection of Cancer Immunotherapy Success

Andrew Sewell, PhD, Distinguished Research Professor and Wellcome Trust Senior Investigator, Division of Infection and Immunity, Cardiff University School of Medicine

We have developed a successful pipeline for discovering what so-called “orphan T cells” recognize and applied this to dissect what dominant persistent anti-cancer T cells recognize during successful immunotherapy. This work has uncovered a new, unanticipated, mode of T cell recognition. I will describe this new mode of recognition in atomic-level detail and describe why and how it might be linked to successful clearance of solid cancers.

10:45 PLENARY:

Live Q&A 

Panel Moderator:
Janine Schuurman, PhD, Senior Vice President, Antibody Research & Technology, Research & Innovation, Genmab BV
Andrew Sewell, PhD, Distinguished Research Professor and Wellcome Trust Senior Investigator, Division of Infection and Immunity, Cardiff University School of Medicine
10:55 Coffee Break in the Exhibit Hall with Poster Viewing



Chairperson's Remarks

Bryan Briney, PhD, Assistant Professor, Immunology & Microbial Science, Scripps Research Institute

SARS-CoV-2 Antibody Therapeutics: Rapid Supply of Potent and Virus Neutralizing Antibodies from Antibody Repertoire Biobanks of Convalescent Donors Using Advanced Droplet Microfluidics

Matthias Hillenbrand, PhD, Senior Scientist, Memo Therapeutics

Memo Therapeutics embarked on the race to develop an antibody-based medicine for COVID-19 in April 2020. Using our microfluidic single-cell-based RT-PCR and recombinant mammalian expression technology Dropzylla, we generated recombinant antibody repertoire biobanks from clinically selected convalescent COVID-19 donors. Screening of the repertoire libraries yielded a large portfolio of SARS-CoV-2-neutralizing antibodies against a multitude of possible variants of SARS-CoV-2 in less than one month. Our selected candidate, CoVAb36 showed picomolar neutralization of wt SARS-CoV-2 and good developability and yield in a fast track GMP production process.


The Temporal Dynamics of the Humoral Immune Response Following COVID-19 Recovery and Immunisation with mRNA Vaccine

Yariv Wine, PhD, Assistant Professor, The Shmunis School of Biomedicine and Cancer Research, Tel Aviv University, Israel

Here, we describe the longitudinal kinetics of the serological memory in COVID-19 recovered patients over the period of 14 months. The decay rate is associated with the robustness of the response and the decay was significantly slower compared to naïve vaccinees, suggesting that the serological memory following natural infection is more robust compared to vaccination. These data highlight the possible superiority of hybrid immunity.

  • ?NEW TALK - This Presentation Will be Given for the First Time
Erica Lovett, Research Scientist, AbCellera

As the pandemic continues, more transmissible SARS-CoV-2 variants that evade COVID-19 treatments have emerged. As part of its ongoing pandemic response, AbCellera discovered a highly potent monoclonal antibody, bebtelovimab (LY-CoV1404) from a convalescent COVID-19 patient sample that could present a long-term solution to the ongoing pandemic. Bebtelovimab targets a rarely-mutated epitope on the SARS-CoV-2 spike protein and potently neutralizes variants of concern, including the Delta variant.

13:10 Session Break
Moa Fransson, PhD, CEO, Genagon Therapeutics AB
Shelley Izquierdo, Senior Director, Antibody Discovery, OmniAb

We have characterized a novel multi-Tm protein target relevant for cancers with a high infiltration of macrophages, such as triple negative breast cancer.  Our proof-of-concept studies demonstrate that blocking target function results in reduced tumor growth or clearance.

13:50 Session Break



A Compact Vocabulary of Paratope-Epitope Interactions Enables Predictability of Antibody-Antigen Binding

Victor Greiff, PhD, Associate Professor, Immunology, University of Oslo

The predictability of antibody-antigen binding is a prerequisite for de novo antibody and (neo-)epitope design. In a dataset of antibody-antigen structures, we identified interaction motifs, which compose a structure-based vocabulary of paratope-epitope interactions. We show that this vocabulary enables the machine learnability of antibody-antigen binding on the paratope-epitope level. Our work leverages combined structure- and sequence-based learning to demonstrate that machine-learning-driven predictive paratope and epitope engineering is feasible.

  • NEW TALK - This Presentation Will be Given for the First Time

TNFR2 Agonism and Antagonism – The TNFR2 Paradigm

Denise L. Faustman, MD, PhD, Associate Professor & Director, Immunobiology Labs, Massachusetts General Hospital

Although antibody success in the clinic can often be achieved with blocking antibodies, it is more difficult to create antibodies that intracellularly signal in positive (agonistic) or negative (antagonistic) ways especially as it relates to the TNF superfamily of receptors. We focus on the creation of extracellular hexagonal networks with strategically binding antibodies to the cell surface with an emphasis on the TNFR2 receptor.

  • NEW DATA - This Presentation Contains New Data

Structures of Mouse and Human GITR-GITRL Complexes Reveal Unique TNFSF Interactions

Feng Wang, PhD, Associate Director, Recombinant Proteins, Bristol-Myers Squibb

GITR and GITR ligand play a role in immune cell signaling, activation, and survival. Here we present structures of human and mouse GITR bound to their cognate ligands. Human GITR–GITRL has potential to form a hexameric network, while murine complex forms a linear chain. Mutations at the receptor–receptor interface in human GITR reduce cell signaling with in vitro assays and minimize higher order membrane structures in cell imaging experiments.

  • ​NEW TALK - This Presentation Will be Given for the First Time
Volker Lang, PhD, Managing Director, AbCheck s.r.o.

Specific requirements have to be met for the discovery of antibodies with challenging Target Product Profiles (TPPs). AbCheck has developed a technology to efficiently meet these requirements for e.g. functional antibodies or antibodies against targets with high homology. Our novel, tailored microfluidics technology is based on high throughput functional sorting of immune plasma cell repertoires at single cell level.

16:45 Refreshment Break in the Exhibit Hall with Poster Viewing



mRNA-Based COVID-19 Vaccines: Structure, Formulation and Stability

Gideon Kersten, PhD, Professor, Vaccine Delivery, Division of Biotherapeutics, Leiden University

Recently introduced vaccines, based on lipid nanoparticles (LNPs) with encapsulated mRNA strands encoding the viral spike glycoprotein of SARS-CoV-2, have shown to be particularly effective in preventing COVID-19 infection. However, a drawback of the current mRNA-LNP COVID-19 vaccines is that they have to be stored at (ultra)low temperatures.  I will discuss proposed structures of mRNA-LNPs, factors that impact mRNA-LNP stability and strategies to optimize mRNA-LNP vaccine product stability.

  • ​NEW TALK - This Presentation Will be Given for the First Time

Rational Selection of Building Blocks for the Assembly of Bispecific Antibodies

Danyang Gong, PhD, Scientist, Amgen Inc.

Bispecific antibodies are often composed of multiple polypeptide chains, therefore the driving of correct quaternary assembly of these chains represents a major challenge to meet industrial scale productivity. Here we describe Chain Selectivity Assessment (CSA), a high-throughput method to rationally select parental mAbs to make bispecific antibodies. By deploying CSA, we have successfully identified mAbs that exhibit a native preference towards cognate chain pairing such that enables the production of classic Hetero-IgGs without additional engineering. Furthermore, CSA also identified rare LCs that permit positive binding of the non-cognate arm in the common LC Hetero-IgGs, also without engineering.


Design and Validation of a Novel Engineered, FcγRIIb-Selective Fc Platform for Therapeutic Antibody Development

Gavin Jones, MDE, BioPharm Molecular Discovery, Drug Design and Selection, Platform Technology and Science, GSK
Eric Escobar, PhD, Principal Scientist, Protein Engineer Lead, Exploratory Research Unit, Zymeworks

The inhibitory Fcγ receptor FcγRIIb has potential therapeutic applications in oncology and autoimmune disease, but design of FcγRIIb-selective antibodies has been hindered by high homology between FcγRIIb and the activating FcγRIIa receptor. We combined iterative computational design and high-throughput screening approaches with the Azymetric Fc heterodimer platform to identify asymmetric point mutations and extensions to a wildtype Fc loop structure that together drive selective Fc-FcγRIIb engagement. The resulting library of engineered Fc regions is FcγRIIb-selective, retains IgG-like developability profiles, and modulates in vitro and in vivo functional activity across multiple antibody systems, enabling the development of novel Fc-engineered therapeutics.

19:00 Close of Engineering Antibodies