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Cross-reactivity

Cross-reactivity

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Engineering Murine Cross-Reactivity Into an Affibody to Human Death Receptor 5.

Tse-Han Kuo¹, Nagamani Vunnam², Jonathan N Sachs²

¹Department of Chemical Engineering and Materials Science, University of Minnesota - Twin Cities, Minneapolis, Minnesota, USA.

Biotechnology and Bioengineering

|May 6, 2026

Summary

Researchers engineered an affibody molecule to target death receptor 5 (DR5) in both humans and mice. This improved therapeutic candidate shows potential for treating metabolic dysfunction-associated steatohepatitis (MASH) and other liver diseases.

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Area of Science:

Protein engineering
Immunotherapy
Translational research

Background:

Death receptor 5 (DR5) is crucial in metabolic dysfunction-associated steatohepatitis (MASH), mediating hepatocyte apoptosis and inflammation.
Interspecies cross-reactive therapeutics targeting conserved epitopes are vital for translational research.

Purpose of the Study:

To engineer an affibody molecule for cross-reactivity to both human and murine DR5.
To enhance binding affinity to human DR5 and introduce binding to murine DR5.

Main Methods:

Rational library design guided by enrichment information and helix-walking mutagenesis.
Alternating binding selections between human and murine DR5.
Deep sequencing for paratope analysis.

Main Results:

Engineered affibody variants showed significantly improved binding to both human and murine DR5.
The dominant variant, ABYDR5-A, achieved 15 nM affinity for murine DR5 and 5.8 nM for human DR5.
ABYDR5-A demonstrated nanomolar IC50 values for antagonism of TRAIL-induced DR5 signaling in both species.

Conclusions:

The engineered affibody ABYDR5-A is a promising candidate for therapeutic development targeting DR5-mediated liver diseases like MASH.
Further studies including functional characterization and pharmacokinetic optimization are needed for preclinical and clinical advancement.