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Scalable High Throughput Selection From Phage-displayed Synthetic Antibody Libraries

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Soluble Antigen Array Displaying Proinsulin(F25D) Selectively Targets Anti-insulin B Cells without Hormonal Effects.

Grant M Downes¹, Kyle D Apley², Gang Hu³

¹Bioengineering Graduate Program, University of Kansas, Lawrence, Kansas 66045, United States.

Molecular Pharmaceutics

|January 23, 2026

Summary

A novel soluble antigen array (SAgA) targeting mutated proinsulin (M-PI(F25D)) shows promise for Type 1 diabetes (T1D) antigen-specific immunotherapy (ASIT). This approach avoids glycemic effects while specifically targeting autoreactive B cells and anti-insulin antibodies.

Keywords:

Type 1 diabetes anti-insulin B cells antigen-specific immunotherapy hyaluronic acid−protein conjugates nonhormonal proinsulin soluble antigen arrays

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The Use of Fluorescent Target Arrays for Assessment of T Cell Responses In vivo

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Published on: June 19, 2014

Area of Science:

Immunology
Endocrinology
Biotechnology

Background:

Type 1 diabetes (T1D) pathogenesis involves antigen presentation to autoreactive T cells by dendritic cells and B lymphocytes in pancreatic islets.
Current immunosuppressive therapies like rituximab and teplizumab carry risks of infection due to B or T cell depletion.
Antigen-specific immunotherapy (ASIT) offers a targeted approach to suppress or delete autoreactive cells.

Purpose of the Study:

To develop a novel soluble antigen array (SAgA) platform for T1D intervention.
To create a mutated proinsulin antigen (proinsulin(F25D)) conjugated to a hyaluronic acid (HA) backbone (SAgA_M-PI(F25D)) that retains disease-targeting capabilities without glycemic activity.
To evaluate the specificity and efficacy of SAgA_M-PI(F25D) in targeting autoreactive B cells and anti-insulin antibodies.

Main Methods:

Conjugation of mutated proinsulin (proinsulin(F25D)) to a hyaluronic acid (HA) backbone to form SAgA_M-PI(F25D).
Assessment of insulin receptor-β activity and in vivo glycemic effects.
Binding assays with a disease-relevant monoclonal anti-insulin antibody and murine transgenic (Tg125) B cells specific for human insulin.

Main Results:

SAgA_M-PI(F25D) demonstrated a pronounced reduction in insulin receptor-β activity.
The developed SAgA lacked significant glycemic activity in vivo.
SAgA_M-PI(F25D) exhibited low nanomolar binding affinity for a disease-relevant monoclonal anti-insulin antibody and bound specifically to murine transgenic (Tg125) B cells.

Conclusions:

The mutated proinsulin SAgA (SAgA_M-PI(F25D)) effectively avoids glycemic effects while maintaining specificity for anti-insulin antibodies and insulin-binding B cells.
This SAgA platform represents a promising candidate for antigen-specific immunotherapy in Type 1 diabetes.
The targeted approach of SAgA_M-PI(F25D) offers a potential alternative to broader immunosuppressive therapies for T1D.