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A humanized monovalent CD3 antibody which can activate homologous complement.

E G Routledge¹, I Lloyd, S D Gorman

¹Department of Pathology, Cambridge University.

European Journal of Immunology

|November 1, 1991

Summary

Researchers humanized a rat antibody targeting T cells to reduce immune responses and enhance therapy. A novel monovalent form effectively lysed T cells, offering potential for treating organ rejection, autoimmunity, and lymphoma.

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Area of Science:

Immunology
Biotechnology

Background:

The rat monoclonal antibody (mAb) YTH12.5 targets the CD3 antigen complex on human T cells.
Improving antibody efficacy and reducing immunogenicity are crucial for human therapy.

Purpose of the Study:

To humanize the YTH12.5 antibody for reduced immunogenicity.
To enhance effector function and create a monovalent form for improved therapeutic potential.

Main Methods:

Humanization of the YTH12.5 antibody using framework grafting.
Sequence analysis of the V lambda gene identified it as a potentially new V lambda gene family.
Creation of a monovalent antibody by introducing a truncated human IgG1 heavy chain gene.
Comparison of monovalent and bivalent humanized mAbs in complement-mediated cell lysis assays.

Main Results:

Successful humanization of the YTH12.5 lambda light chain, representing a novel V lambda gene family.
The monovalent humanized CD3 mAb mediated lysis of human T cell blasts.
The bivalent form of the humanized mAb did not induce lysis in the same assay.

Conclusions:

The humanized, complement-fixing CD3 mAb shows promise for therapeutic applications.
Potential uses include managing organ rejection, autoimmunity, and treating T cell lymphoma.