Proteome integral solubility alteration assay for monitoring antibody-antigen cell interactions

2025 · doi:10.1101/2025.09.04.673944
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Abstract

The Proteome Integral Solubility Alteration (PISA) assay is commonly used to identify and characterize interactions between small molecules and the cellular proteome. In this study, a modified PISA approach identified tumor necrosis factor alpha (TNFα) as the antigen of the monoclonal antibody infliximab in activated monocytes - uniquely among ∼8,000 cellular proteins. These results highlight the potential of PISA-based analysis not only for monitoring antibody-antigen interactions in therapeutic development, but also for identifying new antigens and characterizing the initial effector functions of antibodies within complex proteome environments. Teaser Modified PISA pinpointed TNF-α as Infliximab’s antigen among 8000 proteins, highlighting broad potential for therapeutic antigen studies.
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Abstract The Proteome Integral Solubility Alteration (PISA) assay is commonly used to identify and characterize interactions between small molecules and the cellular proteome. In this study, a modified PISA approach identified tumor necrosis factor alpha (TNFα) as the antigen of the monoclonal antibody infliximab in activated monocytes - uniquely among ∼8,000 cellular proteins. These results highlight the potential of PISA-based analysis not only for monitoring antibody-antigen interactions in therapeutic development, but also for identifying new antigens and characterizing the initial effector functions of antibodies within complex proteome environments. Teaser Modified PISA pinpointed TNF-α as Infliximab’s antigen among 8000 proteins, highlighting broad potential for therapeutic antigen studies. Competing Interest Statement The authors have declared no competing interest.

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