What is it about?
Chaperone proteins are known to bind to aggregated proteins. This paper examines the role of a particular chaperone and shows that it can influence the immune response to aggregated protein.
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Why is it important?
Biological medicines, or biologics, are widely used to treat inflammatory conditions and other diseases. They are monoclonal antibodies and are designed to target or block a specific protein or receptor. Some patients develop immunological responses to these antibodies, inhibiting their efficacy. Such responses could be triggered by the presence of aggregates of the biologic in the preparation: aggregates can form naturally on storage, and constitute disordered assemblies or ‘clumps’. Here, we show that a chaperone protein, which is a common class of impurities in preparations of biologics, can adhere to aggregates and promote specific antibody responses. This observation points to another mechanism for stimulation of immune responses to biologics.
Perspectives
We have followed up this paper with a further publication, which also shows this effect for aggregated antibodies (doi.org/10.1007/s11095-019-2586-7). Previous work on immunological responses to trace impurities within preparations of biologics has focused on individual proteins as antigens. Here we show that the role of chaperones as adjuvants also needs to be considered.
Jeremy Derrick
University of Manchester
Read the Original
This page is a summary of: Influence of Escherichia coli
chaperone DnaK on protein immunogenicity, Immunology, December 2016, Wiley,
DOI: 10.1111/imm.12689.
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