Paper of the Month: July Edition
Antigen detoxification is an important process in the production of vaccine products and is achieved, for example, by treatment with formaldehyde. This study aimed at elucidating the effect of such a treatment on the sensitivity of antigens towards the enzymatic degradation by endo-lysosomal proteases. To this end, conformational changes of cytochrome c, amongst other model proteins, were monitored using a Chirascan CD spectrometer. It was found that formaldehyde or formaldehyde/glycine treatment caused structural changes that are thought to make the altered protein conformation more accessible to proteases such as cathepsin S and, thus, enhance proteolytic degradation. This is expected to affect immunogenicity and the efficacy of vaccine products that contain antigens that have been inactivated by formaldehyde treatment.
Michiels, Meiring, Jiskoot, Kersten, and Metz. 2020. “Formaldehyde Treatment of Proteins Enhances Proteolytic Degradation by the Endo-Lysosomal Protease Cathepsin S.” Scientific Reports 10: 11535.
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