Paper of the Month: July Edition
Summary:
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.
Citation:
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.
Digital Object Identifier:
doi.org/10.1038/s41598-020-68248-z