Formaldehyde treatment of proteins enhances proteolytic degradation by the endo-lysosomal protease cathepsin S.

ABSTRACT: Enzymatic degradation of protein antigens by endo-lysosomal proteases in antigen-presenting cells is crucial for achieving cellular immunity. Structural changes caused by vaccine production process steps, such as formaldehyde inactivation, could affect the sensitivity of the antigen to lysosomal proteases. The aim of this study was to assess the effect of the formaldehyde detoxification process on the enzymatic proteolysis of antigens by studying model proteins. Bovine serum albumin, β-lactoglobulin A and cytochrome c were treated with various concentrations of isotopically labelled formaldehyde and glycine, and subjected to proteolytic digestion by cathepsin S, an important endo-lysosomal endoprotease. Degradation products were analysed by mass spectrometry and size exclusion chromatograp

SUBMITTER: Michiels TJM 

PROVIDER: S-EPMC7360561 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature