Supporting data for the MS identification of distinct transferrin glycopeptide glycoforms and citrullinated peptides associated with inflammation or autoimmunity

Abstract

This data article presents the results of all the statistical analyses applied to the relative intensities of the detected 2D-DiGE protein spots for each of the 3 performed DiGE experiments. The data reveals specific subsets of protein spots with significant differences between WT and CD38-deficient mice with either Collagen-induced arthritis (CIA), or with chronic inflammation induced by CFA, or under steady-state conditions. This article also shows the MS data analyses that allowed the identification of the protein species which serve to discriminate the different experimental groups used in this study. Moreover, the article presents MS data on the citrullinated peptides linked to specific protein species that were generated in CIA+ or CFA-treated mice. Lastly, this data article provides MS data on the efficiency of the analyses of the transferrin (Tf) glycopeptide glycosylation pattern in spleen and serum from CIA+ mice and normal controls. The data supplied in this work is related to the research article entitled “identification of multiple transferrin species in spleen and serum from mice with collagen-induced arthritis which may reflect changes in transferrin glycosylation associated with disease activity: the role of CD38” [1]. All mass spectrometry data have been deposited to the ProteomeXchange Consortium via the PRIDE partner repository with identifiers PRIDE: PXD002644, PRIDE: PXD002643, PRIDE: PXD003183 and PRIDE: PXD003163.

Crystal structures of H-2Db in complex with the LCMV-derived peptides GP92 and GP392 explain pleiotropic effects of glycosylation on antigen presentation and immunogenicity

“…Instead, glycosylation and any following modification would result in the formation T-cell neo-epitopes [ 23 ]. Formation of glycosylation/de-glycosylation derived neo-epitopes has been reported in a large ensemble of diseases including ovarian carcinoma, melanoma, leukemia as well as autoimmune diseases such as rheumatoid arthritis [ 12 , 13 , 15 , 60 ].…”

“…g . advanced mass-spectrometry with high sensitivity [ 16 , 60 , 62 , 63 ] would allow the identification of disease-associated PTM neo-epitopes, and allow us to readdress previously published work in order to assess whether glycosylated versions of GP92 are actually presented or not on the surface of infected cells. Here we report the structural bases underlying how glycosylation of GP92 can clearly result in the formation of immunogenic neo-epitopes that may select for different T cell populations.…”