Murine
zymosan-induced
peritonitis is a widely used model for studying the molecular and cellular events responsible for the initiation, persistence and/or resolution of
inflammation. Among these events, it is becoming increasingly evident that changes in glycosylation of
proteins, especially in the plasma and at the site of
inflammation, play an important role in the inflammatory response. Using matrix-assisted
laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS)-based glycosylation profiling, we investigated the qualitative and quantitative effect of
zymosan-induced
peritonitis on N-glycosylation in mouse plasma and peritoneal fluid. Our results show that both N-glycomes exhibit highly similar glycosylation patterns, consisting mainly of diantennary and triantennary complex type N-
glycans with high levels (>95 %) of galactosylation and sialylation (mostly NeuGc) and a medium degree of core fucosylation (30 %). Moreover, MS/MS structural analysis, assisted by linkage-specific derivatization of
sialic acids, revealed the presence of O-acetylated
sialic acids as well as disialylated antennae ("branching sialylation") characterized by the presence of α2-6-linked NeuGc on the GlcNAc of the NeuGcα2-3-Galβ1-3-GlcNAc terminal motif. A significant decrease of (core) fucosylation together with an increase of both α2-3-linked NeuGc and "branching sialylation" were observed in N-glycomes of mice challenged with
zymosan, but not in control mice injected with PBS. Importantly, substantial changes in glycosylation were already observed 12 h after induction of
peritonitis, thereby demonstrating an unexpected velocity of the biological mechanisms involved.