N-Glycomics of Human Erythrocytes

Glycosylation is a complex post-translational modification that conveys functional diversity to glycoconjugates. Cell surface glycosylation mediates several biological activities such as induction of the intracellular signaling pathway and pathogen recognition. Red blood cell (RBC) membrane N-glycans determine type influence lifespan. Although proteomic studies have been carried out, RBC proteins has not systematically investigated. This work aims at exploring human N-glycome by high-sensitivity MALDI-MS techniques outline fingerprint N-glycans. To this purpose, MALDI-TOF spectra healthy subjects harboring different groups were acquired. Results showed predominant occurrence neutral sialylated with bisected N-acetylglucosamine core- and/or antennary fucosylation. In higher mass region, these species presented multiple N-acetyllactosamine repeating units. Amongst detected glycoforms, presence glycans bearing ABO(H) antigens allowed us define distinctive spectrum for each group. For first time, advanced glycomic applied comprehensive exploration N-glycosylation, providing new tool early detection distinct glycome changes associated disease conditions well understanding molecular recognition pathogens.