Preprint Article Version 1 Preserved in Portico This version is not peer-reviewed

N-Glycomics of Human Erythrocytes

Version 1 : Received: 30 June 2021 / Approved: 2 July 2021 / Online: 2 July 2021 (15:48:47 CEST)

A peer-reviewed article of this Preprint also exists.

Bua, R.O.; Messina, A.; Sturiale, L.; Barone, R.; Garozzo, D.; Palmigiano, A. N-Glycomics of Human Erythrocytes. Int. J. Mol. Sci. 2021, 22, 8063. Bua, R.O.; Messina, A.; Sturiale, L.; Barone, R.; Garozzo, D.; Palmigiano, A. N-Glycomics of Human Erythrocytes. Int. J. Mol. Sci. 2021, 22, 8063.

Journal reference: Int. J. Mol. Sci. 2021, 22, 8063
DOI: 10.3390/ijms22158063

Abstract

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

Subject Areas

Red Blood Cells; N-glycosylation; MALDI-TOF; ABO(H) blood groups

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