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Glycosylation of mouse and human immune cells: insights emerging from N-glycomics analyses

Aristotelis Antonopoulos1, Simon J North, Stuart M Haslam

  • 1Division of Molecular Biosciences, Faculty of Natural Sciences, Imperial College London, London SW7 2AZ, UK. a.dell@imperial.ac.uk

Biochemical Society Transactions
|September 23, 2011
PubMed

Insights

Complex N-glycans on immune cells are crucial for cell communication. Structural analysis reveals insights into their role in health and diseases like congenital neutropenia.

Area of Science:

  • Immunology
  • Glycobiology
  • Structural Biology

Background:

  • N-glycans mediate crucial cell-cell communication in the immune system via interactions with glycan-binding proteins.
  • Understanding the structural nuances of N-glycans is essential for deciphering their functional roles in immunity.

Purpose of the Study:

  • To explore emerging themes in the structural analysis of complex-type N-linked glycans from human and murine immune cell lines.
  • To highlight the significance of terminal epitopes and multiply branched N-glycans.
  • To discuss the impact of glycosylation on human health, focusing on specific diseases.

Main Methods:

  • Utilized high-sensitivity MALDI-TOF MS (matrix-assisted laser desorption ionization-time-of-flight mass spectrometry) technology.
  • Performed structural analysis on complex-type N-linked glycans derived from human and murine immune cell lines.

Main Results:

  • Identified key structural features of N-glycans, including terminal epitopes and multiply branched structures.
  • Provided a detailed structural characterization of N-glycans from immune cells.
  • Established a link between specific glycosylation patterns and diseases.

Conclusions:

  • Structural analysis of N-glycans provides critical insights into immune cell communication.
  • Glycosylation patterns significantly influence human health and disease pathogenesis, exemplified by congenital neutropenia and glycogen storage disease.

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