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A Human Lectin Microarray for Sperm Surface Glycosylation Analysis.

Yangyang Sun1, Li Cheng2, Yihua Gu3

  • 1From the ‡Shanghai Center for Systems Biomedicine, Key Laboratory of Systems Biomedicine (Ministry of Education), Shanghai Jiao Tong University, Shanghai 200240, China; ¶State Key Laboratory of Oncogenes and Related Genes, Shanghai Jiao Tong University, Shanghai 200240, China; §§Department of Bioengineering, School of Marine Science and Technology, Harbin Institute of Technology at Weihai, Weihai 264209, China.

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Summary
This summary is machine-generated.

This study introduces the first human lectin microarray for analyzing human glycosylation. The new tool, featuring 60 human lectins, successfully probed human sperm and revealed key protein interactions, enhancing sperm function.

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Area of Science:

  • Glycobiology and Post-Translational Modifications
  • Proteomics and Protein-Carbohydrate Interactions
  • Biotechnology and Array-Based Assays

Background:

  • Glycosylation is a critical protein post-translational modification, essential for numerous biological functions.
  • Existing lectin microarrays predominantly use plant lectins, limiting their effectiveness for complex human glycan analysis.
  • There is a significant demand for advanced technologies to study human glycosylation patterns.

Purpose of the Study:

  • To construct and validate the first human lectin microarray for comprehensive human glycosylation studies.
  • To identify specific human lectin-glycan interactions relevant to human biology.
  • To explore the functional implications of these interactions, particularly in human sperm.

Main Methods:

  • Development of a microarray featuring 60 purified human lectin and lectin-like proteins expressed in yeast.
  • Probing the human lectin microarray with human sperm samples to identify binding specificities.
  • Validation of observed bindings using flow cytometry, fluorescence immunostaining, mass spectrometry, and functional assays.

Main Results:

  • The human lectin microarray demonstrated binding to human glycans, with notable interactions observed for galectin-1, galectin-7, galectin-8, N-acetylgalactosamine-6-O-sulfotransferase (GalNAc-T6), and ER-Golgi intermediate compartment 53 kDa protein (ERGIC-53/LMAN1) with human sperm.
  • Mass spectrometry identified heat shock protein 90 (HSP90) as a binding partner for galectin-1.
  • Galectin-8 binding was shown to significantly enhance the acrosome reaction in human sperm.

Conclusions:

  • The developed human lectin microarray is a valuable tool for investigating human glycosylation and protein-glycan interactions.
  • This platform enables the discovery of novel lectin-glycan associations and their functional roles in human cells and tissues.
  • The human lectin microarray is anticipated to advance human and mammalian glycobiology research.