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Cell adhesion is  an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain,...
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Engineering a versatile tandem repeat-type alpha2-6sialic acid-binding lectin.

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Researchers engineered a novel lectin (SRC2) with high affinity and selectivity for alpha2,6-sialylated N-glycans. This tool shows promise for sialoglycomics and flow cytometry analysis due to its unique erythrocyte-binding properties.

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Area of Science:

  • Biochemistry
  • Glycobiology
  • Molecular Biology

Background:

  • Development of lectins for specific glycan recognition is crucial in glycobiology.
  • Monovalent lectins often exhibit low binding affinity, limiting their applications.
  • Existing alpha2,6-sialic acid-specific lectins can cause cell agglutination, complicating analyses.

Purpose of the Study:

  • To engineer a high-affinity, selective lectin for alpha2,6-sialylated N-glycans.
  • To develop a versatile tool for sialoglycomics and flow cytometry.
  • To overcome limitations of existing lectins, such as low affinity and cell agglutination.

Main Methods:

  • Engineering a tandem repeat construct (SRC2) from a galactose-specific lectin C-terminal domain.
  • Affinity and selectivity analysis of SRC2 for alpha2,6-sialylated N-glycans compared to Sambucus sieboldiana lectin (SSA).
  • Assessment of hemagglutinating and erythrocyte-binding activities of SRC2.

Main Results:

  • SRC2 demonstrated substantial affinity for alpha2,6-sialylated N-glycans (K(d) ~10(-6)M), comparable to SSA.
  • SRC2 exhibited higher selectivity for branched N-glycans than SSA.
  • SRC2 showed no hemagglutinating activity but strong erythrocyte-binding, unlike SSA.

Conclusions:

  • The engineered SRC2 lectin is a potent tool for sialoglycomics with high affinity and selectivity.
  • SRC2's unique erythrocyte-binding property without agglutination is advantageous for flow cytometry.
  • High productivity in bacteria and easy release of captured glycoproteins enhance SRC2's versatility.