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Nadezhda V Shilova1,2, Svetlana M Polyakova3, Alexey Yu Nokel3,2

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(Strept)avidins, commonly used in assays, also bind to glycans like blood group antigens. This non-specific glycan binding, requiring polyvalence, can cause errors in carbohydrate analysis and requires careful control of (strept)avidin concentrations.

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Area of Science:

  • Biochemistry
  • Immunology
  • Glycobiology

Background:

  • (Strept)avidins are widely employed reagents in immunological assays and histochemistry for detecting biotinylated molecules.
  • Their primary function relies on high-affinity binding to biotin.

Purpose of the Study:

  • To investigate potential non-specific binding interactions of (strept)avidins beyond biotin.
  • To identify the nature of these interactions and their implications in biological sample analysis.

Main Methods:

  • Utilized fluorescently labeled and conjugated (strept)avidins.
  • Tested binding against various glycans, including mammalian glycoprotein and glycolipid fragments (e.g., ABO blood group antigens, oligolactosamines, 6-O-sulfated oligosaccharides).
  • Assessed inhibition of glycan binding using monomeric and polymeric glycan conjugates at varying concentrations.

Main Results:

  • Demonstrated that (strept)avidins bind to specific glycans, including ABO blood group antigens and sulfated oligosaccharides, in addition to biotin.
  • This glycan-binding activity is polyvalent-dependent, being inhibited by polymeric glycan conjugates but not monomeric ones at micromolar concentrations.
  • The findings highlight a potential source of artifact in analyses involving complex carbohydrate structures.

Conclusions:

  • The non-specific binding of (strept)avidins to cell surface glycans can interfere with immunological assays and histochemistry.
  • Researchers should be mindful of this interaction, especially in samples rich in glycoproteins and glycolipids.
  • Minimizing (strept)avidin excess in analytical systems is crucial to prevent erroneous results when analyzing carbohydrate-containing samples.