Streptavidin contains an RYD sequence which mimics the RGD receptor domain of fibronectin

Biochem Biophys Res Commun. 1990 Aug 16;170(3):1236-41. doi: 10.1016/0006-291x(90)90526-s.


Streptavidin binds at low levels and high affinity to cell surfaces, the cause of which can be traced to the occurrence of a sequence containing RYD (Arg-Tyr-Asp) in the protein molecule. This binding is enhanced in the presence of biotin. Cell-bound streptavidin can be displaced by fibronectin, as well as by RGD- and RYD-containing peptides. In addition, streptavidin can displace fibronectin from cell surfaces. The RYD sequence of streptavidin thus mimics RGD (Arg-Gly-Asp), the universal recognition domain present in fibronectin and other adhesion-related molecules. The observed adhesion to cells has no relevance to biotin-binding since the RYD sequence is not part of the biotin-binding site of streptavidin. Since the use of streptavidin in avidin-biotin technology is based on its biotin-binding properties, researchers are hereby warned against its indiscriminate use in histochemical and cytochemical studies.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Bacterial Proteins / analysis
  • Bacterial Proteins / metabolism*
  • Binding Sites
  • Cell Line
  • Cell Membrane / metabolism*
  • Cricetinae
  • Fibronectins / analysis
  • Fibronectins / metabolism*
  • Molecular Sequence Data
  • Streptavidin


  • Bacterial Proteins
  • Fibronectins
  • Streptavidin