title: Streptavidin contains an RYD sequence which mimics the RGD receptor domain of fibronectin.
abstract: 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.
authors.affiliation: Department of Biophysics, Weizmann Institute of Science, Rehovot, Israel.
authors.forename: R
authors.initials: R
authors.lastname: Alon
authors.forename: E A
authors.initials: EA
authors.lastname: Bayer
authors.forename: M
authors.initials: M
authors.lastname: Wilchek
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001426:Bacterial Proteins / Q000032:analysis / Q000378:metabolism*; D001665:Binding Sites; D002460:Cell Line; D002462:Cell Membrane / Q000378:metabolism*; D006224:Cricetinae; D005353:Fibronectins / Q000032:analysis / Q000378:metabolism*; D008969:Molecular Sequence Data; D019809:Streptavidin
chemical_list: D001426:Bacterial Proteins; D005353:Fibronectins; D019809:Streptavidin