Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8306007 | Biochimie Open | 2018 | 7 Pages |
Abstract
The recombinant fucolectin-related protein (FRP) of unknown function, encoded by the SP2159 gene of Streptococcus pneumoniae, was expressed in E. coli. In this study, its glycan-recognition epitopes and their binding potencies were examined by enzyme-linked lectinosorbent and inhibition assays. The results indicate that FRP reacted strongly with human blood group ABH and l-Fucα1â2-active glycotopes and in their polyvalent (super) forms. When expressed by mass relative potency, the binding affinities of FRP to poly-l-Fucα1âglycotopes were about 5.0 Ã 105 folds higher than that of the mono-l-Fucα1âglycotope form. This unique binding property of FRP can be used as a special tool to differentiate complex forms of l-Fucα1â2 and other forms of glycotopes.
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Biochemistry
Authors
Albert M. Wu, Tanuja Singh, Yung Liang Chen, Kimberly M. Anderson, Su Chen Li, Yu Teh Li,