Glycan binding profile of a fucolectin-related protein (FRP) encoded by the SP2159 gene of Streptococcus pneumoniae

Albert M Wu; Tanuja Singh; Yung Liang Chen; Kimberly M Anderson; Su Chen Li; Yu Teh Li

doi:10.1016/j.biopen.2017.12.002

Glycan binding profile of a fucolectin-related protein (FRP) encoded by the SP2159 gene of Streptococcus pneumoniae

Biochim Open. 2017 Dec 23:6:17-23. doi: 10.1016/j.biopen.2017.12.002. eCollection 2018 Jun.

Authors

Albert M Wu¹, Tanuja Singh¹, Yung Liang Chen², Kimberly M Anderson³, Su Chen Li³, Yu Teh Li³

Affiliations

¹ Glyco-Immunochemistry Research Laboratory, Institute of Biomedical Sciences, College of Medicine, Chang-Gung University, Kwei-san, Tao-yuan, 333, Taiwan.
² Graduate Institute of Medical Laboratory Science and Biotechnology, Yuanpei University of Medical Technology, Hsinchu City 300, Taiwan.
³ Department of Biochemistry and Molecular Biology, Tulane University, School of Medicine, 1430 Tulane Ave., New Orleans, LA 70112, USA.

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-Fucα1→2-active glycotopes and in their polyvalent (super) forms. When expressed by mass relative potency, the binding affinities of FRP to poly-l-Fucα1→glycotopes were about 5.0 × 10⁵ folds higher than that of the mono-l-Fucα1→glycotope form. This unique binding property of FRP can be used as a special tool to differentiate complex forms of l-Fucα1→2 and other forms of glycotopes.

Keywords: Fucolectin-related protein; Glycan recognition epitopes; Glycotopes; Polyvalency.