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

Albert M. Wu^*, Tanuja Singh, Yung Liang Chen, Kimberly M. Anderson, Su Chen Li, Yu Teh Li

^*Corresponding author for this work

Department of Molecular Biology

Research output: Contribution to journal › Journal Article › peer-review

2 Scopus citations

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.

Original language	English
Pages (from-to)	17-23
Number of pages	7
Journal	Biochimie Open
Volume	6
DOIs	https://doi.org/10.1016/j.biopen.2017.12.002
State	Published - 06 2018

Bibliographical note

Publisher Copyright:
© 2018 The Authors

Keywords

Fucolectin-related protein
Glycan recognition epitopes
Glycotopes
Polyvalency

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10.1016/j.biopen.2017.12.002

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

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",

author = "Wu, {Albert M.} and Tanuja Singh and Chen, {Yung Liang} and Anderson, {Kimberly M.} and Li, {Su Chen} and Li, {Yu Teh}",

note = "Publisher Copyright: {\textcopyright} 2018 The Authors",

year = "2018",

month = jun,

doi = "10.1016/j.biopen.2017.12.002",

language = "英语",

volume = "6",

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journal = "Biochimie Open",

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AU - Wu, Albert M.

AU - Singh, Tanuja

AU - Chen, Yung Liang

AU - Anderson, Kimberly M.

AU - Li, Su Chen

AU - Li, Yu Teh

PY - 2018/6

Y1 - 2018/6

N2 - 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.

AB - 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.

KW - Fucolectin-related protein

KW - Glycan recognition epitopes

KW - Glycotopes

KW - Polyvalency

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SN - 2214-0085

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JO - Biochimie Open

JF - Biochimie Open

ER -

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

Abstract

Bibliographical note

Keywords

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