Structural characterization and interaction with RCA120 of a highly sulfated keratan sulfate from blue shark (Prionace glauca) cartilage

Qinying Li; Guoyun Li; Xiaoliang Zhao; Xindi Shan; Chao Cai; Jing Zhao; Fuming Zhang; Robert J. Linhardt; Guangli Yu

doi:10.3390/md16040128

Structural characterization and interaction with RCA₁₂₀ of a highly sulfated keratan sulfate from blue shark (Prionace glauca) cartilage

Qinying Li, Guoyun Li, Xiaoliang Zhao, Xindi Shan, Chao Cai, Jing Zhao, Fuming Zhang, Robert J. Linhardt, Guangli Yu

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

4 Scopus citations

Abstract

As an important glycosaminoglycan, keratan sulfate (KS) mainly exists in corneal and cartilage, possessing various biological activities. In this study, we purified KS from blue shark (Prionace glauca) cartilage and prepared KS oligosaccharides (KSO) through keratanase II-catalyzed hydrolysis. The structures of KS and KSO were characterized using multi-dimensional nuclear magnetic resonance (NMR) spectra and liquid chromatography-mass spectrometry (LC-MS). Shark cartilage KS was highly sulfated and modified with ~2.69% N-acetylneuraminic acid (NeuAc) through α(2,3)-linked to galactose. Additionally, KS exhibited binding affinity to Ricinus communis agglutinin I (RCA₁₂₀) in a concentration-dependent manner, a highly toxic lectin from beans of the castor plant. Furthermore, KSO from dp2 to dp8 bound to RCA₁₂₀ in the increasing trend while the binding affinity of dp8 was superior to polysaccharide. These results define novel structural features for KS from Prionace glauca cartilage and demonstrate the potential application on ricin-antidote exploitation.

Original language	English
Article number	128
Journal	Marine Drugs
Volume	16
Issue number	4
DOIs	https://doi.org/10.3390/md16040128
State	Published - Apr 2018
Externally published	Yes

Keywords

HILIC-FTMS
Keratan sulfate
NMR spectra
Prionace glauca cartilage
Ricinus communis agglutinin I
Structural characterization

Access to Document

10.3390/md16040128

Cite this

@article{68a7a90a2bf44f9faab5b180d0aac6d8,

title = "Structural characterization and interaction with RCA120 of a highly sulfated keratan sulfate from blue shark (Prionace glauca) cartilage",

abstract = "As an important glycosaminoglycan, keratan sulfate (KS) mainly exists in corneal and cartilage, possessing various biological activities. In this study, we purified KS from blue shark (Prionace glauca) cartilage and prepared KS oligosaccharides (KSO) through keratanase II-catalyzed hydrolysis. The structures of KS and KSO were characterized using multi-dimensional nuclear magnetic resonance (NMR) spectra and liquid chromatography-mass spectrometry (LC-MS). Shark cartilage KS was highly sulfated and modified with ~2.69% N-acetylneuraminic acid (NeuAc) through α(2,3)-linked to galactose. Additionally, KS exhibited binding affinity to Ricinus communis agglutinin I (RCA120) in a concentration-dependent manner, a highly toxic lectin from beans of the castor plant. Furthermore, KSO from dp2 to dp8 bound to RCA120 in the increasing trend while the binding affinity of dp8 was superior to polysaccharide. These results define novel structural features for KS from Prionace glauca cartilage and demonstrate the potential application on ricin-antidote exploitation.",

keywords = "HILIC-FTMS, Keratan sulfate, NMR spectra, Prionace glauca cartilage, Ricinus communis agglutinin I, Structural characterization",

author = "Qinying Li and Guoyun Li and Xiaoliang Zhao and Xindi Shan and Chao Cai and Jing Zhao and Fuming Zhang and Linhardt, {Robert J.} and Guangli Yu",

note = "Publisher Copyright: {\textcopyright} 2018 by the authors.",

year = "2018",

month = apr,

doi = "10.3390/md16040128",

language = "English",

volume = "16",

journal = "Marine Drugs",

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T1 - Structural characterization and interaction with RCA120 of a highly sulfated keratan sulfate from blue shark (Prionace glauca) cartilage

AU - Li, Qinying

AU - Li, Guoyun

AU - Zhao, Xiaoliang

AU - Shan, Xindi

AU - Cai, Chao

AU - Zhao, Jing

AU - Zhang, Fuming

AU - Linhardt, Robert J.

AU - Yu, Guangli

PY - 2018/4

Y1 - 2018/4

N2 - As an important glycosaminoglycan, keratan sulfate (KS) mainly exists in corneal and cartilage, possessing various biological activities. In this study, we purified KS from blue shark (Prionace glauca) cartilage and prepared KS oligosaccharides (KSO) through keratanase II-catalyzed hydrolysis. The structures of KS and KSO were characterized using multi-dimensional nuclear magnetic resonance (NMR) spectra and liquid chromatography-mass spectrometry (LC-MS). Shark cartilage KS was highly sulfated and modified with ~2.69% N-acetylneuraminic acid (NeuAc) through α(2,3)-linked to galactose. Additionally, KS exhibited binding affinity to Ricinus communis agglutinin I (RCA120) in a concentration-dependent manner, a highly toxic lectin from beans of the castor plant. Furthermore, KSO from dp2 to dp8 bound to RCA120 in the increasing trend while the binding affinity of dp8 was superior to polysaccharide. These results define novel structural features for KS from Prionace glauca cartilage and demonstrate the potential application on ricin-antidote exploitation.

AB - As an important glycosaminoglycan, keratan sulfate (KS) mainly exists in corneal and cartilage, possessing various biological activities. In this study, we purified KS from blue shark (Prionace glauca) cartilage and prepared KS oligosaccharides (KSO) through keratanase II-catalyzed hydrolysis. The structures of KS and KSO were characterized using multi-dimensional nuclear magnetic resonance (NMR) spectra and liquid chromatography-mass spectrometry (LC-MS). Shark cartilage KS was highly sulfated and modified with ~2.69% N-acetylneuraminic acid (NeuAc) through α(2,3)-linked to galactose. Additionally, KS exhibited binding affinity to Ricinus communis agglutinin I (RCA120) in a concentration-dependent manner, a highly toxic lectin from beans of the castor plant. Furthermore, KSO from dp2 to dp8 bound to RCA120 in the increasing trend while the binding affinity of dp8 was superior to polysaccharide. These results define novel structural features for KS from Prionace glauca cartilage and demonstrate the potential application on ricin-antidote exploitation.

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KW - NMR spectra

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KW - Ricinus communis agglutinin I

KW - Structural characterization

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