Earticle

초록

영어

Mushroom lectins harboring carbohydrate binding specificity are powerful tools to detect glycoconjugates with N-linked or O-linked glycans. In this study, we purified a novel core 1 O-linked glycan-specific lectin from the fruiting body extract of a mushroom Helicium erinaceus by ion-exchange chromatography, affinity chromatography on fetuin-agarose, gel filtration chromatography. The purified lectin was designed as HEL1 (H. erinaceus lectin 1). Tricine-PAGE, MALDI-TOF mass spectrometry, and N-terminal amino acid sequencing indicated that the native lectin has an identical form with a molecular weight of approximate 15 kDa and a lectin-like structure sequence. Isoelectric focusing of the lectin showed bands near pI 5.4. Agglutination assay displayed HEL1 was more effective toward porcine’s erythrocyte rather than other animals red blood cells. Glycan microarray analysis showed that HEL1 interacts with Galβ1-3GalNAc present in Thomsen-Friedenreich antigen or core 1 O-linked glycan structure such as Peanut agglutinain (PNA). Comparing the glycan binding affinities in glycan microarray, both HEL1 and PNA bound core 1 O-linked glycan. Interestingly, HEL1 can bind a broad range of glycan structures with an extension on the β1-3Gal linked to the GalNAc as well as a terminal α(2-3) linked sialic acid which is not bound by PNA. These HEL1 binding affinities could be useful to apply the cancer research and diagnostic assay involving core 1 and extended core 1 glycan structures.

저자

• Seonghun Kim [ Jeonbuk Branch Institute, Korea Research Institute of Bioscience and Biotechnology, Jeongeup 580- 185, Korea; Biosystems and Bioengineering Program, University of Science and Technology (UST), Daejeon 305-350, Korea ]

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간행물

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• 간행물명

  한국당과학회 학술대회

• 간기

  연간

• 수록기간

  2006~2022

• 십진분류

  KDC 517 DDC 614