About: Purification, primary structure, and biological activity of the high-mannose N-glycan-specific lectin from cultivated Eucheuma denticulatum

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About: Purification, primary structure, and biological activity of the high-mannose N-glycan-specific lectin from cultivated Eucheuma denticulatum Goto Sponge NotDistinct Permalink

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Purification, primary structure, and biological activity of the high-mannose N-glycan-specific lectin from cultivated Eucheuma denticulatum
Creator	Hirayama, Makoto Hori, Kanji Bui, & Dinh, Le Ly, Minh
source	Medline; PMC
abstract	Three isolectins from cultivated Eucheuma denticulatum were isolated. They were commonly monomeric proteins of about 28 kDa with a range of averaged molecular weights from 27,834 to 27,868 Da among the isolectins and shared almost the same 20 N-terminal amino acid sequences. Complementary DNA (cDNA) cloning based on the rapid amplification cDNA ends (RACE) methods elucidated the full-length sequence of EDA-2 which encodes 269 amino acids, including initiating methionine, with four tandemly repeated domains of about 67 amino acids. The primary structure of EDA-2 is highly similar to those of the high-mannose N-glycan specific lectins including Oscillatoria agardhii (OAA) and Burkholderia oklahomensis EO147 (BOA) from cyanobacteria, Myxococcus xanthus (MBHA) and Pseudomonas fluorescens Pf0-1 (PFL) from bacteria, and ESA-2 from a macro red alga. The hemagglutination activities were commonly inhibited by the glycoproteins bearing high-mannose N-glycans, but not by monosaccharides examined, including mannose. In a direct binding experiment with pyridylaminated oligosaccharides, an isolectin EDA-2 exclusively bound to high-mannose type N-glycans, but not to other glycans that include complex types and a core pentasaccharide of N-glycans, indicating that it recognized the branched oligomannoside moiety. Its binding activity was subtly different among the oligomannoside structures examined, showing that the lectin has preference affinity for high-mannose type N-glycans with an exposed (α1-3) mannose residue in the D2 arm. Interestingly, EDAs, the mixture of three isolectins inhibited the growth of shrimp pathogenic bacterium, Vibrio alginolyticus, although it did not affect the growth of V. parahaemolyticus and V. harveyi. Growth inhibition of V. alginolyticus with EDAs was not observed in the presence of yeast mannan bearing high-mannose N-glycans, suggesting that EDAs caused the activity through binding to the target receptor(s) on the surface of V. alginolyticus. These results indicate that cultivated carrageenophyte E. denticulatum is a good source of a lectin(s) that may be useful as a carbohydrate probe and an antibacterial reagent.
has issue date	2014-11-05(xsd:dateTime)
bibo:doi	10.1007/s10811-014-0441-0
bibo:pmid	32214663
has license	no-cc
sha1sum (hex)	fec3a0862943b980e70cc998c05d913a0ffcdf6c
schema:url	https://doi.org/10.1007/s10811-014-0441-0
resource representing a document's title	Purification, primary structure, and biological activity of the high-mannose N-glycan-specific lectin from cultivated Eucheuma denticulatum
has PubMed Central identifier	PMC7088313
has PubMed identifier	32214663
schema:publication	J Appl Phycol
resource representing a document's body	covid:fec3a0862943b980e70cc998c05d913a0ffcdf6c#body_text
is schema:about of	named entity 'shrimp' named entity 'lectins' named entity 'receptor' named entity 'affinity' named entity 'V. parahaemolyticus' named entity 'type' named entity 'pathogenic bacterium' named entity 'encodes' named entity 'V. alginolyticus' named entity 'bacteria' named entity 'inhibited' named entity 'structures' named entity 'mixture' named entity 'inhibited' named entity 'Purification' named entity 'PURIFICATION' named entity 'HIGH' named entity 'KDA' named entity 'AMINO ACIDS' named entity 'REAGENT' named entity 'OLIGOMANNOSIDE' named entity 'MYXOCOCCUS XANTHUS' named entity 'ARM' named entity 'PROBE' named entity 'OSCILLATORIA AGARDHII' named entity 'YEAST' named entity 'PROTEINS' named entity 'ENDS' named entity 'AFFINITY' named entity 'SIMILAR' named entity 'CLONING' named entity '28S' named entity 'GLYCANS' named entity 'PREFERENCE' named entity 'MONOSACCHARIDES' named entity 'INHIBITED' named entity 'INCLUDE' named entity 'ISOLATED' named entity 'AMINO ACID SEQUENCES' named entity 'PENTASACCHARIDE' named entity 'ACTIVITIES' named entity 'N-TERMINAL AMINO ACID' named entity 'CORE' named entity 'INDICATING' named entity 'HEMAGGLUTINATION' named entity 'BACTERIUM' named entity 'BOUND' named entity 'TYPES' named entity 'PRIMARY STRUCTURE' named entity 'SPECIFIC' named entity 'BIOLOGICAL ACTIVITY' named entity 'LECTIN' named entity 'HIGH-MANNOSE N-GLYCAN' named entity 'LENGTH' named entity 'GOOD' named entity 'DIRECT BINDING' named entity 'BINDING ACTIVITY' named entity 'OLIGOSACCHARIDES' named entity 'MOLECULAR WEIGHTS' named entity 'HIGHLY' named entity 'USEFUL' named entity 'ACTIVITY' named entity 'RED' named entity 'EXPOSED' named entity 'PATHOGENIC' named entity 'VIBRIO ALGINOLYTICUS' named entity 'MANNAN' named entity 'SHARED' named entity 'INCLUDING' named entity 'EXPERIMENT' named entity 'BUT' named entity 'SPECIFIC' named entity 'SURFACE' named entity 'CARBOHYDRATE' named entity 'RAPID' named entity 'RESULTS' named entity 'GROWTH'

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