About: A Novel High-Mannose Specific Lectin from the Green Alga Halimeda renschii Exhibits a Potent Anti-Influenza Virus Activity through High-Affinity Binding to the Viral Hemagglutinin

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About: A Novel High-Mannose Specific Lectin from the Green Alga Halimeda renschii Exhibits a Potent Anti-Influenza Virus Activity through High-Affinity Binding to the Viral Hemagglutinin Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	A Novel High-Mannose Specific Lectin from the Green Alga Halimeda renschii Exhibits a Potent Anti-Influenza Virus Activity through High-Affinity Binding to the Viral Hemagglutinin
Creator	Hirayama, Makoto Hori, Kanji Morimoto, Kinjiro Sato, Yuichiro Mu, Jinmin
Source	Medline; PMC
abstract	We have isolated a novel lectin, named HRL40 from the green alga Halimeda renschii. In hemagglutination-inhibition test and oligosaccharide-binding experiment with 29 pyridylaminated oligosaccharides, HRL40 exhibited a strict binding specificity for high-mannose N-glycans having an exposed (α1-3) mannose residue in the D2 arm of branched mannosides, and did not have an affinity for monosaccharides and other oligosaccharides examined, including complex N-glycans, an N-glycan core pentasaccharide, and oligosaccharides from glycolipids. The carbohydrate binding profile of HRL40 resembled those of Type I high-mannose specific antiviral algal lectins, or the Oscillatoria agardhii agglutinin (OAA) family, which were previously isolated from red algae and a blue-green alga (cyanobacterium). HRL40 potently inhibited the infection of influenza virus (A/H3N2/Udorn/72) into NCI-H292 cells with half-maximal effective dose (ED(50)) of 2.45 nM through high-affinity binding to a viral envelope hemagglutinin (K(D), 3.69 × 10(−11) M). HRL40 consisted of two isolectins (HRL40-1 and HRL40-2), which could be separated by reverse-phase HPLC. Both isolectins had the same molecular weight of 46,564 Da and were a disulfide -linked tetrameric protein of a 11,641 Da polypeptide containing at least 13 half-cystines. Thus, HRL40, which is the first Type I high-mannose specific antiviral lectin from the green alga, had the same carbohydrate binding specificity as the OAA family, but a molecular structure distinct from the family.
has issue date	2017-08-16(xsd:dateTime)
bibo:doi	10.3390/md15080255
bibo:pmid	28813016
has license	cc-by
sha1sum (hex)	ffb147f62b6570ee48fa765305c24ebcc8e4912f
schema:url	https://doi.org/10.3390/md15080255
resource representing a document's title	A Novel High-Mannose Specific Lectin from the Green Alga Halimeda renschii Exhibits a Potent Anti-Influenza Virus Activity through High-Affinity Binding to the Viral Hemagglutinin
has PubMed Central identifier	PMC5577609
has PubMed identifier	28813016
schema:publication	Mar Drugs
resource representing a document's body	covid:ffb147f62b6570ee48fa765305c24ebcc8e4912f#body_text
is schema:about of	named entity 'AFFINITY' named entity 'HIGH' named entity 'BINDING' named entity 'ALGA' named entity 'HEMAGGLUTININ' named entity 'NAMED' named entity 'ALGA' named entity 'GREEN ' named entity 'ISOLATED' named entity 'MANNOSE SPECIFIC LECTIN' named entity 'HALIMEDA RENSCHII' named entity 'INFLUENZA VIRUS' named entity 'VIRAL' named entity 'ACTIVITY' named entity 'THE GREEN' named entity 'NOVEL' named entity 'EXHIBITS' named entity 'LECTIN' named entity 'HALIMEDA RENSCHII' named entity 'HAVE' named entity 'NOVEL' named entity 'THE GREEN' named entity 'GREEN ' covid:arg/ffb147f62b6570ee48fa765305c24ebcc8e4912f named entity 'lectin' named entity 'Binding' named entity 'Halimeda' named entity 'lectin' named entity 'Mannose' named entity 'Hemagglutinin' named entity 'oligosaccharides' named entity 'plants and animals' named entity 'gradient elution' named entity 'precipitate' named entity 'influenza virus' named entity 'molecular weights' named entity 'Ann Arbor' named entity 'HPLC' named entity 'Hemagglutinin' named entity 'green alga' named entity 'viral strain' named entity 'lectins' named entity 'surface plasmon resonance' named entity 'protein' named entity 'Hemagglutination' named entity 'Japan' named entity 'mannan' named entity 'amino acids' named entity 'trifluoroacetic acid' named entity 'immunocompetence' named entity 'Japan' named entity 'kDa' named entity 'eluate' named entity 'oligosaccharides' named entity 'molecule' named entity 'binding sites' named entity 'sialoglycoproteins' named entity 'host cells' named entity 'chromatography' named entity 'lectins' named entity 'aqueous' named entity 'gel-filtration' named entity 'glycoproteins' named entity 'amino acids' named entity 'ultrafiltration' named entity 'lectin' named entity 'gel-filtration' named entity 'PEER REVIEW' named entity 'yeast' named entity 'influenza' named entity 'amino acids' named entity 'molecular weight' named entity 'N-glycans' named entity 'Protein content' named entity 'protein' named entity 'methanol' named entity 'D-Xylose'

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