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
| العنوان: | 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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| المؤلفون: | Jinmin Mu, Kanji Hori, Yuichiro Sato, Makoto Hirayama, Kinjiro Morimoto |
| المصدر: | Marine Drugs Marine Drugs, Vol 15, Iss 8, p 255 (2017) Marine Drugs; Volume 15; Issue 8; Pages: 255 |
| سنة النشر: | 2017 |
| مصطلحات موضوعية: | 0301 basic medicine, Halimeda renschii, Pharmaceutical Science, Hemagglutinin (influenza), Mannose, Hemagglutinins, Viral, Oligosaccharides, high-mannose specificity, anti-influenza virus activity, Biology, Antiviral Agents, Article, 03 medical and health sciences, chemistry.chemical_compound, Agglutinin, Glycolipid, Isolectins, Chlorophyta, Polysaccharides, Lectins, Drug Discovery, green alga, Amino Acid Sequence, lcsh:QH301-705.5, Pharmacology, Toxicology and Pharmaceutics (miscellaneous), Binding selectivity, Mannan-binding lectin, Influenza A Virus, H3N2 Subtype, Monosaccharides, Lectin, Virus Internalization, 030104 developmental biology, Mannose-Binding Lectins, lcsh:Biology (General), Biochemistry, chemistry, Rhodophyta, biology.protein, lectin, Protein Binding |
| الوصف: | 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 (ED50) of 2.45 nM through high-affinity binding to a viral envelope hemagglutinin (KD, 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. |
| وصف الملف: | application/pdf |
| تدمد: | 1660-3397 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::928f7d60b57a2341c667679ee69adfcc https://pubmed.ncbi.nlm.nih.gov/28813016 |
| Rights: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....928f7d60b57a2341c667679ee69adfcc |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 16603397 |
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