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Mar. Drugs 2017, 15(8), 255; doi:10.3390/md15080255

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

1
Graduate School of Biosphere Science, Hiroshima University, Kagamiyama 1-4-4, Higashi-Hiroshima 739-8528, Japan
2
Faculty of Pharmacy, Yasuda Women’s University, Yasuhigashi 6-13-1, Asaminami-Ku, Hiroshima 731-0153, Japan
*
Author to whom correspondence should be addressed.
Received: 8 July 2017 / Revised: 8 August 2017 / Accepted: 8 August 2017 / Published: 16 August 2017
(This article belongs to the Special Issue Structures, Functions and Applications of Marine Lectins)
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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 (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. View Full-Text
Keywords: lectin; green alga; Halimeda renschii; high-mannose specificity; anti-influenza virus activity lectin; green alga; Halimeda renschii; high-mannose specificity; anti-influenza virus activity
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MDPI and ACS Style

Mu, J.; Hirayama, M.; Sato, Y.; Morimoto, K.; Hori, K. 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. Mar. Drugs 2017, 15, 255.

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