2017
DOI: 10.3390/md15080255
|View full text |Cite
|
Sign up to set email alerts
|

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

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 oligosacch… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

1
40
0
2

Year Published

2018
2018
2024
2024

Publication Types

Select...
7
1
1

Relationship

0
9

Authors

Journals

citations
Cited by 42 publications
(53 citation statements)
references
References 39 publications
1
40
0
2
Order By: Relevance
“…Based on the qualitative HI assay, both of the P. australis and P. minor extracts did not have an affinity to the various simple sugars tested. This result is in line with previous reports that macroalgae lectins generally do not have an affinity to simple sugars but have more affinity to glycoconjugates (Hung et al, 2015;Mu, Hirayama, Sato, Morimoto, & Hori, 2017;Nagano et al, 2002;Singh & Walia, 2018). Lectincontaining extract of P. australis bond 7 glycoproteins, i.e., thyroglobulin from bovine thyroid gland (BTG), thyroglobulin from porcine thyroid gland (PTG), Asialo-Fetuin (aFe), Asialo-BSM (aBSM), Asialo-PTG (aPTG), Asialo-Tf (aTf), and Asialo-BTG (aBTG), while P. minor extract only bound 3 asialo glycoproteins, i.e.…”
Section: Resultssupporting
confidence: 93%
“…Based on the qualitative HI assay, both of the P. australis and P. minor extracts did not have an affinity to the various simple sugars tested. This result is in line with previous reports that macroalgae lectins generally do not have an affinity to simple sugars but have more affinity to glycoconjugates (Hung et al, 2015;Mu, Hirayama, Sato, Morimoto, & Hori, 2017;Nagano et al, 2002;Singh & Walia, 2018). Lectincontaining extract of P. australis bond 7 glycoproteins, i.e., thyroglobulin from bovine thyroid gland (BTG), thyroglobulin from porcine thyroid gland (PTG), Asialo-Fetuin (aFe), Asialo-BSM (aBSM), Asialo-PTG (aPTG), Asialo-Tf (aTf), and Asialo-BTG (aBTG), while P. minor extract only bound 3 asialo glycoproteins, i.e.…”
Section: Resultssupporting
confidence: 93%
“…They are a structurally diverse group of highly specific and reversibly carbohydrate-binding proteins [70]. The three groups of macroalgae (Rhodophyta, Phaeophyta, and Chlorophyta) can produce lectins [71], and these lectins present great potential for the development of new drugs [72][73][74][75][76]. In fact, because of the highly specific way lectins bind to sugars outside cell surfaces inhibiting cell proliferation [77,78], lectins primarily show antiviral, antibacterial, and antifungal activities [73,[79][80][81].…”
Section: Griffithsinmentioning
confidence: 99%
“…Mannose-specific Lectin from Green alga Halimeda renschii showed strong activity against influenza virus due to high affinity binding to hemagglutinins on envelopes of viruses [115].…”
Section: Glycoproteinsmentioning
confidence: 99%