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Characterization of a Novel Mannose-Binding Lectin with Antiviral Activities from Red Alga, Grateloupia chiangii

Lectins have the ability to bind specific carbohydrates and they have potential applications as medical and pharmacological agents. The unique structure and usefulness of red algal lectin have been reported, but these lectins are limited to a few marine algal groups. In this study, a novel mannose-b...

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Autores principales: Hwang, Hyun-Ju, Han, Jin-Wook, Jeon, Hancheol, Cho, Kichul, Kim, Ju-hee, Lee, Dae-Sung, Han, Jong Won
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7072537/
https://www.ncbi.nlm.nih.gov/pubmed/32092955
http://dx.doi.org/10.3390/biom10020333
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author Hwang, Hyun-Ju
Han, Jin-Wook
Jeon, Hancheol
Cho, Kichul
Kim, Ju-hee
Lee, Dae-Sung
Han, Jong Won
author_facet Hwang, Hyun-Ju
Han, Jin-Wook
Jeon, Hancheol
Cho, Kichul
Kim, Ju-hee
Lee, Dae-Sung
Han, Jong Won
author_sort Hwang, Hyun-Ju
collection PubMed
description Lectins have the ability to bind specific carbohydrates and they have potential applications as medical and pharmacological agents. The unique structure and usefulness of red algal lectin have been reported, but these lectins are limited to a few marine algal groups. In this study, a novel mannose-binding lectin from Grateloupia chiangii (G. chiangii lectin, GCL) was purified using antiviral screens and affinity chromatography. We characterized the molecular weight, agglutination activity, hemagglutination activity, and heat stability of GCL. To determine the carbohydrate specificity, a glycan microarray was performed. GCL showed strong binding affinity for Maltohexaose-β-Sp1 and Maltoheptaose-β-Sp1 with weak affinity for other monosaccharides and preferred binding to high-mannan structures. The N-terminal sequence and peptide sequence of GCL were determined using an Edman degradation method and LC-MS/MS, and the cDNA and peptide sequences were deduced. GCL was shown to consist of 231 amino acids (24.9 kDa) and the N-terminus methionine was eliminated after translation. GCL possessed a tandem repeat structure of six domains, similar to the other red algal lectins. The mannose binding properties and tandem repeat structure of GCL may confer it the potential to act as an antiviral agent for protection against viral infection.
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spelling pubmed-70725372020-03-19 Characterization of a Novel Mannose-Binding Lectin with Antiviral Activities from Red Alga, Grateloupia chiangii Hwang, Hyun-Ju Han, Jin-Wook Jeon, Hancheol Cho, Kichul Kim, Ju-hee Lee, Dae-Sung Han, Jong Won Biomolecules Article Lectins have the ability to bind specific carbohydrates and they have potential applications as medical and pharmacological agents. The unique structure and usefulness of red algal lectin have been reported, but these lectins are limited to a few marine algal groups. In this study, a novel mannose-binding lectin from Grateloupia chiangii (G. chiangii lectin, GCL) was purified using antiviral screens and affinity chromatography. We characterized the molecular weight, agglutination activity, hemagglutination activity, and heat stability of GCL. To determine the carbohydrate specificity, a glycan microarray was performed. GCL showed strong binding affinity for Maltohexaose-β-Sp1 and Maltoheptaose-β-Sp1 with weak affinity for other monosaccharides and preferred binding to high-mannan structures. The N-terminal sequence and peptide sequence of GCL were determined using an Edman degradation method and LC-MS/MS, and the cDNA and peptide sequences were deduced. GCL was shown to consist of 231 amino acids (24.9 kDa) and the N-terminus methionine was eliminated after translation. GCL possessed a tandem repeat structure of six domains, similar to the other red algal lectins. The mannose binding properties and tandem repeat structure of GCL may confer it the potential to act as an antiviral agent for protection against viral infection. MDPI 2020-02-19 /pmc/articles/PMC7072537/ /pubmed/32092955 http://dx.doi.org/10.3390/biom10020333 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Hwang, Hyun-Ju
Han, Jin-Wook
Jeon, Hancheol
Cho, Kichul
Kim, Ju-hee
Lee, Dae-Sung
Han, Jong Won
Characterization of a Novel Mannose-Binding Lectin with Antiviral Activities from Red Alga, Grateloupia chiangii
title Characterization of a Novel Mannose-Binding Lectin with Antiviral Activities from Red Alga, Grateloupia chiangii
title_full Characterization of a Novel Mannose-Binding Lectin with Antiviral Activities from Red Alga, Grateloupia chiangii
title_fullStr Characterization of a Novel Mannose-Binding Lectin with Antiviral Activities from Red Alga, Grateloupia chiangii
title_full_unstemmed Characterization of a Novel Mannose-Binding Lectin with Antiviral Activities from Red Alga, Grateloupia chiangii
title_short Characterization of a Novel Mannose-Binding Lectin with Antiviral Activities from Red Alga, Grateloupia chiangii
title_sort characterization of a novel mannose-binding lectin with antiviral activities from red alga, grateloupia chiangii
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7072537/
https://www.ncbi.nlm.nih.gov/pubmed/32092955
http://dx.doi.org/10.3390/biom10020333
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