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The Lectin Frontier Database (LfDB), and Data Generation Based on Frontal Affinity Chromatography
Lectins are a large group of carbohydrate-binding proteins, having been shown to comprise at least 48 protein scaffolds or protein family entries. They occur ubiquitously in living organisms—from humans to microorganisms, including viruses—and while their functions are yet to be fully elucidated, th...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6272529/ https://www.ncbi.nlm.nih.gov/pubmed/25580689 http://dx.doi.org/10.3390/molecules20010951 |
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author | Hirabayashi, Jun Tateno, Hiroaki Shikanai, Toshihide Aoki-Kinoshita, Kiyoko F. Narimatsu, Hisashi |
author_facet | Hirabayashi, Jun Tateno, Hiroaki Shikanai, Toshihide Aoki-Kinoshita, Kiyoko F. Narimatsu, Hisashi |
author_sort | Hirabayashi, Jun |
collection | PubMed |
description | Lectins are a large group of carbohydrate-binding proteins, having been shown to comprise at least 48 protein scaffolds or protein family entries. They occur ubiquitously in living organisms—from humans to microorganisms, including viruses—and while their functions are yet to be fully elucidated, their main underlying actions are thought to mediate cell-cell and cell-glycoconjugate interactions, which play important roles in an extensive range of biological processes. The basic feature of each lectin’s function resides in its specific sugar-binding properties. In this regard, it is beneficial for researchers to have access to fundamental information about the detailed oligosaccharide specificities of diverse lectins. In this review, the authors describe a publicly available lectin database named “Lectin frontier DataBase (LfDB)”, which undertakes the continuous publication and updating of comprehensive data for lectin-standard oligosaccharide interactions in terms of dissociation constants (K(d)’s). For K(d) determination, an advanced system of frontal affinity chromatography (FAC) is used, with which quantitative datasets of interactions between immobilized lectins and >100 fluorescently labeled standard glycans have been generated. The FAC system is unique in its clear principle, simple procedure and high sensitivity, with an increasing number (>67) of associated publications that attest to its reliability. Thus, LfDB, is expected to play an essential role in lectin research, not only in basic but also in applied fields of glycoscience. |
format | Online Article Text |
id | pubmed-6272529 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-62725292018-12-28 The Lectin Frontier Database (LfDB), and Data Generation Based on Frontal Affinity Chromatography Hirabayashi, Jun Tateno, Hiroaki Shikanai, Toshihide Aoki-Kinoshita, Kiyoko F. Narimatsu, Hisashi Molecules Review Lectins are a large group of carbohydrate-binding proteins, having been shown to comprise at least 48 protein scaffolds or protein family entries. They occur ubiquitously in living organisms—from humans to microorganisms, including viruses—and while their functions are yet to be fully elucidated, their main underlying actions are thought to mediate cell-cell and cell-glycoconjugate interactions, which play important roles in an extensive range of biological processes. The basic feature of each lectin’s function resides in its specific sugar-binding properties. In this regard, it is beneficial for researchers to have access to fundamental information about the detailed oligosaccharide specificities of diverse lectins. In this review, the authors describe a publicly available lectin database named “Lectin frontier DataBase (LfDB)”, which undertakes the continuous publication and updating of comprehensive data for lectin-standard oligosaccharide interactions in terms of dissociation constants (K(d)’s). For K(d) determination, an advanced system of frontal affinity chromatography (FAC) is used, with which quantitative datasets of interactions between immobilized lectins and >100 fluorescently labeled standard glycans have been generated. The FAC system is unique in its clear principle, simple procedure and high sensitivity, with an increasing number (>67) of associated publications that attest to its reliability. Thus, LfDB, is expected to play an essential role in lectin research, not only in basic but also in applied fields of glycoscience. MDPI 2015-01-08 /pmc/articles/PMC6272529/ /pubmed/25580689 http://dx.doi.org/10.3390/molecules20010951 Text en © 2015 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 license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Hirabayashi, Jun Tateno, Hiroaki Shikanai, Toshihide Aoki-Kinoshita, Kiyoko F. Narimatsu, Hisashi The Lectin Frontier Database (LfDB), and Data Generation Based on Frontal Affinity Chromatography |
title | The Lectin Frontier Database (LfDB), and Data Generation Based on Frontal Affinity Chromatography |
title_full | The Lectin Frontier Database (LfDB), and Data Generation Based on Frontal Affinity Chromatography |
title_fullStr | The Lectin Frontier Database (LfDB), and Data Generation Based on Frontal Affinity Chromatography |
title_full_unstemmed | The Lectin Frontier Database (LfDB), and Data Generation Based on Frontal Affinity Chromatography |
title_short | The Lectin Frontier Database (LfDB), and Data Generation Based on Frontal Affinity Chromatography |
title_sort | lectin frontier database (lfdb), and data generation based on frontal affinity chromatography |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6272529/ https://www.ncbi.nlm.nih.gov/pubmed/25580689 http://dx.doi.org/10.3390/molecules20010951 |
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