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Determination of thermodynamic parameters of Xerocomus chrysenteron lectin interactions with N-acetylgalactosamine and Thomsen-Friedenreich antigen by isothermal titration calorimetry
BACKGROUND: Lectins are carbohydrate-binding proteins which potentially bind to cell surface glycoconjugates. They are found in various organisms including fungi. A lectin from the mushroom Xerocomus chrysenteron (XCL) has been isolated recently. It shows insecticidal activity and has antiproliferat...
Autores principales: | , , , |
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Formato: | Texto |
Lenguaje: | English |
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BioMed Central
2005
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1166539/ https://www.ncbi.nlm.nih.gov/pubmed/15929788 http://dx.doi.org/10.1186/1471-2091-6-11 |
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author | Damian, Luminita Fournier, Didier Winterhalter, Mathias Paquereau, Laurent |
author_facet | Damian, Luminita Fournier, Didier Winterhalter, Mathias Paquereau, Laurent |
author_sort | Damian, Luminita |
collection | PubMed |
description | BACKGROUND: Lectins are carbohydrate-binding proteins which potentially bind to cell surface glycoconjugates. They are found in various organisms including fungi. A lectin from the mushroom Xerocomus chrysenteron (XCL) has been isolated recently. It shows insecticidal activity and has antiproliferative properties. RESULTS: As the monosaccharide binding specificity is an important determinant of lectin function, we determined the affinity of XCL for the galactose moiety. Isothermal titration calorimetry studies revealed a dissociation constant K(d )of 5.2 μM for the XCL:N-acetylgalactosamine interaction at 27degreesC. Higher affinities were observed at lower temperatures and higher osmotic pressures. The dissociation constant was five hundred times higher for the disaccharide beta-D-Gal(1–3)-D-GalNAc, Thomsen-Friedenreich (TF) antigen (Kd of 0.94 μM). By using fetuin and asialofetuin in interaction with the XCL, we revealed its ability to recognize the Thomsen-Friedenreich motif on glycoproteins. CONCLUSION: The XCL antiproliferative effect and the TF antigen specificity presented in this work suggest that XCL and ABL may have similar binding mechanisms. The recent structure determination of these two proteins lead us to analyse these interactions in the light of our thermodynamic data. The understanding of this type of interaction may be a useful tool for the regulation of cell proliferation. |
format | Text |
id | pubmed-1166539 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2005 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-11665392005-06-30 Determination of thermodynamic parameters of Xerocomus chrysenteron lectin interactions with N-acetylgalactosamine and Thomsen-Friedenreich antigen by isothermal titration calorimetry Damian, Luminita Fournier, Didier Winterhalter, Mathias Paquereau, Laurent BMC Biochem Research Article BACKGROUND: Lectins are carbohydrate-binding proteins which potentially bind to cell surface glycoconjugates. They are found in various organisms including fungi. A lectin from the mushroom Xerocomus chrysenteron (XCL) has been isolated recently. It shows insecticidal activity and has antiproliferative properties. RESULTS: As the monosaccharide binding specificity is an important determinant of lectin function, we determined the affinity of XCL for the galactose moiety. Isothermal titration calorimetry studies revealed a dissociation constant K(d )of 5.2 μM for the XCL:N-acetylgalactosamine interaction at 27degreesC. Higher affinities were observed at lower temperatures and higher osmotic pressures. The dissociation constant was five hundred times higher for the disaccharide beta-D-Gal(1–3)-D-GalNAc, Thomsen-Friedenreich (TF) antigen (Kd of 0.94 μM). By using fetuin and asialofetuin in interaction with the XCL, we revealed its ability to recognize the Thomsen-Friedenreich motif on glycoproteins. CONCLUSION: The XCL antiproliferative effect and the TF antigen specificity presented in this work suggest that XCL and ABL may have similar binding mechanisms. The recent structure determination of these two proteins lead us to analyse these interactions in the light of our thermodynamic data. The understanding of this type of interaction may be a useful tool for the regulation of cell proliferation. BioMed Central 2005-06-01 /pmc/articles/PMC1166539/ /pubmed/15929788 http://dx.doi.org/10.1186/1471-2091-6-11 Text en Copyright © 2005 Damian et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Damian, Luminita Fournier, Didier Winterhalter, Mathias Paquereau, Laurent Determination of thermodynamic parameters of Xerocomus chrysenteron lectin interactions with N-acetylgalactosamine and Thomsen-Friedenreich antigen by isothermal titration calorimetry |
title | Determination of thermodynamic parameters of Xerocomus chrysenteron lectin interactions with N-acetylgalactosamine and Thomsen-Friedenreich antigen by isothermal titration calorimetry |
title_full | Determination of thermodynamic parameters of Xerocomus chrysenteron lectin interactions with N-acetylgalactosamine and Thomsen-Friedenreich antigen by isothermal titration calorimetry |
title_fullStr | Determination of thermodynamic parameters of Xerocomus chrysenteron lectin interactions with N-acetylgalactosamine and Thomsen-Friedenreich antigen by isothermal titration calorimetry |
title_full_unstemmed | Determination of thermodynamic parameters of Xerocomus chrysenteron lectin interactions with N-acetylgalactosamine and Thomsen-Friedenreich antigen by isothermal titration calorimetry |
title_short | Determination of thermodynamic parameters of Xerocomus chrysenteron lectin interactions with N-acetylgalactosamine and Thomsen-Friedenreich antigen by isothermal titration calorimetry |
title_sort | determination of thermodynamic parameters of xerocomus chrysenteron lectin interactions with n-acetylgalactosamine and thomsen-friedenreich antigen by isothermal titration calorimetry |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1166539/ https://www.ncbi.nlm.nih.gov/pubmed/15929788 http://dx.doi.org/10.1186/1471-2091-6-11 |
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