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Isolation and Partial Characterisation of a Novel Lectin from Aegle marmelos Fruit and Its Effect on Adherence and Invasion of Shigellae to HT29 Cells

Lectins are a class of ubiquitous proteins/glycoproteins that are abundantly found in nature. Lectins have unique carbohydrate binding property and hence have been exploited as drugs against various infectious diseases. We have isolated one such novel lectin from the fruit pulp of Aegle marmelos. Th...

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Autores principales: Raja, Subramaniya Bharathi, Murali, Malliga Raman, Kumar, Nirmal Kasinathan, Devaraj, Sivasitambaram Niranjali
Formato: Texto
Lenguaje:English
Publicado: Public Library of Science 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3025011/
https://www.ncbi.nlm.nih.gov/pubmed/21283697
http://dx.doi.org/10.1371/journal.pone.0016231
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author Raja, Subramaniya Bharathi
Murali, Malliga Raman
Kumar, Nirmal Kasinathan
Devaraj, Sivasitambaram Niranjali
author_facet Raja, Subramaniya Bharathi
Murali, Malliga Raman
Kumar, Nirmal Kasinathan
Devaraj, Sivasitambaram Niranjali
author_sort Raja, Subramaniya Bharathi
collection PubMed
description Lectins are a class of ubiquitous proteins/glycoproteins that are abundantly found in nature. Lectins have unique carbohydrate binding property and hence have been exploited as drugs against various infectious diseases. We have isolated one such novel lectin from the fruit pulp of Aegle marmelos. The isolated lectin was partially characterised and its effect against Shigella dysenteriae infection was evaluated. The isolated lectin was found to be a dimeric protein with N-acetylgalactosamine, mannose and sialic acid binding specificity. The effect of Aegle marmelos fruit lectin on the adherence of Shigella dysenteriae to human colonic epithelial cells (HT29 cells) was evaluated by Enzyme Linked Immune Sorbent Assay and invasion was analysed. The protective nature of the Aegle marmelos fruit lectin was assessed by analyzing apoptosis through dual staining method. Aegle marmelos fruit lectin significantly inhibited hemagglutination activity of Shigella and its minimum inhibitory concentration is 0.625 µg/well. Further, at this concentration lectin inhibited Shigella dysenteriae adherence and invasion of HT29 cells and protects the HT29 cells from Shigella dysenteriae induced apoptosis. To conclude, isolated lectin dimeric protein with N-acetylgalactosamine, Mannose and sialic acid binding specificity and inhibits adherence and invasion of Shigellae to HT29 cells thus, protects the host.
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spelling pubmed-30250112011-01-31 Isolation and Partial Characterisation of a Novel Lectin from Aegle marmelos Fruit and Its Effect on Adherence and Invasion of Shigellae to HT29 Cells Raja, Subramaniya Bharathi Murali, Malliga Raman Kumar, Nirmal Kasinathan Devaraj, Sivasitambaram Niranjali PLoS One Research Article Lectins are a class of ubiquitous proteins/glycoproteins that are abundantly found in nature. Lectins have unique carbohydrate binding property and hence have been exploited as drugs against various infectious diseases. We have isolated one such novel lectin from the fruit pulp of Aegle marmelos. The isolated lectin was partially characterised and its effect against Shigella dysenteriae infection was evaluated. The isolated lectin was found to be a dimeric protein with N-acetylgalactosamine, mannose and sialic acid binding specificity. The effect of Aegle marmelos fruit lectin on the adherence of Shigella dysenteriae to human colonic epithelial cells (HT29 cells) was evaluated by Enzyme Linked Immune Sorbent Assay and invasion was analysed. The protective nature of the Aegle marmelos fruit lectin was assessed by analyzing apoptosis through dual staining method. Aegle marmelos fruit lectin significantly inhibited hemagglutination activity of Shigella and its minimum inhibitory concentration is 0.625 µg/well. Further, at this concentration lectin inhibited Shigella dysenteriae adherence and invasion of HT29 cells and protects the HT29 cells from Shigella dysenteriae induced apoptosis. To conclude, isolated lectin dimeric protein with N-acetylgalactosamine, Mannose and sialic acid binding specificity and inhibits adherence and invasion of Shigellae to HT29 cells thus, protects the host. Public Library of Science 2011-01-21 /pmc/articles/PMC3025011/ /pubmed/21283697 http://dx.doi.org/10.1371/journal.pone.0016231 Text en Raja et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Raja, Subramaniya Bharathi
Murali, Malliga Raman
Kumar, Nirmal Kasinathan
Devaraj, Sivasitambaram Niranjali
Isolation and Partial Characterisation of a Novel Lectin from Aegle marmelos Fruit and Its Effect on Adherence and Invasion of Shigellae to HT29 Cells
title Isolation and Partial Characterisation of a Novel Lectin from Aegle marmelos Fruit and Its Effect on Adherence and Invasion of Shigellae to HT29 Cells
title_full Isolation and Partial Characterisation of a Novel Lectin from Aegle marmelos Fruit and Its Effect on Adherence and Invasion of Shigellae to HT29 Cells
title_fullStr Isolation and Partial Characterisation of a Novel Lectin from Aegle marmelos Fruit and Its Effect on Adherence and Invasion of Shigellae to HT29 Cells
title_full_unstemmed Isolation and Partial Characterisation of a Novel Lectin from Aegle marmelos Fruit and Its Effect on Adherence and Invasion of Shigellae to HT29 Cells
title_short Isolation and Partial Characterisation of a Novel Lectin from Aegle marmelos Fruit and Its Effect on Adherence and Invasion of Shigellae to HT29 Cells
title_sort isolation and partial characterisation of a novel lectin from aegle marmelos fruit and its effect on adherence and invasion of shigellae to ht29 cells
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3025011/
https://www.ncbi.nlm.nih.gov/pubmed/21283697
http://dx.doi.org/10.1371/journal.pone.0016231
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