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Structural Analysis and Characterization of an Antiproliferative Lectin from Canavalia villosa Seeds
Cells use glycans to encode information that modulates processes ranging from cell–cell recognition to programmed cell death. This information is encoded within a glycocode, and its decoding is performed by carbohydrate-binding proteins. Among these, lectins stand out due to their specific and rever...
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Published in: | International journal of molecular sciences 2023-11, Vol.24 (21), p.15966 |
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creator | Lossio, Claudia F. Osterne, Vinicius J. S. Pinto-Junior, Vanir R. Chen, Simin Oliveira, Messias V. Verduijn, Joost Verbeke, Isabel Serna, Sonia Reichardt, Niels C. Skirtach, Andre Cavada, Benildo S. Van Damme, Els J. M. Nascimento, Kyria S. |
description | Cells use glycans to encode information that modulates processes ranging from cell–cell recognition to programmed cell death. This information is encoded within a glycocode, and its decoding is performed by carbohydrate-binding proteins. Among these, lectins stand out due to their specific and reversible interaction with carbohydrates. Changes in glycosylation patterns are observed in several pathologies, including cancer, where abnormal glycans are found on the surfaces of affected tissues. Given the importance of the bioprospection of promising biomolecules, the current work aimed to determine the structural properties and anticancer potential of the mannose-specific lectin from seeds of Canavalia villosa (Cvill). Experimental elucidation of the primary and 3D structures of the lectin, along with glycan array and molecular docking, facilitated the determination of its fine carbohydrate-binding specificity. These structural insights, coupled with the lectin’s specificity, have been combined to explain the antiproliferative effect of Cvill against cancer cell lines. This effect is dependent on the carbohydrate-binding activity of Cvill and its uptake in the cells, with concomitant activation of autophagic and apoptotic pathways. |
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This effect is dependent on the carbohydrate-binding activity of Cvill and its uptake in the cells, with concomitant activation of autophagic and apoptotic pathways.</description><subject>Apoptosis</subject><subject>Autophagy</subject><subject>Binding sites</subject><subject>Canavalia villosa</subject><subject>Cancer</subject><subject>Carbohydrates</subject><subject>Cell death</subject><subject>Crystallography</subject><subject>Crystals</subject><subject>glycans</subject><subject>lectin</subject><subject>Lectins</subject><subject>Legumes</subject><subject>Ligands</subject><subject>Mass spectrometry</subject><subject>Potassium</subject><subject>Scientific imaging</subject><subject>Seeds</subject><subject>Tumors</subject><issn>1422-0067</issn><issn>1661-6596</issn><issn>1422-0067</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid>PIMPY</sourceid><sourceid>DOA</sourceid><recordid>eNpdkc1r3DAQxUVpoek2x9wFvfTiRtLYsnUMSz8CCz2kPZuxNE61aK1UkhfSv77KbiltTjM8fjzmzWPsSooPAEZc-_0hq1ZJ2RmtX7AL2SrVCKH7l__sr9mbnPdCKFCduWDurqTVljVh4DcLhsfsM8fF8e0PTGgLJf8Li48Lj3PVK1P8Q4rBz5SqfiS-I1v8wucUD3yLCx4xeORHH0LMyO-IXH7LXs0YMl3-mRv2_dPHb9svze7r59vtza6xrYDSgOsBnDklEL21ujOTnltJmmbXS00atECASU0dDFNHrsaeDLrOEk22hQ27Pfu6iPvxIfkDpscxoh9PQkz3I6bibaBRDYQSEWcnVAtCo9ODgLa3znUgSVSv92evmvbnSrmMB58thYALxTVXg8EYA6KDir57hu7jmuozT9SgxAnbsOZM2RRzTjT_PVCK8am_8b_-4DdcJI6R</recordid><startdate>20231101</startdate><enddate>20231101</enddate><creator>Lossio, Claudia F.</creator><creator>Osterne, Vinicius J. 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subjects | Apoptosis Autophagy Binding sites Canavalia villosa Cancer Carbohydrates Cell death Crystallography Crystals glycans lectin Lectins Legumes Ligands Mass spectrometry Potassium Scientific imaging Seeds Tumors |
title | Structural Analysis and Characterization of an Antiproliferative Lectin from Canavalia villosa Seeds |
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