Abstract
The lectin found in the tubers of the Winter Aconite (Eranthis hyemalis) plant is an N-acetyl-D-galactosamine specific Type II Ribosome Inactivating Protein (RIP); Type II RIPs have shown anti-cancer properties, and hence have potential as therapeutic agents. Here we present a modified protocol for the extraction and purification of the E. hyemalis lectin (EHL) using affinity chromatography. De novo amino acid sequencing of EHL confirms its classification as a Type II Ribosome Inactivating Protein. The biocidal properties of EHL have been investigated against the nematode Caenorhabditis elegans. Arrested first stage larvae treated with EHL have shown some direct mortality, with surviving larvae subsequently showing a range of phenotypes including food avoidance, reduced fecundity, developmental delay and constitutive dauer larvae formation. Both inappropriate dauer larvae development and failure to locate to bacterial food source are consistent with the disruption of chemosensory function and the ablation of amphid neurons. Further investigation indicates that mutations that disrupt normal amphid formation can block the EHL-induced dauer larvae formation. In combination, these phenotypes indicate that EHL is cytotoxic and suggest a cell specific activity against the amphid neurons of C. elegans.
Highlights
Lectins are a class of carbohydrate binding proteins ubiquitously expressed in plants, animals, bacteria and viruses, characterised by their ability to agglutinate erythrocytes (Peumans & Van Damme, 1995), a property that enabled the development of the ABO system of blood typing
Using a modified extraction protocol developed from previously published studies (Cammue, Peeters & Peumans, 1985; Kumar et al, 1993; George et al, 2011), this paper focuses on the lectin found in the tubers of Winter Aconite, Eranthis hyemalis, (EHL)
Peptide fragment homology searches produced matches to various Type II Ribosome Inactivating Proteins (RIPS) all within ricin-b domain regions. This result confirms the status of E. hyemalis lectin (EHL) as a Type II RIP, as has been reported in previously published sequence data (Kumar et al, 1993)
Summary
Lectins are a class of carbohydrate binding proteins ubiquitously expressed in plants, animals, bacteria and viruses, characterised by their ability to agglutinate erythrocytes (Peumans & Van Damme, 1995), a property that enabled the development of the ABO system of blood typing. The second characteristic common to all lectins is the ability to bind carbohydrates selectively based on the individual sugar specifity of the lectin. This results in lectins binding to the carbohydrate moieties of extracellular glycoconjugates and reversibly without introducing conformational changes to the mono- or oligosaccharides to which they bind (Sharon & Lis, 2004). Balsamin, from Momordica balsamina, demonstrates potent anti-HIV activity (Kaur et al, 2013)
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
