Characterization of sialic acid affinity of the binding domain of mistletoe lectin isoform one

Mohammed, S ORCID: https://orcid.org/0000-0002-3882-6129 and Ferry, N ORCID: https://orcid.org/0000-0003-3728-4302 2021, 'Characterization of sialic acid affinity of the binding domain of mistletoe lectin isoform one' , International Journal of Molecular Sciences, 22 (15) , e8284.

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Abstract

Sialic acid (Sia) is considered as one of the most important biomolecules of life since its derivatives and terminal orientations on cell membranes and macromolecules play a major role in many biological and pathological processes. To date, there is only a limited number of active molecules that can selectively bind to Sia and this limitation has made the study of this glycan challenging. The lectin superfamily is a well-known family of glycan binding proteins, which encompasses many strong glycan binding peptides with diverse glycan affinities. Mistletoe lectin (ML) is considered one of the most active members of lectin family which was initially classified in early studies as a galactose binding lectin; more recent studies have suggested that the peptide can also actively bind to Sia. However, the details with respect to Sia binding of ML and the domain responsible for this binding are left unanswered because no comprehensive studies have been instigated. In this study, we sought to identify the binding domain responsible for the sialic acid affinity of mistletoe lectin isoform I (MLI) in comparison to the binding activity of elderberry lectin isoform I (SNA), which has long been identified as a potent Sia binding lectin. In order to execute this, we performed computational carbohydrate-protein docking for MLB and SNA with Neu5Ac and β-Galactose. We further analyzed the coding sequence of both lectins and identified their glycan binding domains, which were later cloned upstream and downstream to green fluorescent protein (GFP) and expressed in Escherichia coli (E. coli). Finally, the glycan affinity of the expressed fusion proteins was assessed by using different biochemical and cell-based assays and the Sia binding domains were identified.

Item Type: Article
Contributors: Pshezhetsky, AV (Editor), Cairo, CW (Editor) and Garozzo, D (Editor)
Additional Information: ** From MDPI via Jisc Publications Router ** Licence for this article: https://creativecommons.org/licenses/by/4.0/ **Journal IDs: eissn 1422-0067 **History: published 31-07-2021; accepted 29-07-2021
Schools: Schools > School of Environment and Life Sciences > Biomedical Research Centre
Journal or Publication Title: International Journal of Molecular Sciences
Publisher: MDPI
ISSN: 1422-0067
Related URLs:
SWORD Depositor: Publications Router
Depositing User: Publications Router
Date Deposited: 02 Aug 2021 09:24
Last Modified: 28 Aug 2021 10:31
URI: http://usir.salford.ac.uk/id/eprint/61390

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