Functional Characterization of OXYL, A SghC1qDC LacNAc-specific Lectin from The Crinoid Feather Star Anneissia Japonica.

Imtiaj Hasan,Yasuhiro Ozeki,Yuki Fujii,Marco Gerdol

doi:10.3390/md17020136

Abstract

We identified a lectin (carbohydrate-binding protein) belonging to the complement 1q(C1q) family in the feather star Anneissia japonica (a crinoid pertaining to the phylum Echinodermata). The combination of Edman degradation and bioinformatics sequence analysis characterized the primary structure of this novel lectin, named OXYL, as a secreted 158 amino acid-long globular head (sgh)C1q domain containing (C1qDC) protein. Comparative genomics analyses revealed that OXYL pertains to a family of intronless genes found with several paralogous copies in different crinoid species. Immunohistochemistry assays identified the tissues surrounding coelomic cavities and the arms as the main sites of production of OXYL. Glycan array confirmed that this lectin could quantitatively bind to type-2 N-acetyllactosamine (LacNAc: Galβ1-4GlcNAc), but not to type-1 LacNAc (Galβ1-3GlcNAc). Although OXYL displayed agglutinating activity towards Pseudomonas aeruginosa, it had no effect on bacterial growth. On the other hand, it showed a significant anti-biofilm activity. We provide evidence that OXYL can adhere to the surface of human cancer cell lines BT-474, MCF-7, and T47D, with no cytotoxic effect. In BT-474 cells, OXYL led to a moderate activation of the p38 kinase in the MAPK signaling pathway, without affecting the activity of caspase-3. Bacterial agglutination, anti-biofilm activity, cell adhesion, and p38 activation were all suppressed by co-presence of LacNAc. This is the first report on a type-2 LacNAc-specific lectin characterized by a C1q structural fold.

Highlights

IntroductionMolecular recognition is one of the most essential mechanisms used to regulate cell systems.In primitive organisms, in specific cell types and in early developmental stages, glycans (monosaccharide chains) located on the cell surface act as a fundamental sugar code for recognition.specific glycan structures are initially recognized by glycans (via carbohydrate–carbohydrate interaction) [1] and, subsequently, by lectins (via carbohydrate–protein interaction)
Molecular recognition is one of the most essential mechanisms used to regulate cell systems.In primitive organisms, in specific cell types and in early developmental stages, glycans located on the cell surface act as a fundamental sugar code for recognition.specific glycan structures are initially recognized by glycans [1] and, subsequently, by lectins
We reported the discovery of OXYL, a Ca2+ -independent lectin isolated from the arms of the feather star Oxycomanthus japonicus, a species whose scientific name has been recently updated to Anneissia japonica

Summary

Introduction

Molecular recognition is one of the most essential mechanisms used to regulate cell systems.In primitive organisms, in specific cell types and in early developmental stages, glycans (monosaccharide chains) located on the cell surface act as a fundamental sugar code for recognition.specific glycan structures are initially recognized by glycans (via carbohydrate–carbohydrate interaction) [1] and, subsequently, by lectins (via carbohydrate–protein interaction). Molecular recognition is one of the most essential mechanisms used to regulate cell systems. In specific cell types and in early developmental stages, glycans (monosaccharide chains) located on the cell surface act as a fundamental sugar code for recognition. Specific glycan structures are initially recognized by glycans (via carbohydrate–carbohydrate interaction) [1] and, subsequently, by lectins (via carbohydrate–protein interaction). All living organisms are endowed with lectins (glycan-binding proteins) that enable such molecular interactions in different biological contexts. Mar. Drugs 2019, 17, 136; doi:10.3390/md17020136 www.mdpi.com/journal/marinedrugs

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