Details

Autor(en) / Beteiligte

• Mizgina, Tatyana O
• Chikalovets, Irina V
• Bulanova, Tatyana A
• Molchanova, Valentina I
• Filshtein, Alina P
• Ziganshin, Rustam H
• Rogozhin, Eugene A
• Shilova, Nadezhda V
• Chernikov, Oleg V

Titel

New l-Rhamnose-Binding Lectin from the Bivalve Glycymeris yessoensis : Purification, Partial Structural Characterization and Antibacterial Activity

Ist Teil von

• Marine drugs, 2024-01, Vol.22 (1), p.27

Ort / Verlag

Switzerland: MDPI AG

Erscheinungsjahr

2024

Quelle

EZB Electronic Journals Library

Beschreibungen/Notizen

• In this study, a new l-rhamnose-binding lectin (GYL-R) from the hemolymph of bivalve was purified using affinity and ion-exchange chromatography and functionally characterized. Lectin antimicrobial activity was examined in different ways. The lectin was inhibited by saccharides possessing the same configuration of hydroxyl groups at C-2 and C-4, such as l-rhamnose, d-galactose, lactose, l-arabinose and raffinose. Using the glycan microarray approach, natural carbohydrate ligands were established for GYL-R as l-Rha and glycans containing the α-Gal residue in the terminal position. The GYL-R molecular mass determined by MALDI-TOF mass spectrometry was 30,415 Da. The hemagglutination activity of the lectin was not affected by metal ions. The lectin was stable up to 75 °C and between pH 4.0 and 12.0. The amino acid sequence of the five GYL-R segments was obtained with nano-ESI MS/MS and contained both YGR and DPC-peptide motifs which are conserved in most of the l-rhamnose-binding lectin carbohydrate recognition domains. Circular dichroism confirmed that GYL is a α/β-protein with a predominance of the random coil. Furthermore, GYL-R was able to bind and suppress the growth of the Gram-negative bacteria by recognizing lipopolysaccharides. Together, these results suggest that GYL-R is a new member of the RBL family which participates in the self-defense mechanism against bacteria and pathogens with a distinct carbohydrate-binding specificity.