1. β-Galactoside binding lectin from caddisfly larvae, Stenopsyche kodaikanalensis with selective modes of antibacterial activity: Purification and characterization.
- Author
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Sreeramulu B, Arumugam G, Paulchamy R, Karuppiah H, and Sundaram J
- Subjects
- Adsorption, Amino Acid Sequence, Animals, Anti-Bacterial Agents chemistry, Galectins chemistry, Hemagglutination drug effects, Humans, Hydrogen-Ion Concentration, Protein Stability, Temperature, Anti-Bacterial Agents isolation & purification, Anti-Bacterial Agents pharmacology, Galectins isolation & purification, Galectins pharmacology, Insecta, Larva
- Abstract
Insects sustain the invading bacterial pathogens by inducing the production of lectin which participates in surveillance of non-self molecules. The antibacterial property of lectin is an inevitable aspect of innate immune system especially for the insects feeding the detritus organic matter. β-galactoside binding lectin possessing antibacterial property was detected and purified from the hemolymph of larvae of caddisfly, Stenopsyche kodaikanalensis using affinity chromatography. The purified lectin exhibited highest hemagglutination titer value against buffalo erythrocytes and has affinity to lactose and fetuin which contains β-galactoside linkages. It was found to be calcium independent, EDTA insensitive and heat labile. These reveal the characteristics features of S-Lac lectin. The molecular weight of lectin was 360 kDa with five distinct subunits such as 95, 90, 66, 62 and 47 kDa. The sequences acquired through MALDI-TOF-MS analysis shared homologies to the putative conserved region of leguminous lectin. Antibacterial studies were carried out with native soil bacterial isolates. It revealed that the lectin possessed the specific modes of action against bacteria that it can agglutinate the Bacillus subtilis and lyse the Bacillus flexus., (Copyright © 2018 Elsevier B.V. All rights reserved.)
- Published
- 2018
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