HGA-2, a novel galactoside-binding lectin from the sea cucumber Holothuria grisea binds to bacterial cells.

Authors :: de Melo AA
Carneiro RF
de Melo Silva W
Moura Rda M
Silva GC
de Sousa OV
de Sousa Saboya JP
Nascimento KS
Saker-Sampaio S
Nagano CS
Cavada BS
Sampaio AH
Source :: International journal of biological macromolecules [Int J Biol Macromol] 2014 Mar; Vol. 64, pp. 435-42. Date of Electronic Publication: 2014 Jan 03.
Publication Year :: 2014
Abstract: A novel lectin, HGA-2, was isolated from the sea cucumber Holothuria grisea. The protein was isolated by a single chromatographic step using a column of Guar Gum as affinity. HGA-2 showed an apparent molecular mass of 17 kDa and 34 kDa under reducing and nonreducing conditions, respectively. The hemagglutinating activity was specific for rabbit erythrocytes, showing no activity for human blood A, B and O. Its hemagglutinating activity was inhibited by carbohydrates containing galactose, with higher affinity for GalNAc and glycoprotein porcine stomach mucin (PSM). HGA-2 was stable at pH 6-10, significantly declining at pH 5 and a temperature of 40°C, with its activity being abolished at 100 °C. The HGA-2 protein was found to be Ca(2+)-dependent; it was highly toxic against Artemia nauplii and able to recognize and agglutinate cells of Escherichia coli. Amino acid sequences of tryptic peptides of HGA-2 strongly suggest that HGA-2 is a member of the C-type lectin family.<br /> (Copyright © 2014 Elsevier B.V. All rights reserved.)

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