Published in
Elsevier, International Journal of Biological Macromolecules, (64), p. 435-442
DOI: 10.1016/j.ijbiomac.2013.12.035
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HGA-2, a novel galactoside-binding lectin from the sea cucumber Holothuria grisea binds to bacterial cells
,
Jefferson Pablo de Sousa Saboya,
Rômulo Farias Carneiro,
Alexandre Holanda Sampaio,
Raniere da Mata Moura,
Kyria Santiago do Nascimento,
Celso Shiniti Nagano,
Silvana Saker-Sampaio ,
Benildo Sousa Cavada
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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 17kDa and 34kDa 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 E.coli. Amino acid sequences of tryptic peptides of HGA-2 strongly suggest that HGA-2 is a member of the C-type lectin family.