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Comp Biochem Physiol B Biochem Mol Biol. 2018 Feb;216:32-38. doi: 10.1016/j.cbpb.2017.11.008. Epub 2017 Nov 22.

Purification, characterization and biological effect of lectin from the marine sponge Stylissa flexibilis (Lévi, 1961).

Author information

1
NhaTrang Institute of Technology Research and Application - VietNam Academy of Science and Technology, 2A, HungVuong Street, NhaTrang City, KhanhHoa Province, Viet Nam. Electronic address: ledinhhung@nitra.vast.vn.
2
NhaTrang Institute of Technology Research and Application - VietNam Academy of Science and Technology, 2A, HungVuong Street, NhaTrang City, KhanhHoa Province, Viet Nam.
3
NhaTrang University, 02 NguyenDinhChieu, NhaTrang City, KhanhHoa Province, Viet Nam.
4
Institute of Oceanography - VietNam Academy of Science and Technology, 01 CauDa, NhaTrang City, KhanhHoa Province, Viet Nam.

Abstract

SFL, a lectin from the marine sponge Stylissa flexibilis was purified by cold ethanol precipitation followed by ion exchange chromatography on DEAE Sepharose column and Sephacryl S-200 gel filtration. SFL is a dimeric glycoprotein of 32kDa subunits linked by a disulfide bridge with a molecular mass of 64kDa by SDS-PAGE and 65kDa by Sephacryl S-200 gel filtration. SFL preferentially agglutinated enzyme treated human A erythrocytes. The activity of lectin was strongly inhibited by monosaccharide d-galactose and glycoproteins asialo-porcine stomach mucin and asialo-fetuin. The lectin was Ca2+ dependent, stable over a range of pH from 5 to 8, and up to 60°C for 30min. The N-terminal amino acid sequence of SFL was also determined and a blast search on amino acid sequences revealed that the protein showed similarity only with lectins from the marine sponge Spheciospongia vesparia. SFL caused agglutination of Vibrio alginolyticus and V. parahaemolyticus in a dose dependent manner and inhibited the growth rates of the virulent bacterial strains. Growth inhibition of V. alginolyticus and V. parahaemolyticus with SFL was not observed in the presence of d-galactose or asialo-porcine stomach mucin, suggesting that the lectin caused the agglutination through binding to the target receptor(s) on the surface of Vibrios. Thus, the marine sponge S. flexibilis could promise to be a good source of a lectin(s) that may be useful as a carbohydrate probe and an antibacterial reagent.

KEYWORDS:

Antibacterial activity; Carbohydrate binding specificity; Lectin; Marine sponge; Marine vibrios; Molecular mass; Stability; Stylissa flexibilis

PMID:
29175481
DOI:
10.1016/j.cbpb.2017.11.008
[Indexed for MEDLINE]

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