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Structure and anticancer activity of a new lectin from the cultivated red alga, Kappaphycus striatus.

ABSTRACT: The red alga Kappaphycus striatus is economically important food species and extensively cultivated throughout most tropical parts of the world as a source of carrageenan. In this note, the primary structure of a new lectin KSL from this alga was elucidated by the rapid amplification method of complementary DNA (cDNA) ends, which consists of 267 amino acid residues distributed in four tandem-repeated domains of about 67 amino acids and sharing 43% of identity. The calculated molecular mass from the deduced sequence was consistent with that of natural KSL (27,826 Da) determined by electron spray ionization-mass spectrometry. The primary structure of KSL showed high similarity to those of the high mannose N-glycan specific lectins from marine red algae, ESA-2 from Eucheuma serra, EDA-2 from Eucheuma denticulatum, KSA-2 from Kappaphycus striatum, KAAs from Kappaphycus alvarezii and SfLs from Solieria filiformis, and from microorganisms, BOA from Burkholderia oklahomensis, MBHA from Myxococcus xanthus, OAA from Oscillatoria agardhii and PFL from Pseudomonas fluorescens. Furthermore, KSL showed anticancer effects against five carcinoma cell lines, HT29, Hela, MCF-7, SK-LU-1 and AGS, in a dose-dependent manner with the IC50 values of 0.80-1.94 µM, whereas its inhibition activities on cancer cells were not detected in the presence of yeast mannan, an inhibitor against lectin KSL. The cultivated red alga K. striatus could also be a good source of functional lectin(s) for application as anticancer agents.

SUBMITTER: Hung LD

PROVIDER: S-EPMC7538373 | biostudies-literature | 2020 Oct

REPOSITORIES: biostudies-literature

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Structure and anticancer activity of a new lectin from the cultivated red alga, Kappaphycus striatus.

Hung Le Dinh LD Trinh Phan Thi Hoai PTH

Journal of natural medicines 20201006 1

The red alga Kappaphycus striatus is economically important food species and extensively cultivated throughout most tropical parts of the world as a source of carrageenan. In this note, the primary structure of a new lectin KSL from this alga was elucidated by the rapid amplification method of complementary DNA (cDNA) ends, which consists of 267 amino acid residues distributed in four tandem-repeated domains of about 67 amino acids and sharing 43% of identity. The calculated molecular mass from ...[more]

PMID: 33025357

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Project description:Three isolectins from cultivated Eucheuma denticulatum were isolated. They were commonly monomeric proteins of about 28 kDa with a range of averaged molecular weights from 27,834 to 27,868 Da among the isolectins and shared almost the same 20 N-terminal amino acid sequences. Complementary DNA (cDNA) cloning based on the rapid amplification cDNA ends (RACE) methods elucidated the full-length sequence of EDA-2 which encodes 269 amino acids, including initiating methionine, with four tandemly repeated domains of about 67 amino acids. The primary structure of EDA-2 is highly similar to those of the high-mannose N-glycan specific lectins including Oscillatoria agardhii (OAA) and Burkholderia oklahomensis EO147 (BOA) from cyanobacteria, Myxococcus xanthus (MBHA) and Pseudomonas fluorescens Pf0-1 (PFL) from bacteria, and ESA-2 from a macro red alga. The hemagglutination activities were commonly inhibited by the glycoproteins bearing high-mannose N-glycans, but not by monosaccharides examined, including mannose. In a direct binding experiment with pyridylaminated oligosaccharides, an isolectin EDA-2 exclusively bound to high-mannose type N-glycans, but not to other glycans that include complex types and a core pentasaccharide of N-glycans, indicating that it recognized the branched oligomannoside moiety. Its binding activity was subtly different among the oligomannoside structures examined, showing that the lectin has preference affinity for high-mannose type N-glycans with an exposed (?1-3) mannose residue in the D2 arm. Interestingly, EDAs, the mixture of three isolectins inhibited the growth of shrimp pathogenic bacterium, Vibrio alginolyticus, although it did not affect the growth of V. parahaemolyticus and V. harveyi. Growth inhibition of V. alginolyticus with EDAs was not observed in the presence of yeast mannan bearing high-mannose N-glycans, suggesting that EDAs caused the activity through binding to the target receptor(s) on the surface of V. alginolyticus. These results indicate that cultivated carrageenophyte E. denticulatum is a good source of a lectin(s) that may be useful as a carbohydrate probe and an antibacterial reagent.

Dataset Information

Structure and anticancer activity of a new lectin from the cultivated red alga, Kappaphycus striatus.

Publications

Structure and anticancer activity of a new lectin from the cultivated red alga, Kappaphycus striatus.

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