H-3, a new lectin from the marine sponge Haliclona caerulea: Purification and mass spectrometric characterization

Carneiro, Rômulo Farias; Melo, Arthur A.; Almeida, Alexandra Sampaio de; Moura, Raniere da Mata; Chaves, Renata Pinheiro; Sousa, Bruno; Nascimento, Kyria S.; Sampaio, Silvana Saker; Lima, J. A. S.; Cavada, Benildo S.; Nagano, Celso Shiniti; Sampaio, Alexandre Holanda

doi:10.1016/j.biocel.2013.10.005

Cited by 31 publications

(12 citation statements)

References 35 publications

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“…Inhibition by asialo-fetuin has been evidenced for lectins from marine sponges, such as HOL-30 from Halichondria okadai (Kawsar et al, 2008) and HcL from Haliclona cratera (Pajic et al, 2002). On the other hand, inhibition by porcine stomatch mucin and their asialo derivatives bearing O-glycans that is related to galactose binding specificity reported for many lectins from marine sponges, such as CauL from Craniella australiensis (Xiong et al, 2006), Halilectin 2 and Halilectin 3 from Haliclona caerulea (Carneiro et al, 2013a(Carneiro et al, , 2013b, HpL from H. panicea (Kamiya et al, 1990), ACL-II from A. corrugata (Dresch et al, 2012), HcL from Haliclona crater (Pajic et al, 2002) and AaL from A. archeri (Miarons, Fresno, 2000). Table 3.…”

Section: Carbohydrate-binding Specificitymentioning

confidence: 99%

Characterization of the C-type lectin from the marine sponge (Stylissa flexibilis)

Hung

Trung²

2020

Vietnam J. Biotechnol.

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A lectin from the marine sponge Stylissa flexibilis, designated as SFL, 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 32 kDa subunits linked by a disulfide bridge with a molecular mass of 64 kDa by SDS-PAGE and 65 kDa by Sephacryl S-200 gel filtration chromatography. The lectin preferentially agglutinated enzyme treated human A erythrocytes, whereas it did not agglutinate any type of rabbit, human B and O erythrocytes, irrespective of treatment with enzymes. The hemagglutination activity of lectin was strongly inhibited by monosaccharide, D-galactose and glycoproteins, asialo-porcine stomach mucin and asialo-fetuin, indicating that lectin is specific for O-glycans. Activity of SFL was stable over a range of pH from 5 to 8, up to 60 °C for 30 min and its activity was Ca2+ dependent, indicating that SFL was belonged to the C-type lectin family and requires metal for biological activity. SFL caused agglutination of Vibrio alginolyticus and V. parahaemolyticus in a dose dependent manner and inhibited the growth rate of these bacterial strains, suggesting that the lectin caused the agglutination through binding to the target receptor(s) on the surface of Vibrios. Thus, SFL can be considered as a good source of lectin(s) being useful as carbohydrate probe and antibacterial reagent.

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Section: Carbohydrate-binding Specificitymentioning

confidence: 99%

Characterization of the C-type lectin from the marine sponge (Stylissa flexibilis)

Hung

Trung²

2020

Vietnam J. Biotechnol.

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“…Futhermore, inhibition by asialofetuin has been evidenced for lectins from marine sponges, such as HOL-30 from H. okadai (Kawsar et al, 2008) and HcL from Haliclona cratera (Pajic et al, 2002). On the other hand, inhibition by porcine stomatch mucin and their asialo derivatives bearing O-glycans that is related to galactose binding specificity has been reported for many lectins from marine sponges, such as CauL from Craniella australiensis (Xiong et al, 2006), Halilectin 2 and Halilectin 3 from Haliclona caerulea (Carneiro et al, 2013a(Carneiro et al, , 2013b, ACL-II from A. corrugata (Dresch et al, 2012), HcL from Haliclona crater (Pajic et al, 2002) and AaL from A. archeri (Miarons, Fresno, 2000).The inhibition profiles with monosaccharides and glycoproteins were different depending on marine sponge species.…”

Section: Carbohydrate Binding Specificitiesmentioning

confidence: 99%

Haemagglutination activity of lectins from extracts of some Vietnam marine sponges

Hung

Trung²

2020

Vietnam J. Biotechnol.

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Aqueous extracts from 16 species of Vietnam marine sponges were examined for haemagglutination activity using native and enzyme-treated different animal and human erythrocytes. Among these, extracts from 14 species were found to have haemagglutinination activities toward at least one type of erythrocyte tested meaning that 87.5% of the surveyed marine sponge species possess haemagglutination activity. Strong activity was detected in extracts from marine sponge species Acanthella cavernosa, Axinyssa sp., Cinachyrella sp., 01NT.2.4, 3.5, 3.10, 3.11 and 3.18 with enzyme-treated various animal and human erythrocytes. In a haemagglutination–inhibition test with various monosaccharides and glycoproteins, haemagglutination activity of the extract from A. cavernosa had no affinity for any of the monosaccharides, but inhibited by porcine stomach mucin and fetuin, whereas activities of the extract from Cinachyrella sp. were strongly inhibited by monosaccharides, such as D-galactose and N-acetyl-D-galatosamine, but not with glycoproteins. The activity of Stylissa flexibilis extract was inhibited by D-galactose, porcine stomach mucin, fetuin and their asialo derivatives, suggesting the presence of lectin specific for O-glycans of this species. The activities of four sponge extracts from A. cavernosa, S. flexibilis, Axinyssa sp. and Cinachyrella sp. were stable over a wide range of pH and temperature. Haemagglutination activities of A. cavernosa, Axinyssa sp. and Cinachyrella sp. extracts were independent of the presence of divalent cations, except for the haemagglutination activity of extract from S. flexibilis, which was dependent on the presence of divalent cations. The results suggest that Vietnam marine sponges may be good sources of useful lectins for biochemical and biomedical applications.

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“…Its primary structure shows no similarity to any other animal lectin and consists of 251 amino acids, of which 145 arrange themselves into an α-chain and 106 into two β-chains. Alongside, quaternary structure has a heterotrimer conformation stabilized by disulfide bonds [84], which differs from the dimeric [67], trimeric [85], tetrameric [86] or multimeric [87] structure of all other lectin originated from sponges characterized so far. H3 is able to promote cancer cell death exploiting different mechanisms.…”

Section: Phylum Poriferamentioning

confidence: 99%

Antitumor Potential of Marine and Freshwater Lectins

et al. 2019

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Often, even the most effective antineoplastic drugs currently used in clinic do not efficiently allow complete healing due to the related toxicity. The reason for the toxicity lies in the lack of selectivity for cancer cells of the vast majority of anticancer agents. Thus, the need for new potent anticancer compounds characterized by a better toxicological profile is compelling. Lectins belong to a particular class of non-immunogenic glycoproteins and have the characteristics to selectively bind specific sugar sequences on the surface of cells. This property is exploited to exclusively bind cancer cells and exert antitumor activity through the induction of different forms of regulated cell death and the inhibition of cancer cell proliferation. Thanks to the extraordinary biodiversity, marine environments represent a unique source of active natural compounds with anticancer potential. Several marine and freshwater organisms, ranging from the simplest alga to the most complex vertebrate, are amazingly enriched in these proteins. Remarkably, all studies gathered in this review show the impressive anticancer effect of each studied marine lectin combined with irrelevant toxicity in vitro and in vivo and pave the way to design clinical trials to assess the real antineoplastic potential of these promising proteins. It provides a concise and precise description of the experimental results, their interpretation as well as the experimental conclusions that can be drawn.

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H-3, a new lectin from the marine sponge Haliclona caerulea: Purification and mass spectrometric characterization

Cited by 31 publications

References 35 publications

Characterization of the C-type lectin from the marine sponge (Stylissa flexibilis)

Characterization of the C-type lectin from the marine sponge (Stylissa flexibilis)

Haemagglutination activity of lectins from extracts of some Vietnam marine sponges

Antitumor Potential of Marine and Freshwater Lectins

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