Biological activities of ACL-I and physicochemical properties of ACL-II, lectins isolated from the marine sponge Axinella corrugata

Dresch, Roger Remy; Lerner, Cléa; Mothes, Beatriz; Trindade, Vera Maria Treis; Henriques, Amélia T.; Vozari-Hampe, Magdolna M.

doi:10.1016/j.cbpb.2012.01.001

Cited by 15 publications

(17 citation statements)

References 43 publications

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“…Similar to lectins isolated from Haliclona caerulea (Carneiro et al 2013), Axinella corrugata (Dresch et al 2011) and Aplysia kurodai (Kawsar et al 2010), HGL showed a high level of cytotoxicity against Artemia nauplii. However, hemolysis caused by lectin is rare, and few lectins have shown hemolytic activity (Hatakeyama et al 1994, Sudhakar andVincent 2014).…”

Section: Discussionmentioning

confidence: 99%

Hemagglutinating/Hemolytic activities in extracts of marine invertebrates from the Brazilian coast and isolation of two lectins from the marine sponge Cliona varians and the sea cucumber Holothuria grisea

Moura

Melo

Carneiro

et al. 2015

An. Acad. Bras. Ciênc.

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Twenty species of marine invertebrates from the Brazilian coast were screened for hemagglutinating/ hemolytic activity. In at least twelve tested species, hemagglutinating activity was different for different blood types, suggesting the presence of lectins. Extracts from four species showed hemolytic activity. Two new lectins were purified from the marine sponge Cliona varians (CvL-2) and sea cucumber Holothuria grisea (HGL). CvL-2 was able to agglutinate rabbit erythrocytes and was inhibited by galactosides. The hemagglutinating activity was optimal in pH neutral and temperatures below 70 °C. CvL-2 is a trimeric protein with subunits of 175 kDa. On the other hand, HGL showed both hemagglutinating and hemolytic activity in human and rabbit erythrocytes, but hemolysis could be inhibited by osmotic protection, and agglutination was inhibited by mucin. HGL was stable in pH values ranging from 4 to 10 and temperatures up to 90 °C. In electrophoresis and gel filtration, HGL was a monomeric protein with 15 kDa. CvL-2 and HGL showed different levels of toxicity to Artemia naplii. CvL-2 showed LC 50 of 850.1 μg/mL, whereas HGL showed LC 50 of 9.5 µg/mL.

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Section: Discussionmentioning

confidence: 99%

Hemagglutinating/Hemolytic activities in extracts of marine invertebrates from the Brazilian coast and isolation of two lectins from the marine sponge Cliona varians and the sea cucumber Holothuria grisea

Moura

Melo

Carneiro

et al. 2015

An. Acad. Bras. Ciênc.

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“…Currently, only one sponge lectin, AcL‐I, has been tested for toxicity toward A. salina . This lectin exhibited a high cytotoxic activity similar to that of H‐1 (Dresch et al ., ). These results suggest that H. caerulea lectins might play a role in the physiological defense of the sponge.…”

Section: Discussionmentioning

confidence: 97%

Halilectin 1 (H‐1) and Halilectin 2 (H‐2): two new lectins isolated from the marine sponge Haliclona caerulea

Carneiro

Melo

Nascimento

et al. 2012

J of Molecular Recognition

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Two new lectins named Halilectin 1 (H-1) and Halilectin 2 (H-2) were isolated from the marine sponge Haliclona caerulea using a combination of affinity chromatography on stroma fixed onto Sephadex G-25 and cation and anion exchange chromatography. H-1 is a monomeric protein with a molecular mass of 40 kDa estimated using sodium dodecyl sulfate polyacrylamide gel electrophoresis and 15 kDa estimated using a TSK gel. Conversely, H-2 is a homodimeric protein with 15 kDa monomers linked via weak interactions. H-1 more effectively agglutinates trypsinized rabbit erythrocytes, whereas H-2 more effectively agglutinates native rabbit erythrocytes. The hemagglutinating activity of H-1 could be not inhibited by any tested sugars, but H-2 was inhibited by orosomucoid and porcine stomach mucin. Neither lectin was dependent on divalent ions. H-1 was stable at basic pH range and temperatures up to 50 °C, whereas H-2 was stable at acid pH range and temperatures up to 80 °C. The H. caerulea lectins exhibited dose-dependent toxicity against Artemia nauplii. Additionally, 76% of the primary structure of H-2 was determined using tandem mass spectrometry to contain a unique amino acid sequence with no similarity to any members of the animal lectin family.

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“…Due to the strong affinity of sponge lectins for galactoside residues, sepharose or lactose-conjugated matrices were often selected [ 61 , 62 ]. By using affinity chromatography with rabbit erythrocyte stroma followed by a gel filtration on Ultrogel AcA 44 column, the Axinella corrugata (George and Wilson, 1919) lectins-I and -II (AcL-I and -II) were purified [ 53 , 63 ]. Sometimes, a specific antibody directed against lectins was fixed onto a column in order to retain the lectins, as illustrated with the Cinachyrella apion (Uliczka, 1929) lectin (CaL), which was purified by using an antibody directed against the Cliona varians (Duchassaing and Michelotti 1864) lectin (CvL) [ 59 , 60 ].…”

Section: Sponge Lectin Purification Sequencing and Expressionmentioning

confidence: 99%

“…By using this method, both A. corrugata lectin-I and -II (AcL-I and AcL-II) were purified from the sponge A. corrugata . Their relative molecular weights were estimated by gel filtration as 78.5 and 80 kDa, respectively [ 53 , 63 ]. Some lectins were precipitated by using carbohydrates conjugated to poly[ N -(2-hydroxy-ethyl)acrylamide] after affinity chromatography [ 55 ].…”

Section: Sponge Lectin Purification Sequencing and Expressionmentioning

confidence: 99%

Porifera Lectins: Diversity, Physiological Roles and Biotechnological Potential

et al. 2015

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An overview on the diversity of 39 lectins from the phylum Porifera is presented, including 38 lectins, which were identified from the class of demosponges, and one lectin from the class of hexactinellida. Their purification from crude extracts was mainly performed by using affinity chromatography and gel filtration techniques. Other protocols were also developed in order to collect and study sponge lectins, including screening of sponge genomes and expression in heterologous bacterial systems. The characterization of the lectins was performed by Edman degradation or mass spectrometry. Regarding their physiological roles, sponge lectins showed to be involved in morphogenesis and cell interaction, biomineralization and spiculogenesis, as well as host defense mechanisms and potentially in the association between the sponge and its microorganisms. In addition, these lectins exhibited a broad range of bioactivities, including modulation of inflammatory response, antimicrobial and cytotoxic activities, as well as anticancer and neuromodulatory activity. In view of their potential pharmacological applications, sponge lectins constitute promising molecules of biotechnological interest.

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Biological activities of ACL-I and physicochemical properties of ACL-II, lectins isolated from the marine sponge Axinella corrugata

Cited by 15 publications

References 43 publications

Hemagglutinating/Hemolytic activities in extracts of marine invertebrates from the Brazilian coast and isolation of two lectins from the marine sponge Cliona varians and the sea cucumber Holothuria grisea

Hemagglutinating/Hemolytic activities in extracts of marine invertebrates from the Brazilian coast and isolation of two lectins from the marine sponge Cliona varians and the sea cucumber Holothuria grisea

Halilectin 1 (H‐1) and Halilectin 2 (H‐2): two new lectins isolated from the marine sponge Haliclona caerulea

Porifera Lectins: Diversity, Physiological Roles and Biotechnological Potential

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