Purification and partial characterization of an agglutinin from Octopus maya serum

Alpuche, Juan; Pereyra, Ali; Mendoza‐Hernández, Guillermo; Agundis, Concepción; Rosas, Carlos; Zenteno, Edgar

doi:10.1016/j.cbpb.2010.01.006

Cited by 32 publications

(18 citation statements)

References 28 publications

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“…A selective affinity for Gal and Gal-derived sugars was reported not only for lectins from other Pomacea snails (egg lectins from P. urceus and P. flagellata , [23] and adult body lectins from P. flagellata [20]), but also from other snails like Achatina [31]. As a whole, these results agree with previous studies suggesting that lectin specificity in molluscs is relatively conserved for galactosides [32].…”

Section: Discussionsupporting

confidence: 91%

Agglutinating Activity and Structural Characterization of Scalarin, the Major Egg Protein of the Snail Pomacea scalaris (d’Orbigny, 1832)

et al. 2012

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Apple snail perivitellins are emerging as ecologically important reproductive proteins. To elucidate if the protective functions of the egg proteins of Pomacea canaliculata (Caenogastropoda, Ampullariidae), involved in embryo defenses, are present in other Pomacea species we studied scalarin (PsSC), the major perivitellin of Pomacea scalaris. Using small angle X-ray scattering, fluorescence and absorption spectroscopy and biochemical methods, we analyzed PsSC structural stability, agglutinating activity, sugar specificity and protease resistance. PsSC aggluttinated rabbit, and, to a lesser extent, human B and A erythrocytes independently of divalent metals Ca2+ and Mg2+ were strongly inhibited by galactosamine and glucosamine. The protein was structurally stable between pH 2.0 to 10.0, though agglutination occurred only between pH 4.0 to 8.0 (maximum activity at pH 7.0). The agglutinating activity was conserved up to 60°C and completely lost above 80°C, in agreement with the structural thermal stability of the protein (up to 60°C). PsSC was able to withstand in vitro gastrointestinal digestion, and showed no trypsin inhibition activity. The presence of lectin activity has been reported in eggs of other Pomacea snails, but here we link for the first time, this activity to an apple snail multifunctional perivitellin. This novel role for a snail egg storage protein is different from closely related P.canaliculata defensive proteins.

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Section: Discussionsupporting

confidence: 91%

Agglutinating Activity and Structural Characterization of Scalarin, the Major Egg Protein of the Snail Pomacea scalaris (d’Orbigny, 1832)

et al. 2012

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“…Cancer antennarius Stimpson, 1856 and Liocarcinus depurator (Linnaeus, 1758), possess specificity for NeuAc and O-acetyl-sialic residues (Vázquez et al, 2009). The lectins from other invertebrate taxa, such as oysters {Crassostrea virginica (Gmelin, 1791)) and mussel {Mytilus edulis Linnaeus, 1758) (MoUusca, Bivalvia) show specificity for GlcNAc (Vasta et al, 1984;Takagi et al, 1994); Achatina fúlica (Femssac, 1821) and Helix pomatia Linnaeus, 1758 (MoUusca, Gastropoda) are specific for 0-acetylated and Nacetylated sugar residues, respectively (Hammarstrom et al, 1977;Biswas et al, 2000), agglutinin from Octopus maya Voss & Solis Ramirez, 1966 (MoUusca, Cephalopoda) semm showed specificity for galactosamine and methyl alpha and beta galactosides (Alpuche et al, 2010). MaL showed common epitopes with the lectin from M. rosenbergii, since the MaL 86.6 and 66.2 kDa subunits are recognized by monoclonal antibodies against M. rosenbergii lectin.…”

Section: Discussionmentioning

confidence: 99%

Purification and partial characterization of a lectin from the prawn Macrobrachium americanum (Decapoda, Palaemonidae)

Agundis¹,

Pereyra²,

Sáinz³

et al. 2012

Crustac

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Lectins play relevant roles in the innate immunity of invertebrates. From the haemolymph of the prawn Macrobrachium americanum Spence Bate, 1868 we purified by affinity chromatography a lectin (MaL) composed of three subunits (86,6, 66,2 and 42,7 kDa), as identified by SDS-PAGE, It is mainly composed of Gly, Ser and Arg, and Ala, Glx and Lys in a minor proportion; it lacks Trp, Cys and carbohydrates, MaL agglutinated mainly rat erythrocytes, rabbit or mouse erythrocytes were agglutinated with lower capacity; whereas erythrocytes from human or other species were not agglutinated. It is specific for N-acetyl-neuraminic acid (sialic acid), N-acetyl-D-glucosamine and N-acetyl-D-galactosamine; sialylated fetuin and bovine submaxillary mucin are also powerful inhibitors of the lectin's activity. After physical daily manipulation of prawns for 7 days, the lectin concentration and the specific activity (haemagglutinating activity/protein concentration) increased more than four-fold over the control group (those animals that had not been manipulated until bleeding), suggesting that increased lectin concentration and activity after manipulation could be considered as markers of stress.

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“…The stroma-Sephadex chromatography efficiently isolated H-1 that was bound to the resin and was eluted from the affinity matrix in an apparently pure form by the addition of 0.3% NH 4 OH. Stroma is a very useful affinity support for the isolation of animal lectins, such as AcL-I, a lectin from the marine sponge Axinella corrugata (Dresch et al, 2008), and OmA, an agglutinin from the mollusk Octopus maia (Alpuche et al, 2010). H-1 corresponded to 26% of the total HA present in the crude extract.…”

Section: Discussionmentioning

confidence: 99%

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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Purification and partial characterization of an agglutinin from Octopus maya serum

Cited by 32 publications

References 28 publications

Agglutinating Activity and Structural Characterization of Scalarin, the Major Egg Protein of the Snail Pomacea scalaris (d’Orbigny, 1832)

Agglutinating Activity and Structural Characterization of Scalarin, the Major Egg Protein of the Snail Pomacea scalaris (d’Orbigny, 1832)

Purification and partial characterization of a lectin from the prawn Macrobrachium americanum (Decapoda, Palaemonidae)

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

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