Purification and characterization of an N-acetylglucosamine specific lectin from marine bivalve Macoma birmanica

Adhya, Mausumi; Singha, Biswajit; Chatterjee, Bishnu P.

doi:10.1016/j.fsi.2008.11.001

Cited by 22 publications

(27 citation statements)

References 42 publications

(43 reference statements)

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“…The yield of lectin calculated per gram of crude mollusk mantle was 23 Pg/g. This result was comparable with that for lectins from other marine bivalve mollusks [8][9][10]. The exact lectin molecular weight determined by mass spectrometry was 16,492 Da.…”

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Isolation and general characteristics of lectin from the mussel Mytilus trossulus

et al. 2013

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Lectin (MTL) of molecular weight 16,492 Da and pI 6.09 ± 0.01 that was most active in the pH range 9.0-10.0, was thermally labile, and did not require Ca 2+ for activation was isolated from the mussel Mytilus trossulus. The MTL was a Gal/GalNAc-specific lectin that exhibited an affinity for glycoproteins containing mucin-type chains. The cross reactivity between MTL and a lectin isolated from the mussel Crenomytilus grayanus was determined. It was shown that MTL at high concentration stimulated expression of TNF-D and IFN-J; at low concentration, exhibited immunomodulating activity by reducing hyperexpression of cytokine IL-10.Lectins are proteins or glycoproteins that bind specifically and reversibly mono-and oligosaccharides and glycoconjugates without transforming them chemically. Lectins have now been observed in all biological taxa [1]. Marine invertebrates represent a comparatively new source of lectins. With respect to evolution, lectins of invertebrates are precursors of mammalian antibodies and form a primitive immune system. Furthermore, they exhibit antibacterial, cytotoxic, antitumor, mitogenic, and anti-HIV activities [2][3][4][5][6]. The goal of the present work was to isolate and study the physicochemical characteristics of lectin from the mussel Mytilus trossulus.This mussel is cultivated and widely distributed in the Far East. Proteins exhibiting hemagglutinating activity were observed previously in the mantle extract of this mollusk [7]. Therefore, the mantle of mussels collected in Troits Bay (Poset Gulf, Sea of Japan) was used to isolate lectin. Lectin was separated by affinity chromatography on porcine stomach mucin (PSM) and Sepharose. Lectin bound to the sorbent was eluted by Gal solution and purified by gel-permeation chromatography over Sephacryl S-200. A homogeneous protein of molecular weight ~18 kDa that was called MTL was obtained according to SDS-electrophoresis (in the presence and absence of E-mercaptoethanol).The lectin showed the greatest hemagglutinating activity in the reaction with trypsinized human group A erythrocytes. The yield of lectin calculated per gram of crude mollusk mantle was 23 Pg/g. This result was comparable with that for lectins from other marine bivalve mollusks [8][9][10]. The exact lectin molecular weight determined by mass spectrometry was 16,492 Da. The isoelectric point from capillary electrophoresis results was 6.09 ± 0.01. This was consistent with the aminoacid composition of the lectin. MTL contained a large number of non-polar amino acids (39.66%) and negatively charged amino acids (26.90%). The content of positively charged amino acids was insignificant (10.44%).The thermal stability and pH and metal dependences of the lectin were studied using hemagglutination (HA). The lectin exhibited the greatest hemagglutination titre in the pH range 9.0-10.0. The lectin activity fell by 25% at pH 6.0 and by 50% at pH 4.0. Furthermore, MTL was completely inactivated after incubation at 60°C for 30 min. Both metal-independent [8,9] and metal-dependent lectins wer...

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confidence: 83%

“…Furthermore, MTL was completely inactivated after incubation at 60°C for 30 min. Both metal-independent [8,9] and metal-dependent lectins were found among lectins of marine bivalve mollusks. The activity of the latter was manifested only in the presence of divalent metals [11,12].…”

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Isolation and general characteristics of lectin from the mussel Mytilus trossulus

et al. 2013

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“…11 The pattern of monosaccharide specificity of MBA as previously determined by hemagglutination-inhibition assay is in the order Me-bGlcNAc > Me-aGlcNAc > Me-aMan > Me-a/bGlc ) Gal, GalNAc. 11 It has been also noted that MBA interacted well with Nlinked glycans containing mammalian glycoproteins. Among the glycoproteins tested, MBA reacted strongly with complex type Nlinked glycans of thyroglobulin from porcine and bovine, and the propensity of binding was increased gradually with removal of sialic acid and galactose.…”

Section: Introductionmentioning

confidence: 84%

“…In our earlier communication, Macoma birmanica agglutinin (MBA), a monomeric antibacterial lectin of molecular weight 47 kDa, was isolated from marine bivalve M. birmanica. 11 It seemed to play a crucial role in host defense by specifically recognizing the surface-exposed GlcNAc residues of both Gram-positive and Gram-negative bacteria in a dose dependent manner, and was quite capable to suppress the in vitro bacterial growth. 11 The pattern of monosaccharide specificity of MBA as previously determined by hemagglutination-inhibition assay is in the order Me-bGlcNAc > Me-aGlcNAc > Me-aMan > Me-a/bGlc ) Gal, GalNAc.…”

Section: Introductionmentioning

confidence: 99%

“…11 It seemed to play a crucial role in host defense by specifically recognizing the surface-exposed GlcNAc residues of both Gram-positive and Gram-negative bacteria in a dose dependent manner, and was quite capable to suppress the in vitro bacterial growth. 11 The pattern of monosaccharide specificity of MBA as previously determined by hemagglutination-inhibition assay is in the order Me-bGlcNAc > Me-aGlcNAc > Me-aMan > Me-a/bGlc ) Gal, GalNAc. 11 It has been also noted that MBA interacted well with Nlinked glycans containing mammalian glycoproteins.…”

Section: Introductionmentioning

confidence: 99%

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