Structural analysis of Centrolobium tomentosum seed lectin with inflammatory activity

Almeida, Alysson Chaves; Osterne, Vinicius Jose Da Silva; Santiago, M.Q.; Pinto-Junior, Vanir Reis; Silva-Filho, J.C.; Lossio, Claudia Figueiredo; Nascimento, Francisco Lucas Faustino do; Almeida, R.P.H.; Teixeira, Claudener S.; Leal, Rodrigo Bainy; Delatorre, P.; Rocha, B.A.M.; Assreuy, Ana Maria Sampaio; Nascimento, Kyria S.; Cavada, Benildo S.

doi:10.1016/j.abb.2016.03.001

Cited by 30 publications

(9 citation statements)

References 47 publications

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“…On the other hand, those possessing binding affinity for N-acetylglucosamine present systemic anti-inflammatory effect, such as the lectins of Lonchocarpus sericeus (Alencar et al 2005, Napimoga et al 2007 and Lonchocarpus araripensis (Pires et al 2016). In addition, Dalbergiae lectins possessing binding affinity for mannose present pro-inflammatory and nociceptive effects, such as the lectins of Centrolobium tomentosum (Almeida et al 2016) and Platypodium elegans (Araripe et al 2017, Cavada et al 2018, except for the lectin of Andira anthelmia, which presents antinociceptive effect (Nascimento et al 2016).…”

Section: Introductionmentioning

confidence: 99%

Inhibitory effect of Lonchocarpus araripensis lectin in rat acute models of inflammation

Pires

Marques

Alencar

et al. 2019

An. Acad. Bras. Ciênc.

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Dalbergieae tribe lectins, possessing binding affinity for galactose and mannose, present inflammatory and nociceptive effects, while those for N-acetylglucosamine are anti-inflammatory. Since the anti-inflammatory effect of the seed lectin of L. araripensis (LAL) had been already demonstrated in mice, this effect was presently evaluated in rat models of acute inflammation. LAL (0.01-1 mg/kg) was administered by intravenous (i.v.) route in male Wistar rats 30 min before paw edema induction by dextran or carrageenan, and peritonitis by carrageenan. LAL (1 mg/kg) was incubated with N-acetylglucosamine for allowing lectin-sugar interactions before injection into animals. LAL toxicity was evaluated by the parameters: body mass, organs weight, stomach macroscopy, hematological and biochemical dosage. Statistical analysis was performed by ANOVA and Bonferroni's test (p<0.05). The paw edema induced by carrageenan (AUC: 0.96 ± 0.09) was inhibited by LAL about 39% (0-2 h) at all doses, and about 72% (3-5 h) at 0.1 and 1 mg/kg. The increase in the neutrophil migration stimulated by carrageenan was also inhibited by LAL (83%). In both models, LAL inhibitory effect was prevented by GlcNAc. The subchronic treatment with LAL was well tolerated by animals. LAL possesses anti-inflammatory effect via lectin domain, indicating potential modulator role in cellular inflammatory events.

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Section: Introductionmentioning

confidence: 99%

Inhibitory effect of Lonchocarpus araripensis lectin in rat acute models of inflammation

Pires

Marques

Alencar

et al. 2019

An. Acad. Bras. Ciênc.

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“…The single-chain protomers associate into homotetramers. Examples are the mannose-binding lectins characterized in the tribes Baphieae ( Bowringia mildbraedii agglutinin BMA) [17], Dalbergieae ( Centrolobium tomentosum lectin CTL [29], Pterocarpus angolensis lectin PAL [58]), Diocleae (Con A [23,157] (Figure 1C), Cymbosema roseum CRL [33], Dioclea grandiflora lectin Con GF [25], and other Dioclea sp. lectins).…”

Section: Structural Organization Of the Plant Algal And Fungal Mamentioning

confidence: 99%

Overview of the Structure–Function Relationships of Mannose-Specific Lectins from Plants, Algae and Fungi

Barre

Bourne

Damme

et al. 2019

IJMS

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To date, a number of mannose-binding lectins have been isolated and characterized from plants and fungi. These proteins are composed of different structural scaffold structures which harbor a single or multiple carbohydrate-binding sites involved in the specific recognition of mannose-containing glycans. Generally, the mannose-binding site consists of a small, central, carbohydrate-binding pocket responsible for the “broad sugar-binding specificity” toward a single mannose molecule, surrounded by a more extended binding area responsible for the specific recognition of larger mannose-containing N-glycan chains. Accordingly, the mannose-binding specificity of the so-called mannose-binding lectins towards complex mannose-containing N-glycans depends largely on the topography of their mannose-binding site(s). This structure–function relationship introduces a high degree of specificity in the apparently homogeneous group of mannose-binding lectins, with respect to the specific recognition of high-mannose and complex N-glycans. Because of the high specificity towards mannose these lectins are valuable tools for deciphering and characterizing the complex mannose-containing glycans that decorate both normal and transformed cells, e.g., the altered high-mannose N-glycans that often occur at the surface of various cancer cells.

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“…However, like other viciae lectins, they possess two identical mannose-binding sites. They also differ from the single-chain legume lectins, which result from the non-covalent association of four protomers to give homotetrameric mannose-binding lectins occurring in the tribes Baphieae ( Bowringia mildbraedii agglutinin BMA) [34], Dalbergieae ( Centrolobium tomentosum lectin CTL [35], Pterocarpus angolensis lectin PAL [36]), Diocleae (Con A [37], Cymbosema roseum CRL [38], Dioclea grandiflora lectin Con GF [39], and other Dioclea sp. lectins), which exhibit four mannose-binding sites.…”

Section: Structural Scaffolds Of the Man-specific Seaweed Lectinsmentioning

confidence: 99%

Mannose-Specific Lectins from Marine Algae: Diverse Structural Scaffolds Associated to Common Virucidal and Anti-Cancer Properties

et al. 2019

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To date, a number of mannose-specific lectins have been isolated and characterized from seaweeds, especially from red algae. In fact, man-specific seaweed lectins consist of different structural scaffolds harboring a single or a few carbohydrate-binding sites which specifically recognize mannose-containing glycans. Depending on the structural scaffold, man-specific seaweed lectins belong to five distinct structurally-related lectin families, namely (1) the griffithsin lectin family (β-prism I scaffold); (2) the Oscillatoria agardhii agglutinin homolog (OAAH) lectin family (β-barrel scaffold); (3) the legume lectin-like lectin family (β-sandwich scaffold); (4) the Galanthus nivalis agglutinin (GNA)-like lectin family (β-prism II scaffold); and, (5) the MFP2-like lectin family (MFP2-like scaffold). Another algal lectin from Ulva pertusa, has been inferred to the methanol dehydrogenase related lectin family, because it displays a rather different GlcNAc-specificity. In spite of these structural discrepancies, all members from the five lectin families share a common ability to specifically recognize man-containing glycans and, especially, high-mannose type glycans. Because of their mannose-binding specificity, these lectins have been used as valuable tools for deciphering and characterizing the complex mannose-containing glycans from the glycocalyx covering both normal and transformed cells, and as diagnostic tools and therapeutic drugs that specifically recognize the altered high-mannose N-glycans occurring at the surface of various cancer cells. In addition to these anti-cancer properties, man-specific seaweed lectins have been widely used as potent human immunodeficiency virus (HIV-1)-inactivating proteins, due to their capacity to specifically interact with the envelope glycoprotein gp120 and prevent the virion infectivity of HIV-1 towards the host CD4+ T-lymphocyte cells in vitro.

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Structural analysis of Centrolobium tomentosum seed lectin with inflammatory activity

Cited by 30 publications

References 47 publications

Inhibitory effect of Lonchocarpus araripensis lectin in rat acute models of inflammation

Inhibitory effect of Lonchocarpus araripensis lectin in rat acute models of inflammation

Overview of the Structure–Function Relationships of Mannose-Specific Lectins from Plants, Algae and Fungi

Mannose-Specific Lectins from Marine Algae: Diverse Structural Scaffolds Associated to Common Virucidal and Anti-Cancer Properties

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