E H Teixeira

Publications (8)16.74 Total impact

• Source

  Available from: Marcelo H Napimoga

  Dataset: Lectina alga

  E H Teixeira, M H Napimoga, V A Carneiro, T M de Oliveira, K S Nascimento, C S Nagano, J B Souza, A Havt, V P T Pinto, R B Gonçalves, W R L Farias, S Saker-Sampaio, A H Sampaio, B S Cavada
• Article: Antifungal and marker effects of Talisia esculenta lectin on Microsporum canis in vitro

  A.Q. Pinheiro, D.F. Melo, L.M. Macedo, M.G.M. Freire, M.F.G. Rocha, J.J.C. Sidrim, R.S.N. Brilhante, E.H. Teixeira, C.C. Campello, D.C.S.N. Pinheiro, M.G.S. Lima
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  ABSTRACT: Aims:  The purpose of this study was to demonstrate the usefulness of lectin obtained from Talisia esculenta (TEL) seeds as a tool to recognize and study Microsporum canis. For this purpose, we investigated the antifungal and marker action of this lectin and the relationship of these effects with the presence of carbohydrates on the structure of this fungus.Methods and Results:  The in vitro antifungal activity of TEL was analysed by broth microdilution assay. In addition, TEL was assessed against the arthroconidia present on hairs obtained from infected dogs and cats. The affinity of fluorescein isothiocyanate (FITC)-labelled TEL for macroconidia and arthroconidia of M. canis was also tested. The effects of TEL on the growth of the M. canis strains began with 0·125 mg ml−1, and 100% inhibition was obtained with a concentration of 2 mg ml−1. The addition of carbohydrates, especially N-acetyl-glucosamine and d-mannose, inhibited these antifungal effects. TEL was able to inhibit the growth of arthroconidial chitin-rich forms of M. canis obtained from hairs of infected animals and strains cultured in Sabouraud agar. FITC-labelled TEL efficiently marked macroconidial and arthroconidial forms of M. canis, as shown by fluorescent microscopy.Conclusions:  These results show that the inhibitory effects of TEL on M. canis growth may be related to the interaction of lectin with the carbohydrates present at the micro-organism’s surface, mainly d-mannose and N-acetyl-glucosamine.Significance and Impact of the Study: Talisia esculenta can be used as an important tool in the biochemical study of M. canis or as a molecule to recognize this dermatophyte in infected tissue.
  Journal of Applied Microbiology 11/2009; 107(6):2063 - 2069. · 2.34 Impact Factor
• Article: Antifungal and marker effects of Talisia esculenta lectin on Microsporum canis in vitro.

  A Q Pinheiro, D F Melo, L M Macedo, M G M Freire, M F G Rocha, J J C Sidrim, R S N Brilhante, E H Teixeira, C C Campello, D C S N Pinheiro, M G S Lima
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  ABSTRACT: The purpose of this study was to demonstrate the usefulness of lectin obtained from Talisia esculenta (TEL) seeds as a tool to recognize and study Microsporum canis. For this purpose, we investigated the antifungal and marker action of this lectin and the relationship of these effects with the presence of carbohydrates on the structure of this fungus. The in vitro antifungal activity of TEL was analysed by broth microdilution assay. In addition, TEL was assessed against the arthroconidia present on hairs obtained from infected dogs and cats. The affinity of fluorescein isothiocyanate (FITC)-labelled TEL for macroconidia and arthroconidia of M. canis was also tested. The effects of TEL on the growth of the M. canis strains began with 0.125 mg ml(-1), and 100% inhibition was obtained with a concentration of 2 mg ml(-1). The addition of carbohydrates, especially N-acetyl-glucosamine and d-mannose, inhibited these antifungal effects. TEL was able to inhibit the growth of arthroconidial chitin-rich forms of M. canis obtained from hairs of infected animals and strains cultured in Sabouraud agar. FITC-labelled TEL efficiently marked macroconidial and arthroconidial forms of M. canis, as shown by fluorescent microscopy. These results show that the inhibitory effects of TEL on M. canis growth may be related to the interaction of lectin with the carbohydrates present at the micro-organism's surface, mainly D-mannose and N-acetyl-glucosamine. Talisia esculenta can be used as an important tool in the biochemical study of M. canis or as a molecule to recognize this dermatophyte in infected tissue.
  Journal of Applied Microbiology 06/2009; 107(6):2063-9. · 2.34 Impact Factor
• Source

  Available from: Marcelo H Napimoga

  Article: In vitro inhibition of oral streptococci binding to the acquired pellicle by algal lectins.

  E H Teixeira, M H Napimoga, V A Carneiro, T M de Oliveira, K S Nascimento, C S Nagano, J B Souza, A Havt, V P T Pinto, R B Gonçalves, W R L Farias, S Saker-Sampaio, A H Sampaio, B S Cavada
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  ABSTRACT: The initial colonization of the tooth by streptococci involves their attachment to adsorbed components of the acquired pellicle. Avoiding this adhesion may be successful in preventing caries at early stages. Salivary mucins are glycoproteins that when absorbed onto hydroxyapatite may provide binding sites for certain bacteria. Algal lectins may be especially interesting for oral antiadhesion trials because of their great stability and high specificity for mucins. This work aimed to evaluate the potential of two algal lectins to inhibit the adherence of five streptococci species to the acquired pellicle in vitro. The lectins used were extracted from Bryothamnion triquetrum (BTL) and Bryothamnion seaforthii (BSL). Fluorescence microscopy was applied to visualize the ability of fluorescein isothiocyanate-labelled lectins to attach to the pellicle and revealed a similar capability for both lectins. Streptococcal adherence assays were performed using saliva-coated microtitre plates. BSL inhibited more than 75% of Streptococcus sanguis, Streptococcus mitis, Streptococcus sobrinus and Streptococcus mutans adherence, achieving 92% to the latter. BTL only obtained statistically significant results on S. mitis and S. sobrinus, whose adherence was decreased by 32.5% and 54.4%, respectively. Algal lectins are able to inhibit streptococcal adherence. Our results support the proposed application of lectins in antiadhesion therapeutics.
  Journal of Applied Microbiology 11/2007; 103(4):1001-6. · 2.34 Impact Factor
• Source

  Available from: Marcelo H Napimoga

  Article: In vitro inhibition of Streptococci binding to enamel acquired pellicle by plant lectins.

  E H Teixeira, M H Napimoga, V A Carneiro, T M de Oliveira, R M S Cunha, A Havt, J L Martins, V P T Pinto, R B Gonçalves, B S Cavada
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  ABSTRACT: Initial colonization of the tooth surface by streptococci involves the attachment of these bacteria to adsorbed salivary components of the acquired pellicle. In dental biofilm this adhesion may also involve lectin-like components, present on the surface of the organisms, which bind to complementary carbohydrates on the surface of the tooth. Therefore, this work aimed to evaluate the potential of six lectins, extracted from seeds of Leguminosae family members, to inhibit the adherence of five streptococci species to acquired pellicle in vitro. The lectins used in this work were extracted from Canavalia ensiformis, Canavalia brasiliensis, Dioclea violacea, Dioclea grandiflora, Cratylia floribunda and Vatairea macrocarpa. Fluorescence micrography was employed to visualize the ability of FITC-labeled lectins to attach to acquire pellicle. Adherence inhibition was performed on saliva-coated microtiter plates at which lectins solutions were previously incubated followed by incubation with the oral streptococci. Glucose-mannose specific lectins attached to acquired pellicle with high intensity, while galactose specific lectins, from V. macrocarpa, exhibits low intensity attachment. All lectins were able to inhibit the adherence of the microorganisms tested (p < 0.01). Our results suggest that lectins may be useful in anti adhesion therapeutics.
  Journal of Applied Microbiology 07/2006; 101(1):111-6. · 2.34 Impact Factor
• Article: Glucose-mannose-binding lectins isolated from Brazilian beans stimulate the autophosphorylation of the insulin receptor in vitro.

  B S Cavada, M M Iglesias, M F Troncoso, E H Teixeira, D Turyn, F P Dominici
  Hormone and Metabolic Research 03/2003; 35(2):125-7. · 2.19 Impact Factor
• Article: Purification and partial characterization of a lectin from Canavalia grandiflora benth. seeds.

  V M Ceccatto, B S Cavada, E P Nunes, N A P Nogueira, M B Grangeiro, F B M B Moreno, E H Teixeira, A H Sampaio, M A O Alves, M V Ramos, J J Calvete, T B Grangeiro
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  ABSTRACT: A D-glucose/D-mannose specific lectin from seeds of Canavalia grandiflora (ConGF) was purified by affinity chromatography on Sephadex G-50. By SDS-PAGE ConGF yielded three protein bands with apparent molecular masses of 29-30 kDa (alpha chain), 16-18 kDa (beta fragment) and 12-13 kDa (gamma fragment), like other related lectins from the genus Canavalia (Leguminosae). ConGF strongly agglutinates rabbit erythrocytes, has a high content of ASP and SER, and its N-terminal sequence (30 residues) is highly similar to the sequences of other related lectins from subtribe Diocleinae.
  Protein and Peptide Letters 03/2002; 9(1):67-73. · 1.94 Impact Factor
• Source

  Available from: Benildo Cavada

  Article: Leguminous lectins as tools for studying the role of sugar residues in leukocyte recruitment.

  N M Alencar, E H Teixeira, A M Assreuy, B S Cavada, C A Flores, R A Ribeiro
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  ABSTRACT: The natural physiological ligands for selectins are oligosaccharides found in glycoprotein or glycolipid molecules in cell membranes. In order to study the role of sugar residues in the in vivo lectin anti-inflammatory effect, we tested three leguminous lectins with different carbohydrate binding affinities in the peritonitis and paw oedema models induced by carrageenin in rats. L. sericeus lectin was more anti-inflammatory than D. virgata lectin, the effects being reversed by their specific binding sugars (N-acetylglucosamine and alpha-methylmannoside, respectively). However, V. macrocarpa, a galactose-specific lectin, was not anti-inflammatory. The proposed anti-inflammatory activity of lectins could be due to a blockage of neutrophil-selectin carbohydrate ligands. Thus, according to the present data, we suggest an important role for N-acetylglucosamine residue as the major ligand for selectins on rat neutrophil membranes.
  Mediators of Inflammation 02/1999; 8(2):107-13. · 3.26 Impact Factor