Please use this identifier to cite or link to this item: http://repositorio.ufc.br/handle/riufc/73814
Type: Artigo de Periódico
Title: Meristiella echinocarpa lectin (MEL): a new member of the OAAH-lectin family
Authors: Chaves, Renata Pinheiro
Silva, Suzete Roberta da
Silva, João Pedro Freire Alves da
Carneiro, Rômulo Farias
Sousa, Bruno Lopes de
Carvalho, Fátima Cristiane Teles de
Farias, Wladimir Ronald Lobo
Sousa, Oscarina Viana de
Silva, André Luiz Coelho
Sampaio, Alexandre Holanda
Nagano, Celso Shiniti
Keywords: Lectin;Species - Rhodophyta;Pathogenic bacteria;Lecitina;Espécie - Rhodophyta;Bactérias patogênicas
Issue Date: 2018
Publisher: Journal of Applied Phycology
Citation: CHAVES, Renata Pinheiro; SILVA, Suzete Roberta da; SILVA, João Pedro Freire Alves da; CARNEIRO, Rômulo Farias; SOUSA, Bruno Lopes de; ABREU, Jade Oliveira; CARVALHO, Fátima Cristiane Teles de; ROCHA, Cintia Renata Costa; FARIAS, Wladimir Ronald Lobo; SOUSA, Oscarina Viana de; SILVA, André Luiz Coelho; SAMPAIO, Alexandre Holanda Sampaio; NAGANO, Celso Shiniti. Meristiella echinocarpa lectin (MEL): a new member of the OAAH-lectin family. Journal of Applied Phycology , Germany, v. 128, p. 87-92, 2018. Disponível em: https://doi.org/10.1007/s10811-018-1473-7. Acesso em:03 ago 2023.
Abstract: A new lectin from the marine red alga Meristiella echinocarpa (MEL) was isolated and biochemically characterized. MEL is a monomeric protein of 28 kDa with specificity for yeast mannan. Hemagglutination activity of MEL was stable between pH 5 and 10, temperatures up to 50 °C, and neither EDTA nor divalent ions affected it. The complete amino acid sequence of MEL was determined through a combination of tandem mass spectrometry and DNA cloning. As a new member of the OAAH-lectin family, the primary structure of MEL consists of 267 amino acid residues distributed in four tandem repeat domains, sharing at least 48% of identity. Theoretical secondary structure of MEL was composed of 3% α-helix, 40% β-sheet, 19% β-turn, and 38% coil. Melting temperatures of the lectin in the absence and presence of mannan were 54 and 61 °C, respectively. Furthermore, MEL was able to recognize and agglutinate pathogenic bacterial strains, such as multidrug-resistant Salmonella and Vibrio alginolyticus. Keywords . . OAAH-family . Pathogenic bacteria
URI: 0177-5103
http://www.repositorio.ufc.br/handle/riufc/73814
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