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.
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Acknowledgments
This work was supported by the Brazilian agencies CNPq (Conselho Nacional de Desenvolvimento Científico e Tecnológico), FUNCAP (Fundação Cearense de Apoio ao Desenvolvimento Científico e Tecnológico), and FINEP (Financiadora de Estudos e Projetos). The authors thank CETENE by the availability of the mass spectrometer, and, especially, the authors are grateful to Dr. Julia Campos for MALDI-ToF experiments. AHS, CSN, and OVS are senior investigators of CNPq.
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This work is dedicated in memory of Wladimir Ronald Lobo Farias.
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Chaves, R.P., da Silva, S.R., da Silva, J.P.F.A. et al. Meristiella echinocarpa lectin (MEL): a new member of the OAAH-lectin family. J Appl Phycol 30, 2629–2638 (2018). https://doi.org/10.1007/s10811-018-1473-7
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DOI: https://doi.org/10.1007/s10811-018-1473-7