A Simple Electrochemical System to Evaluate Interactions between Bauhinia monandra Leaf Lectin (BmoLL) and Cratylia mollis Seed Lectin (Cramoll) Immobilized in Nafion Nanopores with Pseudomonas aeruginosa Endophytic Strain

Souza, Sandra R. and Oliveira, Benny F. and Pimentel, Jadilma C. and Ramos, Sergio A. F. and Araújo, Janete M. and Napoleão, Thiago H. and Paiva, Patrícia Maria G. and Correia, Maria T. S. and Coelho, Luana Cassandra B. B. (2021) A Simple Electrochemical System to Evaluate Interactions between Bauhinia monandra Leaf Lectin (BmoLL) and Cratylia mollis Seed Lectin (Cramoll) Immobilized in Nafion Nanopores with Pseudomonas aeruginosa Endophytic Strain. In: Recent Research Advances in Biology Vol. 9. B P International, pp. 1-17. ISBN 978-93-91215-73-6

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Abstract

An electrochemical system evaluated the interaction of lectins immobilized in nanopores of Nafion with strains of Pseudomonas aeruginosa. Bauhinia monandra leaf lectin, BmoLL, specific for galactose, interacted with P. aeruginosa strain UFPEDA598, an endophytic bacterium isolated from B. monandra leaves. Cratylia mollis seed lectin, Cramoll, specific for glucose-mannose, did not bind to the endophytic strain, but recognized a pathogenic bacterium of P. aeruginosa, strain UFPEDA-39 (IT2633). BmoLL revealed high recognition of the UFPEDA598 endophytic bacterium strain; the result of this interaction was evidenced by an increase in electrochemical potential and stability in the presence of galactose, the lectin inhibitor, with a binding preference for endophytic membrane carbohydrates. Cramoll did not interact with the endophytic strain, since there was no variation in the electrochemical potential in relation to the control; however, the addition of glucose to the system promoted a lower potential, indicating the lectin preference for the monosaccharide. On the other hand, Cramoll showed high specificity for the membrane carbohydrates of P. aeruginosa strain UFPEDA-39 (IT2633); a decrease in the electrical potential was observed after the interaction, with stability to the glucose-inhibited lectin. We developed a simple, label-free system for recognizing microorganisms in real time. The biosensor clearly distinguished the glycoconjugate surfaces of P. aeruginosa from different environments and can be useful for the selective identification of strains of the same species. The electrochemical detection of lectin interconnections with microorganisms is relevant to unravel structural recognition mechanisms.

Item Type: Book Section
Subjects: STM Library > Biological Science
Depositing User: Managing Editor
Date Deposited: 26 Oct 2023 08:26
Last Modified: 26 Oct 2023 08:26
URI: http://open.journal4submit.com/id/eprint/2998

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