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2 Polish Journal of Microbiology

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Optical lectin based biosensor as tool for bacteria identification

100%

Masarova J. , Szwajcer Dey E. , Danielsson B.

nr Suppl.

Biosensor techniques are based on biospecific interaction between the biological parts of biosensor with the analyte. In biosensor construction, antibodies are usually used for the detection of analytes such as microorganism, because of very strong and highly specific interaction. The disadvantages of this assay are a long time needed for antibody isolation and purification as well as difficult regeneration of biosensor chip. The use of lectins instead of antibodies could solve these problems because a several hundred lectins are commercially available and their stability in standard buffers is better compared to monoclonal antibodies. While antibody can only be used to detect that antigen it was designed for, lectin as low affinity molecule may bind several different pathogens. Using the discriminative effect of an artificial neural network the application of a lectin array will compensate for the lower specificity. Microbial surfaces bear many of the sugar residues capable of interacting with lectins. The ability of lectins to react with microbial glycoconjugates means that it is possible to employ them as probes and sorbents for whole cells, mutants and numerous cellular constituents and metabolites, and it makes them useful tools for identification or typing of bacteria. Lectins are attractive reagents for the clinical diagnostic laboratory because of their diverse specificity, commercial availability, a wide range of molecular weights, and their stability in standard buffers. The construction of lectin biosensor could be an advantage method for detection of pathogenic bacteria.

The cytotoxic and genotoxic effects of conjugated trans-2-nonenal [T2N], an off-flavor compound in beer and-heat processed food arising from lipid oxidation

75%

Szwajcer D. E. , Staniszewska M. , Pasciak M. , Konopacka M. , Rogolinski J. , Gamian A. , Danielsson B.

nr Suppl.

This study investigates the toxic effect of E(2)nonenal (trans-2-nonenal, T2N) and its conjugate with horse muscle myoglobin (Mb) tested on murine cell line L₉₂₉ and human cell line A₅₄₉, as well as the genotoxic effect of these compounds assayed by measuring of micronuclei in human cells K₅₆₂. It is an aldehyde, which is occurring as the substance responsible for an off flavour in aged beers, but originates also from lipid oxidation in heat processed food. T2N is an aldehyde formed from linoleic acid as a secondary oxidation product. The modification of Mb with T2N was analyzed with the use of SDS-polyacrylamide gel electrophoresis (SDS-PAGE), and electrospray ionization mass spectrometry (ESI-MS). Results from SDS-PAGE suggest that T2N substitutes Mb and additionally causes cross-linking with polymerization of Mb resulting in an insoluble fraction. The ESI-MS spectrum of the soluble fraction used in the toxicity tests, demonstrated that conjugation of T2N with Mb yielded Mb adducts with one residue of trans-2-nonenal per myoglobin molecule as the major fraction and adducts with different numbers of T2N molecules as minor fractions. In the cytotoxicity assay the T2N and its Mb conjugate causes 50 % destruction of cells at the concentration 95-125 pg/ml and 200 pg/ml respectively, when L₉₂₉ and A₅₄₉ cell lines were used, whereas Mb control tested up to 2000 mg/ml was without any cytotoxic effect. In genotoxicity in vitro assay we have observed that the T2N and its Mb conjugate expressed the genotoxicity. The number of micronuclei in human K₅₆₂ cells reac₅₆₂ 26 ± 2.16 promille (MN/1000 cells), comparing to 62 ± 8.64 MN/1000 cells for the reference free T2N, whereas a control value was 10.33 ± 1.25 MN/1000 cells. The studied compounds expressed also the apoptotic effect in K₅₆₂ cells as the number of apoptotic cells increased to 44.67 ±4.92 promille for T2N-Mb, comparing to 168.67 ±37.28 promille for free T2N, whereas a control value was 30.33 ± 1.36 promille for Mb. In these assays the T2N-Mb conjugate is several times more toxic in relation to control protein. Results indicate that T2N adducts with protein are potent to induce various cytotoxic and apoptotic effects when assayed in vitro tests. It suggests that higher level of such aldehyde might create in organism severe potential of toxicity.