Publications by authors named "Aneta Sowa-Jasilek"

Anionic antimicrobial peptides constitute an integral component of animal innate immunity, however the mechanisms of their antifungal activity are still poorly understood. The action of a unique anionic peptide 2 (AP2) against fungal pathogen was examined using different microscopic techniques and Fourier transform infrared (FTIR) spectroscopy. Although the exposure to AP2 decreased the survival rate of cells, the viability of protoplasts was not affected, suggesting an important role of the fungal cell wall in the peptide action.

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A lipid-binding protein apolipophorin III (apoLp-III), an exchangeable component of lipophorin particles, is involved in lipid transport and immune response in insects. In Galleria mellonella, apoLp-III binding to high-density lipophorins and formation of low-density lipophorin complexes upon immune challenge was reported. However, an unanswered question remains whether apoLp-III could form different complexes in a pathogen-dependent manner.

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The greater wax moth Galleria mellonella has been increasingly used as a model host to determine Candida albicans virulence and efficacy of antifungal treatment. The G. mellonella lysozyme, similarly to its human counterpart, is a member of the c-type family of lysozymes that exhibits antibacterial and antifungal activity.

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Apolipophorin III (apoLp-III), a lipid-binding protein and an insect homolog of human apolipoprotein E, plays an important role in lipid transport and immune response in insects. In the present study, we have demonstrated a correlation in time between changes in the apoLp-III abundance occurring in the hemolymph, hemocytes, and fat body after immunization of Galleria mellonella larvae with Gram-negative bacteria Escherichia coli, Gram-positive bacteria Micrococcus luteus, yeast Candida albicans, and a filamentous fungus Fusarium oxysporum. Using two-dimensional electrophoresis (IEF/SDS-PAGE) and immunoblotting with anti-apoLp-III antibodies, the profile of apoLp-III forms in G.

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The lysozymes are well known antimicrobial polypeptides exhibiting antibacterial and antifungal activities. Their antibacterial potential is related to muramidase activity and non-enzymatic activity resembling the mode of action of cationic defense peptides. However, the mechanisms responsible for fungistatic and/or fungicidal activity of lysozyme are still not clear.

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