Fungal α-1,3-Glucan as a New Pathogen-Associated Molecular Pattern in the Insect Model Host Galleria mellonella

Molecules

Krzysztof Skrzypiec¹  Paweł Mak²  Piotr Suder³  Sylwia Stączek⁴  Małgorzata Cytryńska⁴  Agnieszka Zdybicka-Barabas⁴  Iwona Wojda⁴  Adrian Wiater⁵ 

[1] Analytical Laboratory, Faculty of Chemistry, Maria Curie-Skłodowska University, M.C. Skłodowska Square 5, 20-031 Lublin, Poland;Department of Analytical Biochemistry, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7 St., 30-387 Krakow, Poland;Department of Analytical Chemistry and Biochemistry, Faculty of Materials Sciences and Ceramics, AGH University of Science and Technology, Mickiewicza 30 Ave., 30-059 Krakow, Poland;Department of Immunobiology, Faculty of Biology and Biotechnology, Institute of Biological Sciences, Maria Curie-Skłodowska University, Akademicka 19 St., 20-033 Lublin, Poland;Department of Industrial and Environmental Microbiology, Faculty of Biology and Biotechnology, Institute of Biological Sciences, Maria Curie-Skłodowska University, Akademicka 19 St., 20-033 Lublin, Poland;

关键词: α-1,3-glucan;    Aspergillus niger;    Galleria mellonella;    insect immune response;    pathogen-associated molecular pattern;    pattern recognition receptors;   

DOI  :  10.3390/molecules26165097

来源: DOAJ

【 摘 要 】

Recognition of pathogen-associated molecular patterns (PAMPs) by appropriate pattern recognition receptors (PRRs) is a key step in activating the host immune response. The role of a fungal PAMP is attributed to β-1,3-glucan. The role of α-1,3-glucan, another fungal cell wall polysaccharide, in modulating the host immune response is not clear. This work investigates the potential of α-1,3-glucan as a fungal PAMP by analyzing the humoral immune response of the greater wax moth Galleria mellonella to Aspergillus niger α-1,3-glucan. We demonstrated that 57-kDa and 61-kDa hemolymph proteins, identified as β-1,3-glucan recognition proteins, bound to A. niger α-1,3-glucan. Other hemolymph proteins, i.e., apolipophorin I, apolipophorin II, prophenoloxidase, phenoloxidase activating factor, arylphorin, and serine protease, were also identified among α-1,3-glucan-interacting proteins. In response to α-1,3-glucan, a 4.5-fold and 3-fold increase in the gene expression of antifungal peptides galiomicin and gallerimycin was demonstrated, respectively. The significant increase in the level of five defense peptides, including galiomicin, corresponded well with the highest antifungal activity in hemolymph. Our results indicate that A. niger α-1,3-glucan is recognized by the insect immune system, and immune response is triggered by this cell wall component. Thus, the role of a fungal PAMP for α-1,3-glucan can be postulated.

【 授权许可】

Unknown