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

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 modul...

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Autores principales: Stączek, Sylwia, Zdybicka-Barabas, Agnieszka, Wojda, Iwona, Wiater, Adrian, Mak, Paweł, Suder, Piotr, Skrzypiec, Krzysztof, Cytryńska, Małgorzata
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8399224/
https://www.ncbi.nlm.nih.gov/pubmed/34443685
http://dx.doi.org/10.3390/molecules26165097
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author Stączek, Sylwia
Zdybicka-Barabas, Agnieszka
Wojda, Iwona
Wiater, Adrian
Mak, Paweł
Suder, Piotr
Skrzypiec, Krzysztof
Cytryńska, Małgorzata
author_facet Stączek, Sylwia
Zdybicka-Barabas, Agnieszka
Wojda, Iwona
Wiater, Adrian
Mak, Paweł
Suder, Piotr
Skrzypiec, Krzysztof
Cytryńska, Małgorzata
author_sort Stączek, Sylwia
collection PubMed
description 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.
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spelling pubmed-83992242021-08-29 Fungal α-1,3-Glucan as a New Pathogen-Associated Molecular Pattern in the Insect Model Host Galleria mellonella Stączek, Sylwia Zdybicka-Barabas, Agnieszka Wojda, Iwona Wiater, Adrian Mak, Paweł Suder, Piotr Skrzypiec, Krzysztof Cytryńska, Małgorzata Molecules Article 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. MDPI 2021-08-23 /pmc/articles/PMC8399224/ /pubmed/34443685 http://dx.doi.org/10.3390/molecules26165097 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Stączek, Sylwia
Zdybicka-Barabas, Agnieszka
Wojda, Iwona
Wiater, Adrian
Mak, Paweł
Suder, Piotr
Skrzypiec, Krzysztof
Cytryńska, Małgorzata
Fungal α-1,3-Glucan as a New Pathogen-Associated Molecular Pattern in the Insect Model Host Galleria mellonella
title Fungal α-1,3-Glucan as a New Pathogen-Associated Molecular Pattern in the Insect Model Host Galleria mellonella
title_full Fungal α-1,3-Glucan as a New Pathogen-Associated Molecular Pattern in the Insect Model Host Galleria mellonella
title_fullStr Fungal α-1,3-Glucan as a New Pathogen-Associated Molecular Pattern in the Insect Model Host Galleria mellonella
title_full_unstemmed Fungal α-1,3-Glucan as a New Pathogen-Associated Molecular Pattern in the Insect Model Host Galleria mellonella
title_short Fungal α-1,3-Glucan as a New Pathogen-Associated Molecular Pattern in the Insect Model Host Galleria mellonella
title_sort fungal α-1,3-glucan as a new pathogen-associated molecular pattern in the insect model host galleria mellonella
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8399224/
https://www.ncbi.nlm.nih.gov/pubmed/34443685
http://dx.doi.org/10.3390/molecules26165097
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