Characterization of Pseudogymnoascus destructans conidial adherence to extracellular matrix: Association with fungal secreted proteases and identification of candidate extracellular matrix binding proteins. (January 2023)

• Record Type: Journal Article
• Authors: Eiamcharoen, Piyaporn; Gelli, Angie; Byrne, Barbara A.; Keel, M. Kevin
• Is Part Of: Microbial pathogenesis. Volume 174(2023)
• Publication Date: 2023-01
• Subjects: White-nose syndrome (WNS) -- Conidial adherence -- Extracellular matrix (ECM) -- Secreted protease -- Moonlighting protein; Pathogenic microorganisms -- Periodicals; Pathology, Molecular -- Periodicals; Communicable Diseases -- microbiology -- Periodicals; Communicable Diseases -- parasitology -- Periodicals; Micro-organismes pathogènes -- Périodiques; Pathologie moléculaire -- Périodiques; Electronic journals; 616.9041
• DOI: 10.1016/j.micpath.2022.105895
• Languages: English
• ISSNs: 0882-4010

Abstract

Abstract: Pseudogymnoascus destructans is the etiological agent of white-nose syndrome (WNS), a fungal skin infection of hibernating bats. Pathophysiology of the disease involves disruption of bat metabolism and hibernation patterns, which subsequently causes premature emergence and mortality. However, information on the mechanism(s) and virulence factors of P. destructans infection is minimally known. Typically, fungal adherence to host cells and extracellular matrix (ECM) is the critical first step of the infection. It allows pathogenic fungi to establish colonization and provides an entry for invasion in host tissues. In this study, we characterized P. destructans conidial adherence to laminin and fibronectin. We found that P. destructans conidia adhered to laminin and fibronectin in a dose-dependent, time-dependent and saturable manner. We also observed changes in the gene expression of secreted proteases, in response to ECM exposure. However, the interaction between fungal conidia and ECM was not specific, nor was it facilitated by enzymatic activity of secreted proteases. We therefore further investigated other P. destructans proteins that recognized ECM and found glyceraldehyde-3-phosphate dehydrogenase and elongation factor 1-alpha among the candidate proteins. Our results demonstrate that P. destructans may use conidial surface proteins to recognize laminin and fibronectin and facilitate conidial adhesion to ECM. In addition, other non-specific interactions may contribute to the conidial adherence to ECM. However, the ECM binding protein candidates identified in this study highlight additional potential fungal virulence factors worth investigating in the P. destructans mechanism of infection in future studies. Highlights: Conidia of P. destructans binds extracellular matrix to establish colonization. Secreted proteases of P. destructans are also located on the outer surface of fungal conidia. Secreted proteases of P. destructans respond to extracellular matrix exposure. Fungal proteins with moonlighting functions on cell surface bind to fibronectin. Glyceraldehyde-3-phosphate dehydrogenase and an elongation factor 1-alpha are proposed fibronectin binding proteins .