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Aspergillus fumigatus spore proteases alter the respiratory mucosa architecture and facilitate equine herpesvirus 1 infection

ABSTRACT: The interaction between Aspergillus fumigatus (Af) spores and the respiratory epithelium, as well as its impact on the epithelial barrier function, remain largely unknown. The respiratory epithelial barrier protects the respiratory epithelium against viral infections. However, it can be compromised by environmental contaminants such as pollen, thereby increasing susceptibility to respiratory viral infections, including alphaherpesvirus equine herpesvirus type 1 (EHV-1). To determine whether Af spores disrupt the epithelial integrity and enhance susceptibility to viral infections, equine respiratory mucosal ex vivo explants were pretreated with Af spore diffusate, followed by EHV-1 inoculation. Af spore proteases were characterized by zymography and identified using mass spectrometry-based proteomics. Proteases of the serine protease, metalloprotease and aspartic protease groups were identified. Morphological analysis of hematoxylin-eosin (HE)-stained sections of the explants revealed that Af spores induced desquamation of epithelial cells and a significant increase in intercellular space at high and low concentrations, respectively. The increase in intercellular space in the epithelium caused by Af spore proteases correlated with an increase in EHV-1 infection. Together, our findings demonstrate that Af spore proteases disrupt epithelial integrity, potentially leading to increased viral infection of the respiratory epithelium.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Neosartorya Fumigata (aspergillus Fumigatus)

TISSUE(S): Spore, Respiratory Tract Epithelium

SUBMITTER: Evy Timmerman

LAB HEAD: Joren Portaels

PROVIDER: PXD053508 | Pride | 2024-08-14

REPOSITORIES: Pride

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			Action	DRS
	PRC-6072DDA_UP_5061_F012257_1p_IhT_trapPM1_Neo_EASYJB_DDM_PRC-6072_A.raw	Raw
	PRC-6072DDA_UP_5061_F012259_1p_IhT_trapPM1_Neo_EASYJB_DDM_PRC-6072_B.raw	Raw
	PRC-6072DDA_UP_5061_F012261_1p_IhT_trapPM1_Neo_EASYJB_DDM_PRC-6072_C.raw	Raw
	allSpectra.CID.ITMS.iso_0.apl	Other
	allSpectra.CID.ITMS.iso_1.apl	Other

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Project description:Bacterial spores play an important role in disease initiation, transmission and persistence. The outermost spore layer, the exosporium, is important as it is the first point of contact between the spore and the environment and may be involved in spore adherence, protection and germination. Clostridium sordellii is a highly lethal, spore forming pathogen that causes soft-tissue infections, enteritis and toxic-shock syndrome. Despite the importance of C. sordellii spores in disease, spore proteins from this bacterium have not been defined or interrogated functionally. In this study, we identified the C. sordellii outer spore proteome and two of the identified proteins, CSA and CSB, were characterised using a genetic and phenotypic approach. Both proteins were essential for the correct formation and positioning of the C. sordellii spore coat and exosporium. The absence of CSA reduced sporulation levels and increased spore sensitivity to heat, sodium hydroxide and hydrochloric acid. By comparison, CSB was required for normal levels of spore adherence to cervical, but not vaginal, cells, with csb mutant spores having increased adherence properties. The establishment of a mouse infection model of the gastrointestinal tract for C. sordellii allowed the role of CSA and CSB to be interrogated in an infected host. Following the oral administration of spores to mice, the wild-type strain efficiently colonized the gastrointestinal tract, with the peak of bacterial numbers occurring at one day post-infection. Colonization was reduced by two logs at four days post-infection. By comparison, mice infected with the csb mutant did not show a reduction in bacterial numbers. The absence of CSB therefore allows the csb mutant to persist within the gastrointestinal tract. We conclude that C. sordellii outer spore proteins are important for the structural and functional integrity of spores, and for colonization and persistence during infection. Finally, Clostridium difficile, Bacillus cereus and Bacillus anthracis encode proteins with homology to CSA and CSB but these bacteria produce spores that are structurally dissimilar to those of C. sordellii, and the function of the proteins in these hosts is different to that in C. sordellii. These findings suggest that, despite their homology, spore proteins can have variable functions in different bacterial species which highlights the necessity of studying each spore protein in the cognate species from which it originates.

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Aspergillus fumigatus spore proteases alter the respiratory mucosa architecture and facilitate equine herpesvirus 1 infection

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