Quantitative proteomics analysis of Angiostrongylus vasorum-induced alterations in dog serum sheds light on the pathogenesis of canine angiostrongylosis

Abstract Blood contains hundreds of proteins, reflecting ongoing cellular processes and immune reactions. Infections with the blood-dwelling cardiopulmonary nematode Angiostrongylus vasorum in dogs manifest with a broad spectrum of clinical signs including respiratory distress, bleeding diathesis an...

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Autores principales: Lucienne Tritten, Nina Gillis-Germitsch, Tobias Kockmann, Manuela Schnyder
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Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/9814cd8a58394a3c9dd1e8738b2f7909
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spelling oai:doaj.org-article:9814cd8a58394a3c9dd1e8738b2f79092021-12-02T14:12:42ZQuantitative proteomics analysis of Angiostrongylus vasorum-induced alterations in dog serum sheds light on the pathogenesis of canine angiostrongylosis10.1038/s41598-020-79459-92045-2322https://doaj.org/article/9814cd8a58394a3c9dd1e8738b2f79092021-01-01T00:00:00Zhttps://doi.org/10.1038/s41598-020-79459-9https://doaj.org/toc/2045-2322Abstract Blood contains hundreds of proteins, reflecting ongoing cellular processes and immune reactions. Infections with the blood-dwelling cardiopulmonary nematode Angiostrongylus vasorum in dogs manifest with a broad spectrum of clinical signs including respiratory distress, bleeding diathesis and neurological signs, and are associated with a perturbed blood protein profile in dogs. However, current knowledge does not completely explain the observed pathologies induced by A. vasorum infections, including bleeding disorders. Using sera from experimentally infected dogs, dog serum proteome was analysed by quantitative mass spectrometry methods over several time points before and after inoculation. Following computational analysis, we identified 139 up- and downregulated proteins after infection (log2 ratio cut-off ≥ 1.0; q-value ≤ 0.05). Among upregulated proteins were chitinase 3-like 1 and pulmonary surfactant-associated protein B (log2 fold-changes ≥ 5). Pathway enrichment revealed the complement (especially the lectin pathway) and coagulation cascades as significantly affected upon analysis of downregulated proteins. Among them were mannan-binding lectin serine peptidases, ficolin, and coagulation factor XIII-B. These results bring new elements towards understanding the underlying pathomechanisms of bleeding diatheses observed in some A. vasorum-infected dogs.Lucienne TrittenNina Gillis-GermitschTobias KockmannManuela SchnyderNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-11 (2021)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Lucienne Tritten
Nina Gillis-Germitsch
Tobias Kockmann
Manuela Schnyder
Quantitative proteomics analysis of Angiostrongylus vasorum-induced alterations in dog serum sheds light on the pathogenesis of canine angiostrongylosis
description Abstract Blood contains hundreds of proteins, reflecting ongoing cellular processes and immune reactions. Infections with the blood-dwelling cardiopulmonary nematode Angiostrongylus vasorum in dogs manifest with a broad spectrum of clinical signs including respiratory distress, bleeding diathesis and neurological signs, and are associated with a perturbed blood protein profile in dogs. However, current knowledge does not completely explain the observed pathologies induced by A. vasorum infections, including bleeding disorders. Using sera from experimentally infected dogs, dog serum proteome was analysed by quantitative mass spectrometry methods over several time points before and after inoculation. Following computational analysis, we identified 139 up- and downregulated proteins after infection (log2 ratio cut-off ≥ 1.0; q-value ≤ 0.05). Among upregulated proteins were chitinase 3-like 1 and pulmonary surfactant-associated protein B (log2 fold-changes ≥ 5). Pathway enrichment revealed the complement (especially the lectin pathway) and coagulation cascades as significantly affected upon analysis of downregulated proteins. Among them were mannan-binding lectin serine peptidases, ficolin, and coagulation factor XIII-B. These results bring new elements towards understanding the underlying pathomechanisms of bleeding diatheses observed in some A. vasorum-infected dogs.
format article
author Lucienne Tritten
Nina Gillis-Germitsch
Tobias Kockmann
Manuela Schnyder
author_facet Lucienne Tritten
Nina Gillis-Germitsch
Tobias Kockmann
Manuela Schnyder
author_sort Lucienne Tritten
title Quantitative proteomics analysis of Angiostrongylus vasorum-induced alterations in dog serum sheds light on the pathogenesis of canine angiostrongylosis
title_short Quantitative proteomics analysis of Angiostrongylus vasorum-induced alterations in dog serum sheds light on the pathogenesis of canine angiostrongylosis
title_full Quantitative proteomics analysis of Angiostrongylus vasorum-induced alterations in dog serum sheds light on the pathogenesis of canine angiostrongylosis
title_fullStr Quantitative proteomics analysis of Angiostrongylus vasorum-induced alterations in dog serum sheds light on the pathogenesis of canine angiostrongylosis
title_full_unstemmed Quantitative proteomics analysis of Angiostrongylus vasorum-induced alterations in dog serum sheds light on the pathogenesis of canine angiostrongylosis
title_sort quantitative proteomics analysis of angiostrongylus vasorum-induced alterations in dog serum sheds light on the pathogenesis of canine angiostrongylosis
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/9814cd8a58394a3c9dd1e8738b2f7909
work_keys_str_mv AT luciennetritten quantitativeproteomicsanalysisofangiostrongylusvasoruminducedalterationsindogserumshedslightonthepathogenesisofcanineangiostrongylosis
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AT tobiaskockmann quantitativeproteomicsanalysisofangiostrongylusvasoruminducedalterationsindogserumshedslightonthepathogenesisofcanineangiostrongylosis
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