4.5 Article

Calendula officinalis Triterpenoid Saponins Impact the Immune Recognition of Proteins in Parasitic Nematodes

Journal

PATHOGENS
Volume 10, Issue 3, Pages -

Publisher

MDPI
DOI: 10.3390/pathogens10030296

Keywords

triterpenoid saponins; TEM nematode ultrastructure; protein patterns

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Funding

  1. Ministry of Science and Higher Education through the Faculty of Biology, University ofWarsaw, Poland [304 117 32/4332, BW1720/22]

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The study shows that triterpenoid saponins can alter the subcellular morphology of parasitic nematode larvae and affect the recognition of immunogenic proteins, leading to changes in proteins involved in signaling and cellular processes. Several candidate proteins, including beta-tubulin, myosin, actin, and ATP-synthase, were found to be downregulated or degraded in larvae exposed to saponins.
The influence of triterpenoid saponins on subcellular morphological changes in the cells of parasitic nematodes remains poorly understood. Our study examines the effect of oleanolic acid glucuronides from marigold (Calendula officinalis) on the possible modification of immunogenic proteins from infective Heligmosomoides polygyrus bakeri larvae (L3). Our findings indicate that the triterpenoid saponins alter the subcellular morphology of the larvae and prevent recognition of nematode-specific proteins by rabbit immune-IgG. TEM ultrastructure and HPLC analysis showed that microtubule and cytoskeleton fibres were fragmented by saponin treatment. MASCOT bioinformatic analysis revealed that in larvae exposed to saponins, the immune epitopes of their proteins altered. Several mitochondrial and cytoskeleton proteins involved in signalling and cellular processes were downregulated or degraded. As possible candidates, the following set of recognised proteins may play a key role in the immunogenicity of larvae: beta-tubulin isotype, alpha-tubulin, myosin, paramyosin isoform-1, actin, disorganized muscle protein-1, ATP-synthase, beta subunit, carboxyl transferase domain protein, glutamate dehydrogenase, enolase (phosphopyruvate hydratase), fructose-bisphosphate aldolase 2, tropomyosin, arginine kinase or putative chaperone protein DnaK, and galactoside-binding lectin. Data are available via ProteomeXchange with identifier PXD024205.

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