Calendula officinalis Triterpenoid Saponins Impact the Immune Recognition of Proteins in Parasitic Nematodes
| Autor: | Kinga Jóźwicka, Katarzyna Goździk, Julita Nowakowska, Maria Doligalska, Klaudia Brodaczewska, Cezary Pączkowski, Ludmiła Szewczak, Anna Szakiel |
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| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
Microbiology (medical)
protein patterns Protein domain lcsh:Medicine Article chemistry.chemical_compound triterpenoid saponins Myosin parasitic diseases Immunology and Allergy Molecular Biology Oleanolic acid Actin General Immunology and Microbiology biology Chemistry lcsh:R Aldolase A biology.organism_classification Tropomyosin Infectious Diseases Biochemistry TEM nematode ultrastructure Calendula officinalis biology.protein Heligmosomoides polygyrus |
| Zdroj: | Pathogens Volume 10 Issue 3 Pathogens, Vol 10, Iss 296, p 296 (2021) |
| ISSN: | 2076-0817 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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