Structural characterization of the Pet c 1.0201 PR-10 protein isolated from roots of Petroselinum crispum (Mill.) Fuss

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dc.contributor.authorStratilova, B.
dc.contributor.authorRehulka, P.
dc.contributor.authorGarajova, S.
dc.contributor.authorRehulkova, H.
dc.contributor.authorStratilova, E.
dc.contributor.authorHrmova, M.
dc.contributor.authorKozmon, S.
dc.date.issued2020
dc.description.abstractThe native dimeric Petroselinum crispum (Mill.) Fuss protein Pet c 1.0201 and a monomeric xyloglucan endotransglycosylase enzyme (Garajova et al., 2008) isolated from the root cells co-purify and share similar molecular masses and acidic isoelectric points. In this work, we determined the complete primary structure of the parsley Pet c 1.0201 protein, based on tryptic and chymotryptic peptides followed by the manual micro-gradient chromatographic separation coupled with offline MALDI-TOF/TOF mass spectrometry. The bioinformatics approach enabled us to include the parsley protein into the PR-10 family, as it exhibited the highest protein sequence identity with the Apium graveolens Api g 1.0201 allergen and the major Daucus carota allergen Dau c 1.0201. Hence, we designated the Petroselinum crispum protein as Pet c 1.0201 and deposited it in the UniProt Knowledgebase under the accession C0HKF5. 3D protein homology modelling and molecular dynamics simulations of the Pet c 1.0201 dimer confirmed the typical structure of the Bet v 1 family allergens, and the potential of the Pet c 1.0201 protein to dimerize in water. However, the behavioural properties of Pet c 1.0201 and the celery allergen Api g 1.0101 differed in the presence of salts due to transiently and stably formed dimeric forms of Pet c 1.0201 and Api g 1.0101, respectively.
dc.description.statementofresponsibilityBarbora Stratilová, Pavel Řehulka, Soňa Garajová, Helena Řehulková, Eva Stratilová, Maria Hrmova, Stanislav Kozmon
dc.identifier.citationPhytochemistry, 2020; 175:112368-1-112368-9
dc.identifier.doi10.1016/j.phytochem.2020.112368
dc.identifier.issn0031-9422
dc.identifier.issn1873-3700
dc.identifier.orcidHrmova, M. [0000-0002-3545-0605]
dc.identifier.urihttp://hdl.handle.net/2440/124457
dc.language.isoen
dc.publisherElsevier
dc.relation.granthttp://purl.org/au-research/grants/arc/DP120100900
dc.rights© 2020 Elsevier Ltd. All rights reserved.
dc.source.urihttps://doi.org/10.1016/j.phytochem.2020.112368
dc.subjectPetroselinum crispum; apiaceae; parsley; mass spectrometry; 3D structural modelling; molecular dynamics simulations; PR-10 proteins
dc.titleStructural characterization of the Pet c 1.0201 PR-10 protein isolated from roots of Petroselinum crispum (Mill.) Fuss
dc.typeJournal article
pubs.publication-statusPublished

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