Stratilova, B.Rehulka, P.Garajova, S.Rehulkova, H.Stratilova, E.Hrmova, M.Kozmon, S.2020-04-302020-04-302020Phytochemistry, 2020; 175:112368-1-112368-90031-94221873-3700http://hdl.handle.net/2440/124457The 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.en© 2020 Elsevier Ltd. All rights reserved.Petroselinum crispum; apiaceae; parsley; mass spectrometry; 3D structural modelling; molecular dynamics simulations; PR-10 proteinsJournal article100001941510.1016/j.phytochem.2020.1123680005391594000032-s2.0-85083423526529159Hrmova, M. [0000-0002-3545-0605]