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dc.creatorPopović, Milica
dc.creatorAnđelković, Uroš
dc.creatorBurazer, Lidija M.
dc.creatorLindner, Buko
dc.creatorPetersen, Arnd
dc.creatorGavrović-Jankulović, Marija
dc.date.accessioned2018-11-22T00:23:59Z
dc.date.available2018-11-22T00:23:59Z
dc.date.issued2013
dc.identifier.issn0031-9422
dc.identifier.urihttp://cherry.chem.bg.ac.rs/handle/123456789/1403
dc.description.abstractPlant proteinase inhibitors are considered important defense molecules against insect and pathogen attack. The cysteine proteinase inhibitor (CPI) from green kiwifruit (Actinidia deliciosa) belongs to the cystatin family and shows potent antifungal activity (in vitro and in vivo). However, the low abundance of this molecule in fruit (6 mu g/g of fresh fruit) seems to limit further investigations on the interaction between phytocystatin and photopathogenic fungi. In this paper the cDNA of the kiwi CPI was expressed in Escherichia coli. Fifteen N-terminal amino acids were identified by Edman degradation, and 77% of the rCPI primary structure was confirmed by mass fingerprint. The structural homology of recombinant CPI (rCPI) to its natural counterpart has been clearly demonstrated in immunological assays (immunoblot and ELISA inhibition). Biological activity of rCPI was demonstrated in inhibition assay with cysteine proteinase papain (EC50 2.78 nM). In addition, rCPI reveals antifungal properties toward pathogenic fungi (Alternaria radicina and Botrytis cinerea), which designates it as an interesting model protein for the exploration of plant phytocystatins - pathogen interactions. Understanding the molecular mechanisms of natural plant resistance could lead to the development of ecologically safe fungicides for controlling post-harvest diseases and maintaining food quality.en
dc.publisherPergamon-Elsevier Science Ltd, Oxford
dc.relationinfo:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172049/RS//
dc.relationinfo:eu-repo/grantAgreement/EC/FP7/256716/EU//
dc.rightsrestrictedAccess
dc.sourcePhytochemistry
dc.subjectCysteine proteinase inhibitoren
dc.subjectPhytocystatinen
dc.subjectAntifungal activityen
dc.subjectKiwifruiten
dc.titleBiochemical and immunological characterization of a recombinantly-produced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa)en
dc.typearticle
dc.rights.licenseARR
dcterms.abstractAндјелковиц, Урос; Буразер, Лидија; Гавровић-Јанкуловић, Марија; Поповић, Милица; Петерсен, Aрнд; Линднер, Буко;
dc.citation.volume94
dc.citation.spage53
dc.citation.epage59
dc.identifier.wos000324721100005
dc.identifier.doi10.1016/j.phytochem.2013.06.006
dc.citation.other94: 53-59
dc.citation.rankM21
dc.identifier.pmid23830694
dc.type.versionpublishedVersionen
dc.identifier.scopus2-s2.0-84885183151
dc.identifier.rcubKon_2523


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