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dc.contributor.authorJezek, J.en
dc.contributor.authorEl Ridi, R.en
dc.contributor.authorSalah, M.en
dc.contributor.authorWagih, A.en
dc.contributor.authorAziz, H. W.en
dc.contributor.authorTallima, H.en
dc.contributor.authorEl Shafie, M. H.en
dc.contributor.authorKhalek, T. A.en
dc.contributor.authorAmmou, F. F. A.en
dc.contributor.authorStrongylis, C.en
dc.contributor.authorMoussis, V.en
dc.contributor.authorTsikaris, V.en
dc.date.accessioned2015-11-24T16:37:56Z-
dc.date.available2015-11-24T16:37:56Z-
dc.identifier.issn0006-3525-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/7979-
dc.rightsDefault Licence-
dc.subjectcathepsin l proteinaseen
dc.subjectpeptidesen
dc.subjectsequentialen
dc.subjectoligopeptide carriersen
dc.subjectsynthetic carriersen
dc.subjectsynthetic peptideen
dc.subjectvaccineen
dc.subjectfasciola giganticaen
dc.subjectimmunogenicityen
dc.subjectprotective potentialen
dc.subjectliver fluke vaccinesen
dc.subjectin-vitroen
dc.subjectcysteine proteinaseen
dc.subjectantigenic peptidesen
dc.subjecthepaticaen
dc.subjectvaccinationen
dc.subjectdiagnosisen
dc.subjectdesignen
dc.subjectcattleen
dc.subjectcytotoxicityen
dc.titleFasciola gigantica cathepsin L proteinase-based synthetic peptide for Immunodiagnosis and prevention of sheep fasciolosisen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.primaryDoi 10.1002/Bip.20788-
heal.identifier.secondary<Go to ISI>://000255448700030-
heal.identifier.secondaryhttp://onlinelibrary.wiley.com/store/10.1002/bip.20788/asset/20788_ftp.pdf?v=1&t=h0f8nn5b&s=3db456bc323c196d84752e1cc7402aa80d175fa7-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.publicationDate2008-
heal.abstractSheep fasciolosis is a devastating burden for the livestock industry. We herein report on immunodiagnosis of fasciolosis, and significant protection of sheep against challenge infection with Fasciola gigantica following immunization with a peptide based on the H-Asp(110)-Lys-Ile-Asp- Trp-Arg-Glu-Ser-Gly-Tyr-Val-Thr-Glu-Val(123)- OH (Fas14p) sequence of E gigantica cathepsin L-cysteine proteinase. This sequence was synthesized in three difterent forms: as N-alpha acetylated (Ac-Asp(110)-Lys-Ile-Asp- Trp-Arg-Glu-Ser-Gly-Tyr-Val-Thr-Glu-Val(123)- OH, FasAc14p), bearing at the amino-terminus an N-alpha acetylated cystein (Ac-Cys-Asp(110)-Lys-Ile-Asp-Trp-Arg-Glu-Ser-Gly- Tyr-Val-Thr-Glu-Val(123)-OH, FasAcCys14p), and conjugated to sequential oligopeptide carrier Ac-[Lys-Aib-Gly](4)-OH (Ac-SOC4) through an amide bond formed between Val(123) carboxylic group of the epitope and the lysine ff groups of the carrier (Ac[Lys(Fas14p)-Aib-GlY](4)-OH). Ac-[Lys(Fas14p)-Aib-Gly](4)-OH failed to readily discriminate between naive and infected sheep. In contrast, the free peptides reproducibly differentiated between parasite-free sheep, sheep infected with parasites other than Fasciola, and experimentally Fasciola-infected sheep. The data together indicated that the peptides might be of considerable use for discriminating between early and late, and low and high burden, sheep infection with F. gigantica. FasAc14p was chosen to determine whether a peptide based on a critical enzymatic site of cathepsin L proteinase may induce protection against challenge infection. Sheep immunization with FasAc14p peptide induced significant expression of interleukin-4 mRNA, and humoral antibodies that bound to molecule(s) on the intact surface membrane of newly excysted juvenile worms, and mediated their attrition. The immune responses were associated with significant (P < 0.02) decrease of 23.1% in worm recovery, but with no decrease in the size or maturation of worms recovered. (c) 2007 Wiley Periodicals, Inc.en
heal.journalNameBiopolymersen
heal.journalTypepeer reviewed-
heal.fullTextAvailabilityTRUE-
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ

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