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Table 1. Antibody recognition of regions (represented by overlapping pin-attached 15-mer peptides) corresponding to the sequence of proteins Dsg1 and Dsg3 by PV patientsproteinsequentialposition ofamino acids#11185, 49y,♂, Dsg1positive#11608, 51y,♀, Dsg1,3positive#11542, 64y,♂, Dsg1positive#10915, 74y,♀, Dsg3positive#11190, 22y,♀, Dsg1positive76-100 - + + - +146-160 - + + - +Dsg1 186-220 - + + - +446-450 - + + - +476-500 - + + - +54-78 + + + + +Dsg3340-354 - + + - +375-389 - + + - +601-615 - + + + -Criteria for peptide recognition to identify possible epitopic regions of proteins Dsg1 and Dsg3:PV patients’ measured OD ≥ mean OD + 7× sd value of control (Dsg1 related pin-attached peptides)PV patients’ measured OD ≥ mean OD + 5× sd value of control (Dsg3 related pin-attached peptides)In summary, five regions within the sequence of the protein Dsg1 (75-100 (Figure 1a),145-160, 185-220, 445-450, 476-500) and four regions within the sequence of the proteinDsg3 (52-78 (Figure 1b), 340-355, 375-390, 600-615) have been determined with positiveserum antibody recognition by three out of five patients (Table 1).AcknowledgmentsThese studies were supported by grants of Hungarian Research Fund (OTKA K 61518), GVOP(GVOP-3.2.1 – 2004 – 04 -0352/3.0, 3.2.1 – 2004-04-0005/3.0). Number of ethical permission:TUKEB 74-75/1998.References1. Waschke, J. Histochem. Cell Biol. 130, 21-54 (2008).2. Wheeler, G.N., Parker, A.E., Thomas, C.L., Ataliotis, P., Poynter, D., Arnemann, J., Rutman, A.J.,Pidsley, S.C., Watt, F.M., Rees, D.A., Buxton, R.S., Magee, A.I. Proc. Natl. Acad. Sci. U.S.A. 88,4796-4800 (1991).3. Amagai, M., Klaus-Kovtun, V., Stanley, J.R. Cell. 67, 869-877 (1991).4. Chou, P.Y., Fasman, G.D. Biochem. 13, 222-45 (1974).5. Eisenberg, D., Wesson, M., Wilcox, W. In Fasman, G.D. (Eds.), Prediction of protein structure andthe principles of protein conformation. Plenum Press, New York, 1989, p. 635.6. Rost, B., Yachdav, G., Liu, J. Nucleic Acids Research 32, W321-W326 (2004).7. Geysen, H.M., Meloen, R.H., Barteling, S.J. Proc. Natl. Acad. Sci. U.S.A. 81, 3998-4002 (1984).475
<strong>Proceedings</strong> of the 31 st European Peptide SymposiumMichal Lebl, Morten Meldal, Knud J. Jensen, Thomas Hoeg-Jensen (Editors)European Peptide Society, 2010T-Cell Epitopes in Autoimmune Bullous Skin DisordersKatalin Uray 1 , Márta Marschalkó 2 , Hajnalka Szabados 1 ,Antal Blazsek 2 , Ferenc Hudecz 1,3 , Sarolta Kárpáti 2 , and Szilvia Bősze 11 Research Group of Peptide Chemistry, Hungarian Academy of Sciences, Eötvös LorándUniversity, Budapest, H-1117, Hungary; 2 Department of Dermato-Venereology and SkinOncology, Semmelweis University, Budapest, H-1085, Hungary; 3 Department ofOrganic Chemistry, Eötvös Loránd University, Budapest, H-1117, HungaryIntroductionAutoimmune bullous skin diseases, such as bullosus pemphigoid (BP) and pemphigusvulgaris (PV), are rare, severe, sometimes life-threatening skin disorders. Serologicallythey are characterized by autoreactive serum antibodies directed against different adhesionmolecules of the epidermis and the dermoepidermal basement zone [1]. The antibodybinding affects the adhesive function of these molecules resulting in detachment of the cellsand subsequent blister formation [2,3].In the pathogenesis of both pemphigus and pemphigoid, autoreactive T-cell responseplays a crucial role, because initiation and perpetuation of B-cell response needs therecognition of T-cell epitopes. In both types of diseases the T-cells recognize epitopes fromthe extracellular domain of desmoglein 3 (Dsg3) [4-6] or NC16a domain of collagen XVII(BP180) proteins [3,6], producing different cytokines, e.g. interferon- (IFN- ).We have selected potential T-cell epitope regions within the proteins BP180 (502-515)and Dsg3 (96-112). The synthetic peptides were used to stimulate the peripheral bloodmonomorphonuclear cells (PBMC) of patients and healthy controls, and the amount ofproduced IFN- was determined by ELISA.Results and DiscussionPeptides were synthesized by solid phase peptide synthesis method using standardFmoc/tBu chemistry on Rink-amide MBHA resin. The peptides were RP-HPLC purified,then characterized by ESI-MS and amino acid analysis, showing the expected <strong>com</strong>position(Table 1).PBMC from the peripheral blood of healthy donors (D1, ♂30y, D2, ♀ 34y) andpatients diagnosed with pemphigus vulgaris (D3, ♂74y, D4, ♀30y) were isolated asdescribed [7]. PBMC were cultured at 1.5-1.8 x 10 5 /well in 96-well U-bottom plates. Dsg3and BP180 peptides were added at concentrations 0.05 and 0.025 mM [8]. As nonspecificpositive control, phytohaemagglutinin (PHA-P) and Enterotoxin B, Staphylococcal (SEB)were used at c = 5 µg/mL. After 20 or 90 h of incubation, supernatants were harvested.IFN- content was measured by sandwich ELISA. As capture antibody human anti-IFN-(BD 551221) was used. The INF- level of PBMC supernatant was determined usingbiotinylated mouse anti-IFN- (BD 554550) as detection antibody.IFNγ concentration (pg/ml)16001400120010008006004002000D1 healthy control ♂30yD3 PV patient ♂74yD4 PV patient ♀30ymedium control peptide #1 peptide #2 peptide #3 peptide #4 peptide #5Fig. 1. IFN- level of supernatants obtained from PBMC of donors after 20 hrs incubationwith 0.025mM peptide, determined by ELISA.476
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Peptides 2010Tales of PeptidesProce
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Peptides 2010Tales of PeptidesProce
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IntroductionWe had the distinct hon
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Scientific programIn planning the 3
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31 st EUROPEAN PEPTIDE SYMPOSIUMSep
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published by John Wiley & Sons as a
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The Josef Rudinger AwardThis award
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Young Investigators' SymposiumThe y
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xxiv
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Design of Peptidyl-Inhibitors for G
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Synthetic Antifreeze Glycopeptide A
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Synthesis and Oxidative Folding of
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Convergent Syntheses of Huprp106-12
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Bactericidal Activity of Small Beta
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Bradykinin Analogues Acylated on Th
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Antimicrobial Activity of Small 3-(
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Interaction of Curcumin with A-Synu
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Fluorescent and Luminescent Fusion
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Cellular Expression of the Human An
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2D IR Spectroscopy of Oligopeptides
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large, non-redundant subset of prot
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The aberrantly glucosylated peptide
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Table 1. Proline cis/trans ratios o
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Table 1. Yields, UV-vis absorption
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Table 1. Purity of the targeted tri
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processes are blocked. Interestingl
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(tb4 n ,1 m )MTII(tb1 n ,4 m )MTIIF
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Fig. 2. a) Part of the 400 MHz HR-M
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Once printed, the amino acid partic
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A) PSA, few seconds73B) PSA, 45 min
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short β strands. In contrast, nume
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neg. control Cs9-Rhd MM-218Fig. 2.
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Table 1. The general structure of t
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% ID in the liver 1 h p.i.100908070
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Peptidyl phosphoranes were first re
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obtained from the same sardines and
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MccJ25 variants were produced by si
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Fig. 2. Proposed signaling mechanis
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Table 1. mCD4-HS12 antiviral activi
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Subject index(S)-2-(1-adamantyl)gly
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chip 18chiral triazine condensing r
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heat stress 348helical conformation
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O-acyl isopeptide method 112obesity
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SH2-ligands 210short collagen-relat
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Author indexAboye, Teshome Leta 142
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Chi, Hongfang 480Chiche, Laurent 6C
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Geronikaki, Athina 444Gessmann, Ren
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Kostova, Kalina 528Kotzia, Georgia
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Nagata, Koji 162Nagayev, Igor Yu. 5
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Salvarese, Nicola 518Sammet, Benedi
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Vauquelin, Georges 138Veiga, Ana Sa
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