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1.

001-es BibID:BIBFORM065593
Első szerző:Gall-Debreceni Anna
Cím:Specific detection and quantitation of bovine IgG in bioreactor derived mouse mAb preparations / Anna Gall-Debreceni, Jozsef Lazar, Janos Kadas, Attila Balogh, Annamaria Ferenczi, Endre Sos, Laszlo Takacs, Istvan Kurucz
Dátum:2016
ISSN:0022-1759
Megjegyzések:Monoclonal antibody and recombinant protein production benefits greatly from bovine serum as an additive. The caveat is that bovine serum IgG, co-purifies with mAbs and IgG Fc-containing fusion proteins and it presents a contaminant in the end products. In order to analytically validate the products, species specific reagents are needed that react with bovine IgG exclusively. Our attempts to find such commercially available reagents failed. Here, we report the production of species specific mAbs which recognize bovine IgG even in the presence of excess amount of mouse IgG. We present five mAbs: Bsi4028, Bsi4032, Bsi4033, Bsi4034 and Bsi4035 suitable to determine the presence of bovine IgG contamination via ELISA or immunoblotting in bioreactor derived mouse mAb preparations. To quantitate bovine IgG content we developed sensitive sandwich ELISAs capable to detect bovine IgG contaminant in the ng/ml (~10-11M/l) range. Finally, we show that bovine IgG is efficiently removed from bioreactor produced mouse mAb preparation via affinity depletion columns prepared with Bsi4028, Bsi4032, Bsi4033, Bsi4034, Bsi4035 mAbs.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Bovine IgG contamination
Detection
Monoclonal antibody
Purification
Megjelenés:Journal of Immunological Methods. - 438 (2016), p. 26-34. -
További szerzők:Lázár József Kádas János (1976-) (molekuláris biológus, biokémikus, kertészmérnök) Balogh Attila Ferenczi Annamária (1986-) (molekuláris biológus, mikrobiológus) Sós Endre Takács László (1955-) Kurucz István
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2.

001-es BibID:BIBFORM047874
035-os BibID:PMID:21732557
Első szerző:Kovács András László (biológus, biológia-kémia tanár)
Cím:Fractionation of the human plasma proteome for monoclonal antibody proteomics-based biomarker discovery / András Kovács, Edit Sperling, József Lázár, Attila Balogh, János Kádas, Ákos Szekrényes, László Takács, István Kurucz, András Guttman
Dátum:2011
ISSN:0173-0835
Megjegyzések:mAb proteomics, a reversed biomarker discovery approach, is a novel methodology to recognize the proteins of biomarker potential, but requires subsequent antigen identification steps. While in case of high-abundant proteins, it generally does not represent a problem, for medium or lower abundant proteins, the identification step requires a large amount of sample to assure the proper amount of antigen for the ID process. In this article, we report on the use of combined chromatographic and precipitation techniques to generate a large set of fractions representing the human plasma proteome, referred to as the Analyte Library, with the goal to use the relevant library fractions for antigen identification in conjunction with mAb proteomics. Starting from 500mL normal pooled human plasma, this process resulted in 783 fractions with the average protein concentration of 1mg/mL. First, the serum albumin and immunoglobulins were depleted followed by prefractionation by ammonium sulfate precipitation steps. Each precipitate was then separated by size exclusion chromatography, followed by cation and anion exchange chromatography. The 20 most concentrated ion exchange chromatography fractions were further separated by hydrophobic interaction chromatography. All chromatography and precipitation steps were carefully designed aiming to maintain the native forms of the intact proteins throughout the fractionation process. The separation route of vitamin D-binding protein (an antibody proteomics lead) was followed in all major fractionation levels by dot blot assay in order to identify the library fraction it accumulated in and the identity of the antigen was verified by Western blot.
Tárgyszavak:Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Electrophoresis. - 32 : 15 (2011), p. 1916-1925. -
További szerzők:Sperling Edit Lázár József Balogh Attila (bőrgyógyász) Kádas János (1976-) (molekuláris biológus, biokémikus, kertészmérnök) Szekrényes Ákos (1983-) (vegyészmérnök) Takács László (1955-) Kurucz István Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:K81839
OTKA
TECH-09-A1-2009-0113; mABCHIC
Egyéb
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Intézményi repozitóriumban (DEA) tárolt változat
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3.

001-es BibID:BIBFORM111963
035-os BibID:(cikkazonosító)100580 (Scopus)85165521769
Első szerző:Lázár József
Cím:Large-scale plasma proteome epitome profiling is an efficient tool for the discovery of cancer biomarkers / Lazar Jozsef, Antal-Szalmas Peter, Kurucz Istvan, Ferenczi Annamaria, Jozsi Mihaly, Tornyi Ilona, Muller Monika, Fekete Janos Tibor, Lamont John, FitzGerald Peter, Gall-Debreceni Anna, Kadas Janos, Vida Andras, Tardieu Nadege, Kieffer Yann, Jullien Anne, Guergova-Kuras Mariana, Hempel William, Kovacs Andras, Kardos Tamas, Bittner Nora, Csanky Eszter, Szilasi Maria, Losonczy Gyorgy, Szondy Klara, Galffy Gabriella, Csada Edit, Szalontai Klara, Somfay Attila, Malka David, Cottu Paul, Bogos Krisztina, Takacs Laszlo
Dátum:2023
ISSN:1535-9476
Megjegyzések:Current proteomic technologies focus on the quantification of protein levels, while little effort is dedicated to the development of systems approaches to simultaneously monitor proteome variability and abundance. Protein variants may display different immunogenic epitopes detectable by monoclonal antibodies. Epitope variability results from alternative splicing, posttranslational modifications, processing, degradation, and complex formation and possess dynamically changing availability of interacting surface structures frequently serve as reachable epitopes, and often carry different functions. Thus, it is highly likely, that the presence of some of the accessible epitopes correlate with function under physiological and pathological conditions. To enable the exploration of the impact of protein variation on the immunogenic epitome first; here, we present a robust and analytically validated protein epitome profiling (PEP) technology for characterizing immunogenic epitopes of the plasma. To this end we prepared mAb libraries directed against the normalized human plasma proteome as a complex natural immunogen. Resulting hybridoma supernatants were selected for mAb production and the corresponding hybridomas were cloned. Monoclonal antibodies react with single epitopes, thus profiling with the libraries is expected to profile many epitopes which we define by the mimotopes, as we present here. Screening blood plasma samples from control subjects (n = 558) and cancer patients (n = 598) for merely 69 native epitopes displayed by 20 abundant plasma proteins resulted in distinct cancer-specific epitope panels that showed high accuracy (AUC 0.826?0.966) and specificity for lung, breast, and colon cancer. Deeper profiling (?290 epitopes of approximately 100 proteins) showed unexpected granularity of the epitope-level expression data and detected neutral and lung-cancer associated epitopes of individual proteins. Biomarker epitope panels selected from a pool of 21 epitopes of 12 proteins were validated in independent clinical cohorts. The results demonstrate the value of PEP as a rich and thus far unexplored source of protein biomarkers with diagnostic potential.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Molecular & Cellular Proteomics. - 22 : 7 (2023), p. 1-18. -
További szerzők:Antal-Szalmás Péter (1968-) (laboratóriumi szakorvos) Kurucz István Ferenczi Annamária (1986-) (molekuláris biológus, mikrobiológus) Józsi Mihály Tornyi Ilona (1982-) (molekuláris biológus) Müller Mónika Fekete János Tibor Lamont, John FitzGerald, Peter Gall-Debreceni Anna Kádas János (1976-) (molekuláris biológus, biokémikus, kertészmérnök) Vida András (1979-) (molekuláris biológus, genetikus) Tardieu, Nadège Kieffer, Yann Jullien, Anne Guergova-Kuras, Mariana Hempel, William Kovács András László (1969-) (biológus, biológia-kémia tanár) Kardos Tamás (1980-) (pulmonológus, klinikai onkológus) Bittner Nóra (1963-) (orvos) Csánky Eszter (1959-) (tüdőgyógyász, klinikai immunológus, allergológus) Szilasi Mária (1953-) (tüdőgyógyász, klinikai immunológus, allergológus, belgyógyász) Losonczy György Szondy Klára Gálffy Gabriella Csada Edit Szalontai Klára Somfay Attila Malka, David Cottu, Paul Bogos Krisztina Takács László (1955-) (orvos)
Pályázati támogatás:TECH-09-A1-2009-0113; mAbCHIC
Egyéb
GOP-1.2.1-09-2010-0019
Egyéb
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4.

001-es BibID:BIBFORM069263
Első szerző:Szebeni János
Cím:Plasma Proteome Profiling with Monoclonal Antibody Libraries : a Pilot Biomarker Analysis for Nanomedicine-Induced Complement Activation / Szebeni János, Weiszhár Zsóka, Rozsnyay Zoltán, Martinsky Todd, Kádas János, Lázár József, Takács László, Kurucz István
Dátum:2013
ISSN:2169-0510 2169-0529
Megjegyzések:Complement (C) activation-related hypersensitivity reactions (HSRs) represent an unsolved adverse immune effect of many i.v. administered "nanomedicines", such as liposomal doxorubicin (Doxil/Caelyx). Because these pseudoallergic reactions can be severe or even lethal, it is an important clinical objective to find biomarkers for proneness for C activa-tion by reactogenic nanoparticles that will allow the prediction of in vivo reactions by in vitro assays. With this goal in mind we identified a normal human blood donor whose serum consistently showed high sensitivity to Caelyx-induced C activation in vitro (CSS). The plasma of this blood (Caelyx-sensitive plasma, CSP) was subjected to proteome profiling with a library of human plasma proteome specific mAbs. The chip (PlasmaScan-380TM) contained 380 non-redundant (with respect to epitopes) mAbs. The analysis revealed 8 proteins that were differentially represented in CSP in com-parison with Caelyx-insensitive control plasma. These proteins were identified by mass spectrometry and Western blot analyses to represent factor H (decreased in CSP), factor H related protein, serum amyloid P component, fibronectin, complement component C4, Apo B100, prothrombin and alpha-2-HS glycoprotein (all increased in CSP). Some of these protein changes are consistent with proneness for increased C activation, suggesting the potential use of this method in the search for biomarkers for liposome-induced or other types of nanomedicine-induced HSRs.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Hypersensitivity Reactions
Complement Factor H
Serum Amyloid P
Proteome Profiling
Biomarkers
Megjelenés:Advances in Nanoparticles. - 2 : 2 (2013), p. 133-144. -
További szerzők:Weiszhár Zsóka Rozsnyay Zoltán Martinsky, Todd Kádas János (1976-) (molekuláris biológus, biokémikus, kertészmérnök) Lázár József Takács László (1955-) Kurucz István
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Intézményi repozitóriumban (DEA) tárolt változat
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5.

001-es BibID:BIBFORM065041
Első szerző:Székely Andrea
Cím:Multi Capillary SDS-Gel Electrophoresis for the Analysis of Fluorescently Labeled mAb preparations: a high throughput quality control process for the production of QuantiPlasma and PlasmaScan mAb libraries / Andrea Székely, Ákos Szekrényes, Márta Kerékgyártó, Attila Balogh, János Kádas, József Lázár, András Guttman, István Kurucz, László Takács
Dátum:2014
ISSN:0173-0835
Megjegyzések:Molecular heterogeneity of mAb preparations is the result of various co- and post-translational modifications and to contaminants related to the production process. Changes in molecular composition results in alterations of functional performance, therefore quality control and validation of therapeutic or diagnostic protein products is essential. A special case is the consistent production of mAb libraries (QuantiPlasma? and PlasmaScan?) for proteome profiling, quality control of which represents a challenge because of high number of mAbs (>1000). Here, we devise a generally applicable multicapillary SDS-gel electrophoresis process for the analysis of fluorescently labeled mAb preparations for the high throughput quality control of mAbs of the QuantiPlasma? and PlasmaScan? libraries.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
capillary electrophoresis
glycoform
mAb proteomics
quality control
SDS
Megjelenés:Electrophoresis. - 35 : 15 (2014), p. 2155-2162. -
További szerzők:Szekrényes Ákos (1983-) (vegyészmérnök) Kerékgyártó Márta (1987-) (molekuláris biológus) Balogh Attila Kádas János (1976-) (molekuláris biológus, biokémikus, kertészmérnök) Lázár József Guttman András (1954-) (vegyészmérnök) Kurucz István Takács László (1955-)
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