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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:BIBFORM082276
Első szerző:Guergova-Kuras, Mariana
Cím:Discovery and validation of a plasma protein biomarker panel for early detection of non small cell lung cancer / Mariana Guergova-Kuras, Istvan Kurucz, William Hempel, Nadège Tardieu, János Kádas, Carole Malderez-Bloes, Yann Kieffer, Anne Jullien, Eszter Csanky, Laszlo Takacs
Dátum:2011
ISSN:1556-0864
Tárgyszavak:Orvostudományok Elméleti orvostudományok poszter
folyóiratcikk
Megjelenés:Journal of Thoracic Oncology. - 6 : 6 (2011), p. S1339-S1339. -
További szerzők:Kurucz István Hempel, William Tardieu, Nadège Kádas János (1976-) (molekuláris biológus, biokémikus, kertészmérnök) Malderez-Bloes, Carole Kieffer, Yann Jullien, Anne Csánky Eszter (1959-) (tüdőgyógyász, klinikai immunológus, allergológus) Takács László (1955-)
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3.

001-es BibID:BIBFORM023718
035-os BibID:(cikkazonosító)M111.010298 (WoS)000298290300017 (Scopus)83055168546
Első szerző:Guergova-Kuras, Mariana
Cím:Discovery of lung cancer biomarkers by profiling the plasma proteome with monoclonal antibody libraries / Mariana Guergova-Kuras, István Kurucz, William Hempel, Nadege Tardieu, János Kádas, Carole Malderez-Bloes, Anne Jullien, Yann Kieffer, Marina Hincapie, András Guttman, Eszter Csánky, Balázs Dezső, Barry L. Karger, László Takács
Dátum:2011
ISSN:1535-9476 1535-9484
Megjegyzések:A challenge in the treatment of lung cancer is the lack of early diagnostics. Here, we describe the application of monoclonal antibody (mAb) proteomics for discovery of a panel of biomarkers for early detection (stage I) of non small cell lung cancer (NSCLC). We produced large monoclonal antibody libraries directed against the natural form of protein antigens present in the plasma of NSCLC patients. Plasma biomarkers associated with the presence of lung cancer were detected via high throughput ELISA. Differential profiling of plasma proteomes of four clinical cohorts, totalling 301 patients with lung cancer and 235 healthy controls, identified 13 lung cancer associated (p<0.05) monoclonal antibodies. The mAbs recognize five different cognate proteins identified using immunoprecipitation followed by mass spectrometry. Four of the five antigens were present in non-small cell lung cancer cells in-situ. The approach is capable of generating independent antibodies against different epitopes of the same proteins, allowing fast translation to multiplexed sandwich assays. Based on these results, we have verified in two independent clinical collections a panel of five biomarkers for classifying patient disease status with a diagnostics performance of 77% sensitivity and 87% specificity. Combining CYFRA, an established cancer marker, with the panel resulted in a performance of 83 % sensitivity at 95 % specificity for stage I NSCLC.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Molecular and Cellular Proteomics. - 10 : 12 (2011), p. 1-14. -
További szerzők:Kurucz István Hempel, William Tardieu, Nadège Kádas János (1976-) (molekuláris biológus, biokémikus, kertészmérnök) Malderez-Bloes, Carole Jullien, Anne Kieffer, Yann Hincapie, Marina Guttman András (1954-) (vegyészmérnök) Csánky Eszter (1959-) (tüdőgyógyász, klinikai immunológus, allergológus) Karger, Barry Takács László (1955-) Dezső Balázs (1951-) (pathológus)
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4.

001-es BibID:BIBFORM069259
Első szerző:Hajdú István (Dunakeszi)
Cím:Monoclonal antibody proteomics : use of antibody mimotope displaying phages and the relevant synthetic peptides for mAb scouting / Hajdú István, Flachner Beáta, Bognár Melinda, Végh Barbara M., Dobi Krisztina, Lőrincz Zsolt, Lázár József, Cseh Sándor, Takács László, Kurucz István
Dátum:2014
ISSN:0165-2478
Megjegyzések:Monoclonal antibody proteomics uses nascent libraries or cloned (PlasmascanTM, QuantiPlasmaTM)libraries of mAbs that react with individual epitopes of proteins in the human plasma. At the initialphase of library creation, cognate protein antigen and the epitope interacting with the antibodies arenot known. Scouting for monoclonal antibodies (mAbs) with the best binding characteristics is of highimportance for mAb based biomarker assay development. However, in the absence of the identity ofthe cognate antigen the task represents a challenge. We combined phage display, and surface plasmonresonance (Biacore) experiments to test whether specific phages and the respective mimotope peptidesobtained from large scale studies are applicable to determine key features of antibodies for scouting. Weshow here that mAb captured phage-mimotope heterogeneity that is the diversity of the selected peptidesequences, is inversely correlated with an important binding descriptor; the off-rate of the antibodies andthat represents clues for driving the selection of useful mAbs for biomarker assay development. Carefullychosen synthetic mimotope peptides are suitable for specificity testing in competitive assays using thetarget proteome, in our case the human plasma.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Proteomics
Monoclonal antibod
y Phage-display
Surface plasmon resonance
Affinity
Megjelenés:Immunology Letters. - 160 : 2 (2014), p. 172-177. -
További szerzők:Flachner Beáta Bognár Melinda Végh Barbara M. Dobi Krisztina Lőrincz Zsolt (1979-) (Biológus) Lázár József Cseh Sándor (1954-) (állatorvos) Takács László (1955-) Kurucz István
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5.

001-es BibID:BIBFORM050944
Első szerző:Kerékgyártó Márta (molekuláris biológus)
Cím:Neoglycoproteins as carbohydrate antigens : synthesis, analysis, and polyclonal antibody response / Márta Kerékgyártó, Anikó Fekete, Zoltán Szurmai, János Kerékgyártó, László Takács, István Kurucz, András Guttman
Dátum:2013
ISSN:0173-0835
Megjegyzések:The analysis and polyclonal antibody response for newly synthesized maltose-BSA conjugate neoglycoproteins is described. In this first proof of concept study, a simple carbohydrate antigen, maltose, was linked to BSA by reductive amination. An aglycone spacer was utilized to conserve the intact annular maltose structure and to promote the accessibility of the carbohydrate immunogen hapten during immunization. The neoglycoproteins were investigated by CGE and the number of conjugated maltose residues was determined by MALDI-TOF MS. The neoglycoproteins were then evaluated by immunization of BALB/c mice and the polyclonal antibody response was tested by ELISA as evidence for the presence of sugar-containing epitope-specific antibodies. Selective antibody binding was demonstrated to the synthesized neoglycoproteins with different (low and high) glycosylation degrees suggesting the possible use of this approach to generate antibodies. Moreover, the polyclonal antibody response was not inhibited by maltose or other simple carbohydrates to confirm presence of the neoglycoprotein-specific antibodies.
Tárgyszavak:Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Carbohydrate antigen
Carbohydrate-specific antibody
ELISA
Neoglyco-protein
Megjelenés:Electrophoresis. - 34 : 16 (2013), p. 2379-2386. -
További szerzők:Fekete Anikó (1973-) (vegyész) Szurmai Zoltán (1953-) (szerves kémikus) Kerékgyártó János (1957-) (biokémikus, vegyész) Takács László (1955-) Kurucz István Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:K-81839
OTKA
TÁMOP-4.2.2.A-11/1/KONV-2012-0023-"VÉD-ELEM"
TÁMOP
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6.

001-es BibID:BIBFORM047885
Első szerző:Kovács András László (biológus, biológia-kémia tanár)
Cím:Fractionation of the human plasma proteome for monoclonal antibody proteomics-based biomarker discovery 2 : antigen identification by dot blot array screening / András Kovács, Zoltán Patai, András Guttman, János Kádas, László Takács, István Kurucz
Dátum:2013
ISSN:0173-0835
Tárgyszavak:Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Electrophoresis. - 34 : 20-21 (2013), p. 3064-3071. -
További szerzők:Patai Zoltán (1987-) (molekuláris biológus) Guttman András (1954-) (vegyészmérnök) Kádas János (1976-) (molekuláris biológus, biokémikus, kertészmérnök) Takács László (1955-) Kurucz István
Pályázati támogatás:K-81839 OTKA
OTKA
TÁMOP-4.2.2/B-10/1-2010-0024
TÁMOP
Molekuláris Orvostudomány Doktori Iskola
TECH-09-A1-2009-0113; mAB-CHIC
Egyéb
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7.

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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8.

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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9.

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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10.

001-es BibID:BIBFORM082285
Első szerző:Takács László
Cím:Non-small cell lung cancer biomarkers : discovery using mab proteomics / L. Takacs, M. Guergova-Kuras, I. Kurucz, N. Tardieu, J. Kadas, C. Malderez-Bloes, A. Jullien, Y. Kieffer, B. Dezso, B. Karger
Dátum:2011
ISSN:0732-183X 1527-7755
Megjegyzések:Background: A challenge in the treatment of lung cancer is the lack of early, pre-symptomatic diagnosis. Here, we describe the application of monoclonal antibody proteomics approach to profile the natural plasma proteome for the discovery of lung cancer biomarkers. Methods: We produced large monoclonal antibody (mAb) libraries directed against the natural form of complex mixtures of protein antigens present in the plasma of non-small cell lung cancer (NSCLC) patients. Lung cancer specific biomarkers in the plasma were detected via high throughput ELISA with mAbs. Antigen identification and specificity of the selected antibodies was determined using immunoprecipitation followed by mass spectrometric analysis. The presence of the biomarkers in non-small cell lung cancer tissues was validated by immunohistochemistry. Results: Differential profiling of plasma proteomes of four clinical collections, totalling 301 patients with lung cancer and 235 healthy controls, identified twenty four monoclonal antibodies recognizing protein biomarkers specific for NSCLC. The majority of the selected mAbs detect antigens present in non-small cell lung cancer cells in-situ. Our study confirms previously reported circumstantial evidences for the association with lung cancer for four of the identified biomarkers and provides an independent validation in larger multi-centric clinical collection for the association of their plasma concentrations to the presence of lung cancer. Multivariate analysis of the biomarker results generated with one of these collections (214 NSCLC cases of which 128 in stage I and 169 healthy controls) yielded a five biomarkers classifier that could discriminate NSCLC cases from healthy controls with 77% sensitivity and 87% specificity. The performance of the classifier was validated in an independent collection and combination with well known a NSCLC biomarkers showed additive effect and combined performance of 84 % sensitivity at 95 % specificity. Conclusions: Using the mAb proteomics approach we have identified a panel of monoclonal antibodies associated with specific protein biomarkers that could be readily transferred to a simple screening test for the early detection of non-small cell lung cancer.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idézhető absztrakt
folyóiratcikk
Megjelenés:Journal of Clinical Oncology. - 29 : 15 suppl. (2011), p. 10561-10561. -
További szerzők:Guergova-Kuras, Mariana Kurucz István Tardieu, Nadège Kádas János (1976-) (molekuláris biológus, biokémikus, kertészmérnök) Malderez-Bloes, Carole Jullien, Anne Kieffer, Yann Dezső Balázs (1951-) (pathológus) Karger, Barry
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11.

001-es BibID:BIBFORM069427
Első szerző:Takács László
Cím:Genomic and proteomic biomarkers in the drug R&D process / Takács László, Debreceni Anna, Kurucz István
Dátum:2013
Tárgyszavak:Orvostudományok Elméleti orvostudományok könyvfejezet
Megjelenés:Chemical Genomics and Proteomics / ed. Ferenc Darvas, András Guttman, György Dormán. - p. 123-142.
További szerzők:Gall-Debreceni Anna Kurucz István
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12.

001-es BibID:BIBFORM043657
Első szerző:Váradi Csaba (molekuláris biológus)
Cím:Analysis of Haptoglobin N-glycome Alterations in Inflammatory and Malignant Lung Diseases by Capillary Electrophoresis / Cs. Varadi, S. Mittermayr, A. Szekrenyes, J. Kadas, L. Takacs, I. Kurucz, A. Guttman
Dátum:2013
ISSN:0173-0835
Megjegyzések:A capillary electrophoresis based method was introduced to compare the N-glycosylation profile ofhaptoglobin in normal and pathologic conditions. To assess the biomarker potential of glycosylationchanges in various lung diseases, haptoglobin was isolated from plasma samples of healthy, pneumonia,chronic obstructive pulmonary disease (COPD) and lung cancer patients by means of two haptoglobinspecific monoclonal antibodies. Haptoglobin N-glycans were then enzymatically released, fluorescentlylabeled and profiled by capillary electrophoresis. Disease associated changes of core and antennaryfucosylation were identified by targeted exoglycosidase digestions and their levels were compared inthe different patient groups. Terms such as of core- and arm-fucosylation degree, as well as branchingdegreewere introduced for easier characterization of the changes and statistical analysis was used toexamine which structures are responsible for the observed differences. Increased level of ?1-6fucosylated tri-antennary glycans was found in all disease groups compared to the control. Elevatedamounts of core- and arm fucosylation on tetra-antennary glycans were detected in the lung cancergroup compared to the COPD group. A larger scale study is necessary to confirm and validate thesepreliminary findings in the glycosylation changes of haptoglobin, so could then be used as biomarkers inthe diagnosis of malignant and inflammatory lung diseases.
Tárgyszavak:Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
biomarker
capillary electrophoresis
Megjelenés:Electrophoresis. - 34 : 16 (2013), p. 2287-2294. -
További szerzők:Mittermayr, Stefan (1983-) (bioinformatikus) Szekrényes Ákos (1983-) (vegyészmérnök) Kádas János (1976-) (molekuláris biológus, biokémikus, kertészmérnök) Takács László (1955-) Kurucz István Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:K-81839
OTKA
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