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1.

001-es BibID:BIBFORM058347
Első szerző:Guttmann Miklós
Cím:Comparative glycoprofiling of HIV gp120 immunogens by capillary electrophoresis and MALDI mass spectrometry / Miklós Guttman, Csaba Váradi, Kelly K. Lee, András Guttman
Dátum:2015
ISSN:0173-0835
Megjegyzések:The Human Immunodeficiency Virus (HIV) envelope glycoprotein (Env) is the primary antigenic feature on the surface of the virus and is of key importance in HIV vaccinology. Vaccine trials with the gp120 subunit of Env are ongoing with the recent RV144 trial showing moderate efficacy. gp120 is densely covered with N-linked glycans that are thought to help evade the host's humoral immune response. To assess how the global glycosylation patterns vary between gp120 constructs, the glycan profiles of several gp120s were examined by capillary electrophoresis with laser induced fluorescence detection and MALDI-MS. The glycosylation profiles were found to be similar for chronic vs. transmitter/founder isolates and only varied moderately between gp120s from different clades. This study revealed that the addition of specific tags, such as the gD tag used in the RV144 trial, had significant effects on the overall glycosylation patterns. Such effects are likely to influence the immunogenicity of various Env immunogens and should be considered for future vaccine strategies, emphasizing the importance of the glycosylation analysis approach described in this paper.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
HIV glycosylation
Megjelenés:Electrophoresis 36 : 11-12 (2015), p. 1305-1313. -
További szerzők:Váradi Csaba (1988-) (molekuláris biológus) Lee, Kelly K. Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:NIH F32-GM097805
Egyéb
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2.

001-es BibID:BIBFORM037888
035-os BibID:PMID:22467923 WOS:000303975300009
Első szerző:Meskó Bertalan (kutatóorvos)
Cím:Peripheral blood gene expression and IgG glycosylation profiles as markers of tocilizumab treatment in rheumatoid arthritis / Bertalan Mesko, Szilárd Póliska, Szilvia Szamosi, Zoltán Szekanecz, János Podani, Csaba Váradi, András Guttman, László Nagy
Dátum:2012
ISSN:0315-162X
Megjegyzések:Objective. Tocilizumab, a humanized anti-interleukin-6 receptor monoclonal antibody, has recentlybeen approved as a biological therapy for rheumatoid arthritis (RA) and other diseases. It is not knownif there are characteristic changes in gene expression and immunoglobulin G glycosylation during therapyor in response to treatment.Methods. Global gene expression profiles from peripheral blood mononuclear cells of 13 patients withRA and active disease at Week 0 (baseline) and Week 4 following treatment were obtained together withclinical measures, serum cytokine levels using ELISA, and the degree of galactosylation of the IgG Nglycanchains. Gene sets separating responders and nonresponders were tested using canonical variatesanalysis. This approach also revealed important gene groups and pathways that differentiate respondersfrom nonresponders.Results. Fifty-nine genes showed significant differences between baseline and Week 4 and thus correlatedwith treatment. Significantly, 4 genes determined responders after correction for multiple testing. Tenof the 12 genes with the most significant changes were validated using real-time quantitative polymerasechain reaction. An increase in the terminal galactose content of N-linked glycans of IgG was observed inresponders versus nonresponders, as well as in treated samples versus samples obtained at baseline.Conclusion. As a preliminary report, gene expression changes as a result of tocilizumab therapy in RAwere examined, and gene sets discriminating between responders and nonresponders were found andvalidated. A significant increase in the degree of galactosylation of IgG N-glycans in patients with RAtreated with tocilizumab was documented.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
egyetemen (Magyarországon) készült közlemény
Megjelenés:The Journal of Rheumatology 39 : 5 (2012), p. 916-928. -
További szerzők:Póliska Szilárd (1978-) (biológus) Szamosi Szilvia (1975-) (belgyógyász, reumatológus) Szekanecz Zoltán (1964-) (reumatológus, belgyógyász, immunológus) Podani János Váradi Csaba (1988-) (molekuláris biológus) Guttman András (1954-) (vegyészmérnök) Nagy László (1966-) (molekuláris sejtbiológus, biokémikus)
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3.

001-es BibID:BIBFORM084931
Első szerző:Szekrényes Ákos (vegyészmérnök)
Cím:Multi-Site N-glycan mapping study 1: Capillary electrophoresis ? laser induced fluorescence / Szekrényes Ákos, Park SungAe Suhr, Santos Marcia, Lew Clarence, Jones Aled, Haxo Ted, Kimzey Michael, Pourkaveh Shiva, Szabó Zoltán, Sosic Zoran, Feng Peng, Váradi Csaba, de l'Escaille François, Falmagne Jean-Bernard, Sejwal Preeti, Niedringhaus Thomas, Michels David, Freckleton Gordon, Hamm Melissa, Manuilov Anastasiya, Schwartz Melissa, Luo Jiann-Kae, van Dyck Jonathan, Leung Pui-King, Olajos Marcell, Gu Yingmei, Gao Kai, Wang Wenbo, Wegstein Jo, Tep Samnang, Guttman András
Dátum:2016
ISSN:1942-0862 1942-0870
Megjegyzések:An international team that included 20 independent laboratories from biopharmaceutical companies, universities, analytical contract laboratories and national authorities in the United States, Europe and Asia was formed to evaluate the reproducibility of sample preparation and analysis of N-glycans using capillary electrophoresis of 8-aminopyrene1,3,6-trisulfonic acid (APTS)-labeled glycans with laser induced fluorescence (CE-LIF) detection (16 sites) and ultra highperformance liquid chromatography (UHPLC, 12 sites; results to be reported in a subsequent publication). All participants used the same lot of chemicals, samples, reagents, and columns/capillaries to run their assays. Migration time, peak area and peak area percent values were determined for all peaks with >0.1% peak area. Our results demonstrated low variability and high reproducibility, both, within any given site as well across all sites, which indicates that a standard N-glycan analysis platform appropriate for general use (clone selection, process development, lot release, etc.) within the industry can be established.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Biotherapeutics
Capillary electrophoresis
Intercompany study
N-glycans
Megjelenés:mAbs. - 8 : 1 (2016), p. 56-64. -
További szerzők:Park, SungAe Suhr Santos, Marcia Lew, Clarence Jones, Aled Haxo, Ted Kimzey, Michael Pourkaveh, Shiva Szabó Zoltán Sosic, Zoran Feng, Peng Váradi Csaba (1988-) (molekuláris biológus) de l'Escaille, François Falmagne, Jean-Bernard Sejwal, Preeti Niedringhaus, Thomas Michels, David Freckleton, Gordon Hamm, Melissa Manuilov, Anastasiya Schwartz, Melissa Luo, Jiann-Kae van Dyck, Jonathan Leung, Pui-King Olajos Marcell Gu, Yingmei Gao, Kai Wang, Wenbo Wegstein, Jo Tep, Samnang Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:K 116263
NKFIH
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4.

001-es BibID:BIBFORM077852
035-os BibID:(PMID)29330871 (Scopus)85041568961 (WOS)000429417500010
Első szerző:Szekrényes Ákos (vegyészmérnök)
Cím:Multi-site N-Glycan mapping study 2 : UHPLC / Ákos Szekrényes, SungAe Suhr Park, Eoin Cosgrave, Aled Jones, Ted Haxo, Michael Kimzey, Shiva Pourkaveh, Zoltán Szabó, Zoran Sosic, Peng Feng, Preeti Sejwal, Kelsey Dent, David Michels, Gordon Freckleton, Jun Qian, Catherine Lancaster, Toni Duffy, Melissa Schwartz, Jiann-Kae Luo, Jonathan van Dyck, Pui-King Leung, Marcell Olajos, Ronald Kowle, Kai Gao, Wenbo Wang, Jo Wegstein, Samnang Tep, Apolka Domokos, Csaba Váradi, András Guttman
Dátum:2018
ISSN:0173-0835 1522-2683
Megjegyzések:In the first part of this publication, the results from an international study evaluating theprecision (i.e., repeatability and reproducibility) of N-glycosylation analysis using capillaryelectrophoresis of APTS-labeled N-glycans were presented. The corresponding resultsfrom ultra-high performance liquid chromatography (UHPLC) with fluorescence detectionare presented here from 12 participating sites. All participants used the same lot of samples,reagents, and columns to perform the assays. Elution time, peak area and peak areapercent values were determined for all peaks 0.1% peak area, and statistical analysis wasperformed following ISO 5725-2 guideline principles. The results demonstrated adequatereproducibility, within any given site as well across all sites, indicating that standardUHPLC-based N-glycan analysis platforms are appropriate for general use
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
2-AB
Biotherapeutics
Intercompany study
N-glycans
UHPLC
Megjelenés:Electrophoresis. - 39 : 7 (2018), p. 998-1005. -
További szerzők:Park, SungAe Suhr Cosgrave, Eoin Jones, Aled Haxo, Ted Kimzey, Michael Pourkaveh, Shiva Szabó Zoltán (orvos) Sosic, Zoran Feng, Peng Sejwal, Preeti Dent, Kelsey Michels, David Freckleton, Gordon Qian, Jun Lancaster, Catherine Duffy, Toni Schwartz, Melissa Luo, Jiann-Kae van Dyck, Jonathan Leung, Pui-King Olajos Marcell Kowle, Ronald Gao, Kai Wang, Wenbo Wegstein, Jo Tep, Samnang Domokos Apolka Váradi Csaba (1988-) (molekuláris biológus) Guttman András (1954-) (vegyészmérnök)
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5.

001-es BibID:BIBFORM058348
Első szerző:Szekrényes Ákos (vegyészmérnök)
Cím:Sample preparation for N-glycosylation analysis of therapeutic monoclonal antibodies by electrophoresis / Ákos Szekrényes, Jan Partyka, Csaba Varadi, Jana Krenkova, Frantisek Foret, András Guttman
Dátum:2015
Megjegyzések:There are a considerable number of biopharmaceuticals that have been approved for clinical use in the past decade. Over half of these new generation drugs are glycoproteins, such as monoclonal antibodies or other recombinant glycoproteins, which are mostly produced in mammalian cell lines. The linked carbohydrate moieties affect not only their physicochemical properties and thermal stability but also crucial features like receptor-binding activity, circulating half-life, as well as immunogenicity. The structural diversity of these attached glycans can be manifested in altered monosaccharide composition and linkages/positions among the monosaccharide building blocks. In addition, as more and more biosimilar products hit the market, understanding the effects of their glycosylation modification has become a recent target in efficacy and safety issues. To ensure consistent quality of these products, glycosylation profiles have to be monitored and controlled in all steps of the manufacturing process, i.e., from clone selection to lot release. In this paper, we describe some of the recently introduced and commonly used sample preparation techniques for capillary electrophoresis (CE)-based profiling and structural elucidation of N-glycans. The presented protocols include protein A affinity partitioning of monoclonal antibodies (mAbs), enzymatic release of the N-linked glycans, labeling of the liberated carbohydrates, reaction mixture purification techniques to remove the excess labeling reagent, and high-resolution and rapid capillary electrophoresis-laser-induced fluorescence (CE-LIF)-based profiling of the labeled and purified N-glycans.
ISBN:978-1-4939-2353-3
Tárgyszavak:Orvostudományok Elméleti orvostudományok könyvfejezet
N-glycosylation analysis
Megjelenés:Microchip Capillary Electrophoresis Protocols : Methods in Molecular Biology / Ann Van Schepdael. - p. 183-195. -
További szerzők:Partyka, Jan Váradi Csaba (1988-) (molekuláris biológus) Krenkova, Jana Foret, František Guttman András (1954-) (vegyészmérnök)
Internet cím:DOI
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6.

001-es BibID:BIBFORM058339
Első szerző:Váradi Csaba (molekuláris biológus)
Cím:Combination of IgG N-glycomics and corresponding transcriptomics data to identify anti-TNFα treatment responders in inflammatory diseases / Csaba Váradi, Zsolt Holló, Szilárd Póliska, László Nagy, Zoltán Szekanecz, Andrea Váncsa, Károly Palatka, András Guttman
Dátum:2015
ISSN:0173-0835
Megjegyzések:Prediction of responsiveness in biological therapies is an important and challenging issue in different diseases. Analyzing glycosylation pattern changes of key serum glycoproteins is one of the possible avenues to follow disease remission. The aim of this study was to investigate the changes of serum IgG glycoforms in Crohn's disease (CD) and rheumatoid arthritis patients in response to antitumor necrosis factor alpha (anti-TNF-?) treatment. IgG was isolated from patient serum samples using Protein A affinity pull-down, followed by the release of N-glycans with peptide-N-glycosidase F. The released glycans were fluorescently tagged with 8-aminopyrene-1,3,6-trisulfonate and analyzed by CGE with laser-induced fluorescent detection. Significant alterations were detected between responders and nonresponders in both disease groups. In CD patients, disease-specific alteration was found in response to anti-TNF-? therapy, which was also confirmed by transcriptomics data analysis of the corresponding glycosyltransferases and glycosidases.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
glikozilacio
Megjelenés:Electrophoresis. - 36 : 11-12 (2015), p. 1330-1335. -
További szerzők:Holló Zsolt Póliska Szilárd (1978-) (biológus) Nagy László (1966-) (molekuláris sejtbiológus, biokémikus) Szekanecz Zoltán (1964-) (reumatológus, belgyógyász, immunológus) Váncsa Andrea (1972-) (orvos) Palatka Károly (1961-) (belgyógyász, gasztroenterológus) Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:MTA-PE Translational Glycomics
MTA
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7.

001-es BibID:BIBFORM058340
035-os BibID:(WoS)000337643500017 (Scopus)84902789927
Első szerző:Váradi Csaba (molekuláris biológus)
Cím:Rapid Magnetic Bead Based Sample Preparation for Automated and High Throughput N-Glycan Analysis of Therapeutic Antibodies / Csaba Váradi, Clarence Lew, András Guttman
Dátum:2014
ISSN:0003-2700
Megjegyzések:Full automation to enable high throughput N-glycosylation profiling and sequencing with good reproducibility is vital to fulfill the contemporary needs of the biopharmaceutical industry and requirements of national regulatory agencies. The most prevalently used glycoanalytical methods of capillary electrophoresis and hydrophilic interaction liquid chromatography, while very efficient, both necessitate extensive sample preparation and cleanup, including glycoprotein capture, N-glycan release, fluorescent derivatization, purification, and preconcentration steps during the process. Currently used protocols to fulfill these tasks require multiple centrifugation and vacuum-centrifugation steps, making liquid handling robot mediated automated sample preparation difficult and expensive. In this paper we report on a rapid magnetic bead based sample preparation approach that enables full automation including all the process phases just in a couple of hours without requiring any centrifugation and/or vacuum centrifugation steps. This novel protocol has been compared to conventional glycan sample preparation strategies using standard glycoproteins (IgG, fetuin, and RNase B) and featured rapid processing time, high release and labeling efficiency, good reproducibility, and the potential of easy automation.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
glycan preparation
Megjelenés:Analytical Chemistry. - 86 : 12 (2014), p. 5682-5687. -
További szerzők:Lew, Clarence Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:MTA-PE Translation Glycomics project
MTA
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8.

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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