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30 results on '"Dreisbach, Annette"'

4. Safety and immunogenicity of an investigational maternal trivalent group B streptococcus vaccine in pregnant women and their infants: Results from a randomized placebo-controlled phase II trial

Author

Swamy, Geeta K., primary, Metz, Torri D., additional, Edwards, Kathryn M., additional, Soper, David E., additional, Beigi, Richard H., additional, Campbell, James D., additional, Grassano, Luca, additional, Buffi, Giada, additional, Dreisbach, Annette, additional, Margarit, Immaculada, additional, Karsten, Annette, additional, Henry, Ouzama, additional, Lattanzi, Maria, additional, and Bebia, Zourab, additional

Published
2020
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5. Tryptic Shaving of Staphylococcus aureus Unveils Immunodominant Epitopes on the Bacterial Cell Surface

Author

Dreisbach, Annette, primary, Wang, Min, additional, van der Kooi-Pol, Magdalena M., additional, Reilman, Ewoud, additional, Koedijk, Dennis G. A. M., additional, Mars, Ruben A. T., additional, Duipmans, José, additional, Jonkman, Marcel, additional, Benschop, Joris J., additional, Bonarius, Hendrik P. J., additional, Groen, Herman, additional, Hecker, Michael, additional, Otto, Andreas, additional, Bäsell, Katrin, additional, Bernhardt, Jörg, additional, Back, Jaap Willem, additional, Becher, Dörte, additional, Buist, Girbe, additional, and van Dijl, Jan Maarten, additional

Published
2020
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6. Safety and immunogenicity of fully liquid and lyophilized formulations of an investigational trivalent group B streptococcus vaccine in healthy non-pregnant women: Results from a randomized comparative phase II trial

Author

Beran, Jiri, primary, Leroux-Roels, Geert, additional, Van Damme, Pierre, additional, de Hoon, Jan, additional, Vandermeulen, Corinne, additional, Al-Ibrahim, Mohamed, additional, Johnson, Casey, additional, Peterson, James, additional, Baker, Sherryl, additional, Seidl, Claudia, additional, Dreisbach, Annette, additional, Karsten, Annette, additional, Corsaro, Bartholomew, additional, Henry, Ouzama, additional, Lattanzi, Maria, additional, and Bebia, Zourab, additional

Published
2020
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7. Tryptic Shaving of Staphylococcus aureusUnveils Immunodominant Epitopes on the Bacterial Cell Surface

Author

Dreisbach, Annette, Wang, Min, van der Kooi-Pol, Magdalena M., Reilman, Ewoud, Koedijk, Dennis G. A. M., Mars, Ruben A. T., Duipmans, José, Jonkman, Marcel, Benschop, Joris J., Bonarius, Hendrik P. J., Groen, Herman, Hecker, Michael, Otto, Andreas, Bäsell, Katrin, Bernhardt, Jörg, Back, Jaap Willem, Becher, Dörte, Buist, Girbe, and van Dijl, Jan Maarten

Abstract

The opportunistic pathogen Staphylococcus aureushas become a major threat for human health and well-being by developing resistance to antibiotics and by fast evolution into new lineages that rapidly spread within the healthy human population. This calls for development of active or passive immunization strategies to prevent or treat acute phase infections. Since no such anti-staphylococcal immunization approaches are available for clinical implementation, the present studies were aimed at identifying new leads for their development. For this purpose, we profiled the cell-surface-exposed staphylococcal proteome under infection-mimicking conditions by combining two approaches for “bacterial shaving” with immobilized or soluble trypsin and subsequent mass spectrometry analysis of liberated peptides. In parallel, non-covalently cell-wall-bound proteins extracted with potassium thiocyanate and the exoproteome fraction were analyzed by gel-free proteomics. All data are available through ProteomeXchange accession PXD000156. To pinpoint immunodominant bacterial-surface-exposed epitopes, we screened selected cell-wall-attached proteins of S. aureusfor binding of immunoglobulin G from patients who have been challenged by different types of S. aureusdue to chronic wound colonization. The combined results of these analyses highlight particular cell-surface-exposed S. aureusproteins with highly immunogenic exposed epitopes as potential targets for development of protective anti-staphylococcal immunization strategies.

Published
2020
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8. The Ins and Outs of the Bacillus subtilis Membrane Proteome

Author

van Dijl, Jan, Dreisbach, Annette, Skwark, Marcin J, Sibbald, Mark J.J.B, Tjalsma, Harold, Zweers, Jessica, Buist, Girbe, Graumann, Peter, Microbes in Health and Disease (MHD), and Translational Immunology Groningen (TRIGR)

Abstract

Bacterial homeostasis is largely determined by a phospholipid bilayer that encloses the cytoplasm. The proteins residing in this cytoplasmic membrane are responsible for communication between the cytoplasm and extracytoplasmic cell compartments or the extracellular milieu of the cell. This chapter deals with the cytoplasmic membrane proteome of Bacillus subtilis. Specifically, we address current views on the roles of membrane proteins in homeostasis, their membrane targeting and retention signals, machinery for membrane insertion, localization of membrane proteins, membrane protein degradation and, finally, the identified and predicted composition of the B. subtilis membrane proteome. Known mechanisms and knowledge gaps are discussed to give a comprehensive overview of the ins and outs of the B. subtilis membrane proteome.

Published
2012

9. In's and out's of the Bacillus subtilis membrane proteome

Author

van Dijl, Jan Maarten, Dreisbach, Annette, Skwark, Marcin J, Sibbald, Mark, Tjalsma, Harold, Zweers, Jessica, Buist, Girbe, Microbes in Health and Disease (MHD), and Translational Immunology Groningen (TRIGR)

Published
2012

17. Surface shaving as a versatile tool to profile global interactions between human serum proteins and the Staphylococcus aureus cell surface

Author

Dreisbach, Annette, primary, van der Kooi-Pol, Magdalena M., additional, Otto, Andreas, additional, Gronau, Katrin, additional, Bonarius, Hendrik P. J., additional, Westra, Hans, additional, Groen, Herman, additional, Becher, Dörte, additional, Hecker, Michael, additional, and van Dijl, Jan M., additional

Published
2011
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21. Staphylococcal PknB as the First Prokaryotic Representative of the Proline-Directed Kinases

Author

Miller, Malgorzata, primary, Donat, Stefanie, additional, Rakette, Sonja, additional, Stehle, Thilo, additional, Kouwen, Thijs R. H. M., additional, Diks, Sander H., additional, Dreisbach, Annette, additional, Reilman, Ewoud, additional, Gronau, Katrin, additional, Becher, Dörte, additional, Peppelenbosch, Maikel P., additional, van Dijl, Jan Maarten, additional, and Ohlsen, Knut, additional

Published
2010
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24. EPIDERMAL GROWTH FACTOR-MEDIATED ACTIVATION OF THE MAP KINASE CASCADE RESULTS IN ALTERED EXPRESSION AND FUNCTION OF ABCG2 (BCRP)

Author

zu Schwabedissen, Henriette E. Meyer, primary, Grube, Markus, additional, Dreisbach, Annette, additional, Jedlitschky, Gabriele, additional, Meissner, Konrad, additional, Linnemann, Knud, additional, Fusch, Christoph, additional, Ritter, Christoph A., additional, Völker, Uwe, additional, and Kroemer, Heyo K., additional

Published
2006
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25. A comprehensive proteome map of growing Bacillus subtilis cells

Author

Eymann, Christine, primary, Dreisbach, Annette, additional, Albrecht, Dirk, additional, Bernhardt, Jörg, additional, Becher, Dörte, additional, Gentner, Sandy, additional, Tam, Le Thi, additional, Büttner, Knut, additional, Buurman, Gerrit, additional, Scharf, Christian, additional, Venz, Simone, additional, Völker, Uwe, additional, and Hecker, Michael, additional

Published
2004
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28. F420H2 oxidase (FprA) fromMethanobrevibacter arboriphilus, a coenzyme F420-dependent enzyme involved in O2 detoxification.

Author

Seedorf, Henning, Dreisbach, Annette, Hedderich, Reiner, Shima, Seigo, and Thauer, Rudolf K.

Subjects
*OXIDATION-reduction reaction, *FLAVOPROTEINS, *HYDROGEN-ion concentration, *CELL suspensions, *CELL culture, *ENZYMES
Abstract

Cell suspensions ofMethanobrevibacter arboriphiluscatalyzed the reduction of O2 with H2 at a maximal specific rate of 0.4 U (µmol/min) per mg protein with an apparentKm for O2 of 30 µM. The reaction was not inhibited by cyanide. The oxidase activity was traced back to a coenzyme F420-dependent enzyme that was purified to apparent homogeneity and that catalyzed the oxidation of 2 F420H2 with 1 O2 to 2 F420 and 2 H2O. The apparentKm for F420 was 30 µM and that for O2 was 2 µM with aVmax of 240 U/mg at 37°C and pH 7.6, the pH optimum of the oxidase. The enzyme did not use NADH or NADPH as electron donor or H2O2 as electron acceptor and was not inhibited by cyanide. The 45-kDa protein, whose gene was cloned and sequenced, contained 1 FMN per mol and harbored a binuclear iron center as indicated by the sequence motifH-X-E-X-D-X62-H-X18-D-X60-H. Sequence comparisons revealed that the F420H2 oxidase fromM. arboriphilusis phylogenetically closely related to FprA fromMethanothermobacter marburgensis(71% sequence identity), a 45-kDa flavoprotein of hitherto unknown function, and to A-type flavoproteins from bacteria (30-40%), which all have dioxygen reductase activity. With heterologously produced FprA fromM. marburgensisit is shown that this protein is also a highly efficient F420H2 oxidase and that it contains 1 FMN and 2 iron atoms. The presence of F420H2 oxidase in methanogenic archaea may explain why some methanogens, e.g., theMethanobrevibacterspecies in the termite hindgut, cannot only tolerate but thrive under microoxic conditions. [ABSTRACT FROM AUTHOR]

Published
2004
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29. Direct mass spectrometric identification of ABCB1 (P-glycoproteinMDR1) from the apical membrane fraction of human placenta using fourier transform ion cyclotron mass spectrometry

Author

Schwabedissen, Henriette E. Meyer zu, Dreisbach, Annette, Hammer, Elke, Fusch, Christoph, Hecker, Michael, Völker, Uwe, and Kroemer, Heyo K.

Abstract

Identification and quantification of proteins from human tissue by electrophoresis and subsequent mass spectrometry (MS) has been mainly restricted to high abundance, non-membrane-bound molecules. Pharmacologically relevant structures such as cytochrome P450 enzyme, drug transporters and receptors were not accessible by this technology. We developed a method to identify an integral membrane-bound protein (ABCB1) from human placenta using Fourier transform ion cyclotron (FTICR)-MS. Apical and basal membrane fractions were enriched from term human placenta using differential centrifugation. Following SDS-page these fractions were cleaved with trypsin, separated by nano-HPLC and subjected to FTICR-MS. We identified a total of 70 and 89 proteins in the apical and basal membranes, respectively. Among these proteins, and restricted to the apical membrane, was the transport protein ABCB1, with 10 peptides identified by MS, covering a total of 10 of the entire protein. The study describes a method suitable for direct monitoring of membrane-bound proteins from human tissue using FTICR-MS.

Published
2006
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30. Epidermal growth factor-mediated activation of the map kinase cascade results in altered expression and function of ABCG2 (BCRP).

Author

Meyer zu Schwabedissen HE, Grube M, Dreisbach A, Jedlitschky G, Meissner K, Linnemann K, Fusch C, Ritter CA, Völker U, and Kroemer HK

Subjects
ATP Binding Cassette Transporter, Subfamily G, Member 2, ATP-Binding Cassette Transporters analysis, ATP-Binding Cassette Transporters biosynthesis, ATP-Binding Cassette Transporters genetics, Adult, Antineoplastic Agents pharmacology, Cell Line, Cell Line, Tumor, Cells, Cultured, Dose-Response Relationship, Drug, Drug Resistance, Enzyme Activation drug effects, Extracellular Signal-Regulated MAP Kinases antagonists & inhibitors, Female, Gestational Age, Humans, JNK Mitogen-Activated Protein Kinases antagonists & inhibitors, MAP Kinase Signaling System, Neoplasm Proteins analysis, Neoplasm Proteins biosynthesis, Neoplasm Proteins genetics, Pregnancy, Protein Kinase Inhibitors pharmacology, RNA, Messenger isolation & purification, RNA, Messenger metabolism, Time Factors, Trophoblasts enzymology, ATP-Binding Cassette Transporters metabolism, Epidermal Growth Factor pharmacology, Extracellular Signal-Regulated MAP Kinases metabolism, Gene Expression Regulation, Developmental drug effects, JNK Mitogen-Activated Protein Kinases metabolism, Neoplasm Proteins metabolism, Trophoblasts drug effects
Abstract

Epidermal growth factor (EGF) is a multifunctional growth factor known to play a major role in proliferation and differentiation processes. EGF-induced differentiation is a prerequisite for function of various cell types, among them cytotrophoblasts, a functionally important cellular fraction in human placenta. Stimulation of cytotrophoblasts with EGF results in formation of a multinuclear syncytium representing the feto-maternal interface, which protects the fetus against exogenous substances. It is well established that part of this protection system is based on ATP-binding cassette (ABC) transporters such as ABCG2 (breast cancer resistance protein, BCRP). However, little is known about regulation of transport proteins in the framework of EGF-mediated cellular differentiation. In the present work we show a significant increase of ABCG2 expression by EGF in cytotrophoblasts, BeWo, and MCF-7 cells on both mRNA and protein levels. This increase resulted in decreased sensitivity to the ABCG2 substrates mitoxantrone and topotecan. In each cell type, EGF increases expression of ABCG2 by activation of mitogen-activated protein kinase cascade via phosphorylation of extracellular regulated kinase (ERK)1/2 and c-jun NH-terminal kinase/stress-activated protein kinase (JNK/SAPK). Consequently, the increase of ABCG2 by EGF was abolished by pretreatment of cells with the tyrosine kinase inhibitor 4-(3-chloroanillino)-6,7-dimethoxyquinazoline (AG1478) or the mitogen-activated protein kinase kinase inhibitor 2'-amino-3'methoxyflavone (PD 98059), thereby reestablishing sensitivity toward mitoxantrone. Moreover, analysis of ABCG2 expression during placental development revealed a significant increase in preterm versus term placenta. Taken together, our data show regulation of ABCG2 expression by EGF. In view of EGF signal transduction as a target for drugs (e.g., gefitinib), which are in turn substrates and/or inhibitors of ABCG2, this regulation has therapeutic consequences.

Published
2006
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