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2. Cloning and characterization of the glucosidase II alpha subunit gene of Trichoderma reesei: A frameshift mutation results in the aberrant glycosylation profile of the hypercellulolytic strain rut-C30

Author

Geysens, Steven, Pakula, Tiina, Uusitalo, Jaana, Dewerte, Isabelle, Penttila, Merja, and Contreras, Roland

Subjects
Celluloid -- Research, Gene mutations -- Research, Genetic code -- Research, Biological sciences
Abstract

The isolation and characterization of the gene encoding the glycosidase II alpha subunit of the industrially important fungus Trichoderma reesei is described. The gene encoding the glucosidase II alpha subunit in the hypercellulolytic strain Rut-C30 contains a frameshift mutation resulting in a truncated gene product.

Published
2005

6. The 2008 update of the Aspergillus nidulans genome annotation: A community effort

Author

Wortman, Jennifer Russo, Gilsenan, Jane Mabey, Joardar, Vinita, Deegan, Jennifer, Clutterbuck, John, Andersen, Mikael R., Archer, David, Bencina, Mojca, Braus, Gerhard, Coutinho, Pedro, von Doehren, Hans, Doonan, John, Driessen, Arnold J. M., Durek, Pawel, Espeso, Eduardo, Fekete, Erzsebet, Flipphi, Michel, Garcia Estrada, Carlos, Geysens, Steven, Goldman, Gustavo, de Groot, Piet W. J., Hansen, Kim, Harris, Steven D., Heinekamp, Thorsten, Helmstaedt, Kerstin, Henrissat, Bernard, Hofmann, Gerald, Homan, Tim, Horio, Tetsuya, Horiuchi, Hiroyuki, James, Steve, Jones, Meriel, Karaffa, Levente, Karanyi, Zsolt, Kato, Masashi, Keller, Nancy, Kelly, Diane E., Kiel, Jan A. K. W., Kim, Jung-Mi, van der Klei, Ida J., Klis, Frans M., Kovalchuk, Andriy, Krasevec, Nada, Kubicek, Christian P., Liu, Bo, MacCabe, Andrew, Meyer, Vera, Mirabito, Pete, Miskei, Marton, Mos, Magdalena, Mullins, Jonathan, Nelson, David R., Nielsen, Jens, Oakley, Berl R., Osmani, Stephen A., Pakula, Tiina, Paszewski, Andrzej, Paulsen, Ian, Pilsyk, Sebastian, Pocsi, Istvan, Punt, Peter J., Ram, Arthur F. J., Ren, Qinghu, Robellet, Xavier, Robson, Geoff, Seiboth, Bernhard, van Solingen, Piet, Specht, Thomas, Sun, Jibin, Taheri-Talesh, Naimeh, Takeshita, Norio, Ussery, Dave, Vankuyk, Patricia A., Visser, Hans, de Vondervoort, Peter J. I. van, Walton, Jonathan, Xiang, Xin, Xiong, Yi, Zeng, An Ping, Brandt, Bernd W., Cornell, Michael J., van den Hondel, Cees A. M. J. J., Visser, Jacob, Oliver, Stephen G., Turner, Geoffrey, Kraševec, Nada, Kuyk, Patricia A. van, Döhren, D.H., van Seilboth, B, de Vries, R., Institut de génétique et microbiologie [Orsay] (IGM), Université Paris-Sud - Paris 11 (UP11)-Centre National de la Recherche Scientifique (CNRS), Instituto de Agroquimica y Tecnologia de Alimentos (IATA), Instituto de Agroquímica y Tecnología de Alimentos - Institute of Agrochemistry and Food Technology [Valencia] (IATA-CSIC), Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology, Molecular Cell Biology, Faculty of Science and Engineering, Host-Microbe Interactions, Man, Biomaterials and Microbes (MBM), Centre for World Food Studies, Bioinformatics, Bio Informatics (IBIVU), Integrative Bioinformatics, Molecular Biology and Microbial Food Safety (SILS, FNWI), and Mass Spectrometry of Biomacromolecules (SILS, FNWI)

Subjects
GENE-CLUSTER, PREDICTION, Assembly, Biológiai tudományok, CADRE, Genome, Természettudományok, CELL-WALL, Genetics, 0303 health sciences, Fungal protein, biology, MESH: Aspergillus nidulans, MESH: Genomics, Fungal community, Genomics, Genome project, Fungal, Aspergillus, [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology, MESH: Genome, Fungal, Identification (biology), MESH: Fungal Proteins, Genome, Fungal, fungal community, Annotation, Genes, Fungal, Computational biology, Vertebrate and Genome Annotation Project, SEQUENCE, Microbiology, Article, Aspergillus nidulans, Fungal Proteins, 03 medical and health sciences, transcription factors, Transcription factors, BIOSYNTHESIS, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, A-FUMIGATUS, genome, 030304 developmental biology, IDENTIFICATION, 030306 microbiology, DNA, NIGER, biology.organism_classification, TRANSCRIPTIONAL ACTIVATOR, Genes, Aspergilli, MESH: Genes, Fungal
Abstract

12 páginas, 2 tablas -- PAGS nros. S2-S13, et al, The identification and annotation of protein-coding genes is one of the primary goals of whole-genome sequencing projects, and the accuracy of predicting the primary protein products of gene expression is vital to the interpretation of the available data and the design of downstream functional applications. Nevertheless, the comprehensive annotation of eukaryotic genomes remains a considerable challenge. Many genomes submitted to public databases, including those of major model organisms, contain significant numbers of wrong and incomplete gene predictions. We present a community-based reannotation of the Aspergillus nidulans genome with the primary goal of increasing the number and quality of protein functional assignments through the careful review of experts in the field of fungal biology, We acknowledge financial support by the European Commission under contract LSSG-CT-2005-018964

Published
2009
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7. In vivo synthesis of mammalian-like, hybrid-type N-glycans in pichia pastoris

Author

Vervecken, Wouter, Kiagorodov, Vladimir, Callewaert, Nico, Geysens, Steven, Vusser, Kristof De, and Contreras, Roland

Subjects
Glycosylation -- Research, Transferases -- Research, Endoplasmic reticulum -- Research, Microbiology -- Research, Biological sciences
Abstract

An engineering of the P. pastoris N-glycosylation pathway to produce nonhyperglycosylated hybrid glycans are described. This is done by inactivation of OCH1 and over expression of an alpha-1,2-mannosidase retained in the endoplasmic reticulum and N-acetyglucosaminyltransferase I and beta-1,4-hybrid-type N-linked oligosaccharide structure on its glycoproteins.

Published
2004

8. Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88

Author

Pel, Herman J., de Winde, Johannes H., Archer, David B., Dyer, Paul S., Hofmann, Gerald, Schaap, Peter J., Turner, Geoffrey, de Vries, Ronald P., Albang, Richard, Albermann, Kaj, Andersen, Mikael R., Bendtsen, Jannick D., Benen, Jacques A. E., van den Berg, Marco, Breestraat, Stefaan, Caddick, Mark X., Contreras, Roland, Cornell, Michael, Coutinho, Pedro M., Danchin, Etienne G. J., Debets, Alfons J. M., Dekker, Peter, van Dijck, Piet W. M., van Dijk, Alard, Dijkhuizen, Lubbert, Driessen, Arnold J. M., d'Enfert, Christophe, Geysens, Steven, Goosen, Coenie, Groot, Gert S. P., de Groot, Piet W. J., Guillemette, Thomas, Henrissat, Bernard, Herweijer, Marga, van den Hombergh, Johannes P. T. W., van den Hondel, Cees A. M. J. J., van der Heijden, Rene T. J. M., van der Kaaij, Rachel M., Klis, Frans M., Kools, Harrie J., Kubicek, Christian P., van Kuyk, Patricia A., Lauber, Juergen, Lu, Xin, van der Maarel, Marc J. E. C., Meulenberg, Rogier, Menke, Hildegard, Mortimer, Martin A., Nielsen, Jens, Oliver, Stephen G., Olsthoorn, Maurien, Pal, Karoly, van Peij, Noel N. M. E., Ram, Arthur F. J., Rinas, Ursula, Roubos, Johannes A., Sagt, Cees M. J., Schmoll, Monika, Sun, Jibin, Ussery, David, Varga, Janos, Vervecken, Wouter, de Vondervoort, Peter J. J. van, Wedler, Holger, Wosten, Han A. B., Zeng, An-Ping, van Ooyen, Albert J. J., Visser, Jaap, Stam, Hein, Pel, Herman J., de Winde, Johannes H., Archer, David B., Dyer, Paul S., Hofmann, Gerald, Schaap, Peter J., Turner, Geoffrey, de Vries, Ronald P., Albang, Richard, Albermann, Kaj, Andersen, Mikael R., Bendtsen, Jannick D., Benen, Jacques A. E., van den Berg, Marco, Breestraat, Stefaan, Caddick, Mark X., Contreras, Roland, Cornell, Michael, Coutinho, Pedro M., Danchin, Etienne G. J., Debets, Alfons J. M., Dekker, Peter, van Dijck, Piet W. M., van Dijk, Alard, Dijkhuizen, Lubbert, Driessen, Arnold J. M., d'Enfert, Christophe, Geysens, Steven, Goosen, Coenie, Groot, Gert S. P., de Groot, Piet W. J., Guillemette, Thomas, Henrissat, Bernard, Herweijer, Marga, van den Hombergh, Johannes P. T. W., van den Hondel, Cees A. M. J. J., van der Heijden, Rene T. J. M., van der Kaaij, Rachel M., Klis, Frans M., Kools, Harrie J., Kubicek, Christian P., van Kuyk, Patricia A., Lauber, Juergen, Lu, Xin, van der Maarel, Marc J. E. C., Meulenberg, Rogier, Menke, Hildegard, Mortimer, Martin A., Nielsen, Jens, Oliver, Stephen G., Olsthoorn, Maurien, Pal, Karoly, van Peij, Noel N. M. E., Ram, Arthur F. J., Rinas, Ursula, Roubos, Johannes A., Sagt, Cees M. J., Schmoll, Monika, Sun, Jibin, Ussery, David, Varga, Janos, Vervecken, Wouter, de Vondervoort, Peter J. J. van, Wedler, Holger, Wosten, Han A. B., Zeng, An-Ping, van Ooyen, Albert J. J., Visser, Jaap, and Stam, Hein

Abstract

The filamentous fungus Aspergillus niger is widely exploited by the fermentation industry for the production of enzymes and organic acids, particularly citric acid. We sequenced the 33.9-megabase genome of A. niger CBS 513.88, the ancestor of currently used enzyme production strains. A high level of synteny was observed with other aspergilli sequenced. Strong function predictions were made for 6,506 of the 14,165 open reading frames identified. A detailed description of the components of the protein secretion pathway was made and striking differences in the hydrolytic enzyme spectra of aspergilli were observed. A reconstructed metabolic network comprising 1,069 unique reactions illustrates the versatile metabolism of A. niger. Noteworthy is the large number of major facilitator superfamily transporters and fungal zinc binuclear cluster transcription factors, and the presence of putative gene clusters for fumonisin and ochratoxin A synthesis.

Published
2007

9. Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88

Author

Sub Molecular Microbiology, Molecular Microbiology, Pel, Herman J., de Winde, Johannes H., Archer, David B., Dyer, Paul S., Hofmann, Gerald, Schaap, Peter J., Turner, Geoffrey, de Vries, Ronald P., Albang, Richard, Albermann, Kaj, Andersen, Mikael R., Bendtsen, Jannick D., Benen, Jacques A. E., van den Berg, Marco, Breestraat, Stefaan, Caddick, Mark X., Contreras, Roland, Cornell, Michael, Coutinho, Pedro M., Danchin, Etienne G. J., Debets, Alfons J. M., Dekker, Peter, van Dijck, Piet W. M., van Dijk, Alard, Dijkhuizen, Lubbert, Driessen, Arnold J. M., d'Enfert, Christophe, Geysens, Steven, Goosen, Coenie, Groot, Gert S. P., de Groot, Piet W. J., Guillemette, Thomas, Henrissat, Bernard, Herweijer, Marga, van den Hombergh, Johannes P. T. W., van den Hondel, Cees A. M. J. J., van der Heijden, Rene T. J. M., van der Kaaij, Rachel M., Klis, Frans M., Kools, Harrie J., Kubicek, Christian P., van Kuyk, Patricia A., Lauber, Juergen, Lu, Xin, van der Maarel, Marc J. E. C., Meulenberg, Rogier, Menke, Hildegard, Mortimer, Martin A., Nielsen, Jens, Oliver, Stephen G., Olsthoorn, Maurien, Pal, Karoly, van Peij, Noel N. M. E., Ram, Arthur F. J., Rinas, Ursula, Roubos, Johannes A., Sagt, Cees M. J., Schmoll, Monika, Sun, Jibin, Ussery, David, Varga, Janos, Vervecken, Wouter, de Vondervoort, Peter J. J. van, Wedler, Holger, Wosten, Han A. B., Zeng, An-Ping, van Ooyen, Albert J. J., Visser, Jaap, Stam, Hein, Sub Molecular Microbiology, Molecular Microbiology, Pel, Herman J., de Winde, Johannes H., Archer, David B., Dyer, Paul S., Hofmann, Gerald, Schaap, Peter J., Turner, Geoffrey, de Vries, Ronald P., Albang, Richard, Albermann, Kaj, Andersen, Mikael R., Bendtsen, Jannick D., Benen, Jacques A. E., van den Berg, Marco, Breestraat, Stefaan, Caddick, Mark X., Contreras, Roland, Cornell, Michael, Coutinho, Pedro M., Danchin, Etienne G. J., Debets, Alfons J. M., Dekker, Peter, van Dijck, Piet W. M., van Dijk, Alard, Dijkhuizen, Lubbert, Driessen, Arnold J. M., d'Enfert, Christophe, Geysens, Steven, Goosen, Coenie, Groot, Gert S. P., de Groot, Piet W. J., Guillemette, Thomas, Henrissat, Bernard, Herweijer, Marga, van den Hombergh, Johannes P. T. W., van den Hondel, Cees A. M. J. J., van der Heijden, Rene T. J. M., van der Kaaij, Rachel M., Klis, Frans M., Kools, Harrie J., Kubicek, Christian P., van Kuyk, Patricia A., Lauber, Juergen, Lu, Xin, van der Maarel, Marc J. E. C., Meulenberg, Rogier, Menke, Hildegard, Mortimer, Martin A., Nielsen, Jens, Oliver, Stephen G., Olsthoorn, Maurien, Pal, Karoly, van Peij, Noel N. M. E., Ram, Arthur F. J., Rinas, Ursula, Roubos, Johannes A., Sagt, Cees M. J., Schmoll, Monika, Sun, Jibin, Ussery, David, Varga, Janos, Vervecken, Wouter, de Vondervoort, Peter J. J. van, Wedler, Holger, Wosten, Han A. B., Zeng, An-Ping, van Ooyen, Albert J. J., Visser, Jaap, and Stam, Hein

Published
2007

10. A bacterial glycosidase enables mannose-6-phosphate modification and improved cellular uptake of yeast-produced recombinant human lysosomal enzymes

Author

Tiels, Petra, primary, Baranova, Ekaterina, additional, Piens, Kathleen, additional, De Visscher, Charlotte, additional, Pynaert, Gwenda, additional, Nerinckx, Wim, additional, Stout, Jan, additional, Fudalej, Franck, additional, Hulpiau, Paco, additional, Tännler, Simon, additional, Geysens, Steven, additional, Van Hecke, Annelies, additional, Valevska, Albena, additional, Vervecken, Wouter, additional, Remaut, Han, additional, and Callewaert, Nico, additional

Published
2012
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12. Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88

Author

Pel, Herman J, primary, de Winde, Johannes H, additional, Archer, David B, additional, Dyer, Paul S, additional, Hofmann, Gerald, additional, Schaap, Peter J, additional, Turner, Geoffrey, additional, de Vries, Ronald P, additional, Albang, Richard, additional, Albermann, Kaj, additional, Andersen, Mikael R, additional, Bendtsen, Jannick D, additional, Benen, Jacques A E, additional, van den Berg, Marco, additional, Breestraat, Stefaan, additional, Caddick, Mark X, additional, Contreras, Roland, additional, Cornell, Michael, additional, Coutinho, Pedro M, additional, Danchin, Etienne G J, additional, Debets, Alfons J M, additional, Dekker, Peter, additional, van Dijck, Piet W M, additional, van Dijk, Alard, additional, Dijkhuizen, Lubbert, additional, Driessen, Arnold J M, additional, d'Enfert, Christophe, additional, Geysens, Steven, additional, Goosen, Coenie, additional, Groot, Gert S P, additional, de Groot, Piet W J, additional, Guillemette, Thomas, additional, Henrissat, Bernard, additional, Herweijer, Marga, additional, van den Hombergh, Johannes P T W, additional, van den Hondel, Cees A M J J, additional, van der Heijden, Rene T J M, additional, van der Kaaij, Rachel M, additional, Klis, Frans M, additional, Kools, Harrie J, additional, Kubicek, Christian P, additional, van Kuyk, Patricia A, additional, Lauber, Jürgen, additional, Lu, Xin, additional, van der Maarel, Marc J E C, additional, Meulenberg, Rogier, additional, Menke, Hildegard, additional, Mortimer, Martin A, additional, Nielsen, Jens, additional, Oliver, Stephen G, additional, Olsthoorn, Maurien, additional, Pal, Karoly, additional, van Peij, Noël N M E, additional, Ram, Arthur F J, additional, Rinas, Ursula, additional, Roubos, Johannes A, additional, Sagt, Cees M J, additional, Schmoll, Monika, additional, Sun, Jibin, additional, Ussery, David, additional, Varga, Janos, additional, Vervecken, Wouter, additional, van de Vondervoort, Peter J J, additional, Wedler, Holger, additional, Wösten, Han A B, additional, Zeng, An-Ping, additional, van Ooyen, Albert J J, additional, Visser, Jaap, additional, and Stam, Hein, additional

Published
2007
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14. Engineering Yarrowia lipolytica to Produce Glycoproteins Homogeneously Modified with the Universal Man3GlcNAc2 N-Glycan Core.

Author

De Pourcq, Karen, Tiels, Petra, Van Hecke, Annelies, Geysens, Steven, Vervecken, Wouter, and Callewaert, Nico

Subjects
YEAST, GLYCOPROTEINS, MANNOSE, BIOSYNTHESIS, GENE expression, GLYCOSYLATION
Abstract

Yarrowia lipolytica is a dimorphic yeast that efficiently secretes various heterologous proteins and is classified as "generally recognized as safe." Therefore, it is an attractive protein production host. However, yeasts modify glycoproteins with nonhuman high mannose-type N-glycans. These structures reduce the protein half-life in vivo and can be immunogenic in man. Here, we describe how we genetically engineered N-glycan biosynthesis in Yarrowia lipolytica so that it produces Man3GlcNAc2 structures on its glycoproteins. We obtained unprecedented levels of homogeneity of this glycanstructure. This is the ideal starting point for building human-like sugars. Disruption of the ALG3 gene resulted in modification of proteins mainly with Man5GlcNAc2 and GlcMan5GlcNAc2 glycans, and to a lesser extent with Glc2Man5GlcNAc2 glycans. To avoid underoccupancy of glycosylation sites, we concomitantly overexpressed ALG6. We also explored several approaches to remove the terminal glucose residues, which hamper further humanization of N-glycosylation; overexpression of the heterodimeric Apergillus niger glucosidase II proved to be the most effective approach. Finally, we overexpressed an α-1,2- mannosidase to obtain Man3GlcNAc2 structures, which are substrates for the synthesis of complex-type glycans. The final Yarrowia lipolytica strain produces proteins glycosylated with the trimannosyl core N-glycan (Man3GlcNAc2), which is the common core of all complex-type N-glycans. All these glycans can be constructed on the obtained trimannosyl N-glycan using either in vivo or in vitro modification with the appropriate glycosyltransferases. The results demonstrate the high potential of Yarrowia lipolytica to be developed as an efficient expression system for the production of glycoproteins with humanized glycans. [ABSTRACT FROM AUTHOR]

Published
2012
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15. Ultrasensitive profiling andsequencing of N-linked oligosaccharides using standard DNA-sequencingequipment.

Author

Callewaert, Nico, Geysens, Steven, Molemans, Francis, and Contreras, Roland

Abstract

The analysis of protein-linked glycans is of increasing importance,both in basic glycobiological research and during the productionprocess of glycoprotein pharmaceuticals. In many cases, the amountof glycoprotein available for typing the glycans is very low. This,combined with the high branching complexity typical for this classof compounds, makes glycan typing a challenging task. We presenthere methodology allowing the medium-throughput analysis of N-glycansderived from low picomole amounts of glycoproteins using the standardDNA-sequencing equipment available in any life sciences laboratory.The high sensitivity of the overall analytical process (from glycoproteinto results) is obtained using state-of-the-art deglycosylation procedurescombined with a highly efficient and reproducible novel postderivatizationcleanup step involving Sephadex G10 packed 96-well filterplates. Allsample preparation steps (enzymatic deglycosylation with PNGaseF, desalting, derivatization with 8-amino-1,3,6-pyrenetrisulfonicacid, and postderivatization cleanup) are performed using 96-well-basedplates. This integrated sample preparation scheme is also compatible withcapillary electrophoresis and MALDI-TOF-MS platforms already inuse in some glycobiology labs and anticipates the higher throughputthat will be offered by the capillary-array-based DNA sequencerscurrently penetrating the market. The described technology should bringhigh-performance glycosylation analysis within reach of each lifesciences lab and thus help expedite the pace of discovery in thefield of glycobiology. [ABSTRACT FROM PUBLISHER]

Published
2001
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16. Use of HDEL‐tagged Trichoderma reeseimannosyl oligosaccharide 1,2‐α‐D‐mannosidase for N‐glycan engineering in Pichia pastoris

Author

Callewaert, Nico, Laroy, Wouter, Cadirgi, Hasan, Geysens, Steven, Saelens, Xavier, Min Jou, Willy, and Contreras, Roland

Abstract

Therapeutic glycoprotein production in the widely used expression host Pichia pastorisis hampered by the differences in the protein‐linked carbohydrate biosynthesis between this yeast and the target organisms such as man. A significant step towards the generation of human‐compatible N‐glycans in this organism is the conversion of the yeast‐type high‐mannose glycans to mammalian‐type high‐mannose and/or complex glycans. In this perspective, we have co‐expressed an endoplasmic reticulum‐targeted Trichoderma reesei1,2‐α‐D‐mannosidase with two glycoproteins: influenza virus haemagglutinin and Trypanosoma cruzi trans‐sialidase. Analysis of the N‐glycans of the two purified proteins showed a >85% decrease in the number of α‐1,2‐linked mannose residues. Moreover, the human‐type high‐mannose oligosaccharide Man5GlcNAc2was the major N‐glycan of the glyco‐engineered trans‐sialidase, indicating that N‐glycan engineering can be effectively accomplished in P. pastoris.

Published
2001
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