http://publicationslist.org/data/henrik.wernerus/atom.xml Henrik Wernérushttp://publicationslist.org/henrik.wernerus$basepathfavicon.icoRecent additions to Henrik Wernérus's PublicationsList.org pagehttp://publicationslist.org/publications.png2007-11-03T16:01:17Z http://publicationslist.org/henrik.wernerus/refid2 2007-11-03T15:58:48Z

Completion of the Human Genome Project and recent developments in proteomics make it possible to systematically generate affinity reagents to a large portion of the proteome. Recently an antibody-based human protein atlas covering many organs including four areas of the brain has been released (www.proteinatlas.org). Due to the heterogeneity, size, and availability of tissue a more thorough analys...<br/><br/>J Mulder, H Wernérus, T-J Shi, F Pontén, S Hober, M Uhlén, T Hökfelt (2007) <i>Neuroscience</i> <i></i> <i></i> 146: 4 1689-1703<br/>

http://publicationslist.org/henrik.wernerus/refid3 2007-11-03T15:58:48Z

AIMS: The study was conducted with an aim to optimize the transformation efficiency of the Gram-positive bacterium Staphylococcus carnosus to a level that would enable the creation of cell surface displayed combinatorial protein libraries. METHODS AND RESULTS: We have thoroughly investigated a number of different parameters for: (i) the preparation of electrocompetent cells; (ii) the treatment of ...<br/><br/>J Löfblom, N Kronqvist, M Uhlén, S Ståhl, H Wernérus (2007) <i>J Appl Microbiol</i> <i></i> <i></i> 102: 3 736-747<br/>

http://publicationslist.org/henrik.wernerus/refid1 2007-11-03T15:58:48Z

For efficient generation of high-affinity protein-based binding molecules, fast and reliable downstream characterization platforms are needed. In this work, we have explored the use of staphylococcal cell surface display together with flow cytometry for affinity characterization of candidate affibody molecules directly on the cell surface. A model system comprising three closely related affibody m...<br/><br/>John Löfblom, Julia Sandberg, Henrik Wernérus, Stefan Ståhl (2007) <i>Appl Environ Microbiol</i> <i></i> <i></i> 73: 21 6714-6721<br/>

http://publicationslist.org/henrik.wernerus/refid4 2007-11-03T15:58:48Z

Monospecific antibodies dfdfdfdf (msAbs) generated through antigen specific purification of polyclonal antisera are valuable tools in proteome analyses. However, proteome wide generation of msAbs would require extensive immunization programs. Therefore, it would be desirable to develop efficient immunization and purification methods to reduce the number of animals needed for such antibody-based re...<br/><br/>Karin Larsson, Kenneth Wester, Peter Nilsson, Mathias Uhlén, Sophia Hober, Henrik Wernérus (2006) <i>J Immunol Methods</i> <i></i> <i></i> 315: 1-2 110-120<br/>

http://publicationslist.org/henrik.wernerus/refid7 2007-11-03T15:58:48Z

We have investigated a staphylococcal surface display system for its potential future use as a protein library display system in combinatorial biochemistry. Efficient affinity-based selections require a system capable of fine affinity discrimination of closely related binders to minimize the loss of potentially improved variants. In this study, a significant breakthrough was achieved to avoid bias...<br/><br/>John Löfblom, Henrik Wernérus, Stefan Ståhl (2005) <i>FEMS Microbiol Lett</i> <i></i> <i></i> 248: 2 189-198<br/>

http://publicationslist.org/henrik.wernerus/refid6 2007-11-03T15:58:48Z

Antibody-based proteomics provides a powerful approach for the functional study of the human proteome involving the systematic generation of protein-specific affinity reagents. We used this strategy to construct a comprehensive, antibody-based protein atlas for expression and localization profiles in 48 normal human tissues and 20 different cancers. Here we report a new publicly available database...<br/><br/>Mathias Uhlén, Erik Björling, Charlotta Agaton, Cristina Al-Khalili Szigyarto, Bahram Amini, Elisabet Andersen, Ann-Catrin Andersson, Pia Angelidou, Anna Asplund, Caroline Asplund, Lisa Berglund, Kristina Bergström, Harry Brumer, Dijana Cerjan, Marica Ekström, Adila Elobeid, Cecilia Eriksson, Linn Fagerberg, Ronny Falk, Jenny Fall, Mattias Forsberg, Marcus Gry Björklund, Kristoffer Gumbel, Asif Halimi, Inga Hallin, Carl Hamsten, Marianne Hansson, My Hedhammar, Görel Hercules, Caroline Kampf, Karin Larsson, Mats Lindskog, Wald Lodewyckx, Jan Lund, Joakim Lundeberg, Kristina Magnusson, Erik Malm, Peter Nilsson, Jenny Odling, Per Oksvold, Ingmarie Olsson, Emma Oster, Jenny Ottosson, Linda Paavilainen, Anja Persson, Rebecca Rimini, Johan Rockberg, Marcus Runeson, Asa Sivertsson, Anna Sköllermo, Johanna Steen, Maria Stenvall, Fredrik Sterky, Sara Strömberg, Mårten Sundberg, Hanna Tegel, Samuel Tourle, Eva Wahlund, Annelie Waldén, Jinghong Wan, Henrik Wernérus, Joakim Westberg, Kenneth Wester, Ulla Wrethagen, Lan Lan Xu, Sophia Hober, Fredrik Pontén (2005) <i>Mol Cell Proteomics</i> <i></i> <i></i> 4: 12 1920-1932<br/>

http://publicationslist.org/henrik.wernerus/refid5 2007-11-03T15:58:48Z

A great need exists for the systematic generation of specific antibodies to explore the human proteome. Here, we show that antibodies specific to human proteins can be generated in a high-throughput manner involving stringent affinity purification using recombinant protein epitope signature tags (PrESTs) as immunogens and affinity-ligands. The specificity of the generated affinity reagents, here c...<br/><br/>Peter Nilsson, Linda Paavilainen, Karin Larsson, Jenny Odling, Mårten Sundberg, Ann-Catrin Andersson, Caroline Kampf, Anja Persson, Cristina Al-Khalili Szigyarto, Jenny Ottosson, Erik Björling, Sophia Hober, Henrik Wernérus, Kenneth Wester, Fredrik Pontén, Mathias Uhlen (2005) <i>Proteomics</i> <i></i> <i></i> 5: 17 4327-4337<br/>

http://publicationslist.org/henrik.wernerus/refid8 2007-11-03T15:58:48Z

Display of heterologous proteins on the surface of micro-organisms, enabled by means of recombinant DNA technology, has become an increasingly popular strategy in microbiology, biotechnology and vaccinology. Both Gram-negative and Gram-positive bacteria have been investigated for potential applications. The present review will describe the most commonly used systems for bacterial display, with a f...<br/><br/>Henrik Wernérus, Stefan Ståhl (2004) <i>Biotechnol Appl Biochem</i> <i></i> <i></i> 40: Pt 3 209-228<br/>

http://publicationslist.org/henrik.wernerus/refid9 2007-11-03T15:58:48Z

Efficient enrichment of staphylococcal cells displaying specific heterologous affinity ligands on their cell surfaces was demonstrated by using fluorescence-activated cell sorting. Using bacterial surface display of peptide or protein libraries for the purpose of combinatorial protein engineering has previously been investigated by using gram-negative bacteria. Here, the potential for using a gram...<br/><br/>Henrik Wernérus, Patrik Samuelson, Stefan Ståhl (2003) <i>Appl Environ Microbiol</i> <i></i> <i></i> 69: 9 5328-5335<br/>

http://publicationslist.org/henrik.wernerus/refid11 2007-11-03T15:59:31Z

A previously developed expression system for surface display of heterologous proteins on the surface of Staphylococcus carnosus employs the secretion signals from a Staphylococcus hyicus lipase and the cell wall anchoring part of Staphylococcus aureus protein A (SpA) to achieve surface display of expressed recombinant proteins. The system has been successfully used in various applications but the ...<br/><br/>Henrik Wernérus, Stefan Ståhl (2002) <i>FEMS Microbiol Lett</i> <i></i> <i></i> 212: 1 47-54<br/>

http://publicationslist.org/henrik.wernerus/refid10 2007-11-03T15:58:48Z

Novel surface proteins can be introduced onto bacterial cell surfaces by recombinant means. Here, we describe various applications of two such display systems for the food-grade bacteria Staphylococcus carnosus and Staphylococcus xylosus, respectively. The achievements in the use of such staphylococci as live bacterial vaccine delivery vehicles will be described. Co-display of proteins and peptide...<br/><br/>Henrik Wernérus, Janne Lehtiö, Patrik Samuelson, Stefan Ståhl (2002) <i>J Biotechnol</i> <i></i> <i></i> 96: 1 67-78<br/>

http://publicationslist.org/henrik.wernerus/refid14 2007-11-03T15:59:31Z

The immobilization of recombinant staphylococci onto cellulose fibers through surface display of a fungal cellulose-binding domain (CBD) was investigated. Chimeric proteins containing the CBD from Trichoderma reesei cellulase Cel6A were found to be correctly targeted to the cell wall of Staphylococcus carnosus cells, since full-length proteins could be extracted and affinity-purified. Furthermore,...<br/><br/>J Lehtiö, H Wernérus, P Samuelson, T T Teeri, S Ståhl (2001) <i>FEMS Microbiol Lett</i> <i></i> <i></i> 195: 2 197-204<br/>

http://publicationslist.org/henrik.wernerus/refid12 2007-11-03T15:59:31Z

Ni(2+)-binding staphylococci were generated through surface display of combinatorially engineered variants of a fungal cellulose-binding domain (CBD) from Trichoderma reesei cellulase Cel7A. Novel CBD variants were generated by combinatorial protein engineering through the randomization of 11 amino acid positions, and eight potentially Ni(2+)-binding CBDs were selected by phage display technology....<br/><br/>H Wernérus, J Lehtiö, T Teeri, P A Nygren, S Ståhl (2001) <i>Appl Environ Microbiol</i> <i></i> <i></i> 67: 10 4678-4684<br/>

http://publicationslist.org/henrik.wernerus/refid15 2007-11-03T15:59:31Z

We have previously reported a strategy for production in Escherichia coli of recombinant immunogens fused to a hydrophobic tag to improve their capacity to associate with an adjuvant formulation [Andersson et al., J. Immunol. Methods 222 (1999) 171]. Here, we describe a further development of the previous strategy and present significant improvements. In the novel system, the target immunogen is p...<br/><br/>C Andersson, L Sandberg, H Wernérus, M Johansson, K Lövgren-Bengtsson, S Ståhl (2000) <i>J Immunol Methods</i> <i></i> <i></i> 238: 1-2 181-193<br/>

http://publicationslist.org/henrik.wernerus/refid16 2007-11-03T15:59:31Z

Recombinant Staphylococcus xylosus and Staphylococcus carnosus strains were generated with surface-exposed chimeric proteins containing polyhistidyl peptides designed for binding to divalent metal ions. Surface accessibility of the chimeric surface proteins was demonstrated and the chimeric surface proteins were found to be functional in terms of metal binding, since the recombinant staphylococcal...<br/><br/>P Samuelson, H Wernérus, M Svedberg, S Ståhl (2000) <i>Appl Environ Microbiol</i> <i></i> <i></i> 66: 3 1243-1248<br/>

http://publicationslist.org/henrik.wernerus/refid13 2007-11-03T15:59:31Z

Novel surface proteins can be introduced onto the bacterial cell surface by recombinant means. Here, we describe the development of such display systems for two food-grade bacteria, Staphylococcus carnosus and Staphylococcus xylosus, and present how such engineered bacteria can be used in different applications. A study will be described in which such staphylococci were employed as vaccine deliver...<br/><br/>S Ståhl, A Robert, E Gunneriusson, H Wernérus, F Cano, S Liljeqvist, M Hansson, T N Nguyen, P Samuelson (2000) <i>Int J Med Microbiol</i> <i></i> <i></i> 290: 7 571-577<br/>