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Article: Reconstitution of recombinant viral envelope proteins.

Oker-Blom, Christian / Vuento, Matti

2003 Volume 372, Page(s) 418–428

MeSH term(s)	Animals ; Baculoviridae/genetics ; Baculoviridae/metabolism ; Cell Culture Techniques/methods ; Cell Line ; Escherichia coli/genetics ; Genetic Vectors ; Genome, Viral ; Lipid Bilayers ; Liposomes ; Protein Folding ; Recombinant Proteins/isolation & purification ; Recombinant Proteins/metabolism ; Spodoptera ; Transfection/methods ; Viral Envelope Proteins/genetics ; Viral Envelope Proteins/isolation & purification ; Viral Envelope Proteins/metabolism
Chemical Substances	Lipid Bilayers ; Liposomes ; Recombinant Proteins ; Viral Envelope Proteins
Language	English
Publishing date	2003
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	0076-6879
ISSN	0076-6879
DOI	10.1016/S0076-6879(03)72025-4
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Article: Peptide-mediated interference with baculovirus transduction.

Mäkelä, Anna R / Närvänen, Ale / Oker-Blom, Christian

Journal of biotechnology

2008 Volume 134, Issue 1-2, Page(s) 20–32

Abstract: Baculovirus represents a multifunctional platform with potential for biomedical applications including disease therapies. The importance of F3, a tumor-homing peptide, in baculovirus transduction was previously recognized by the ability of F3 to augment ... ...

Abstract	Baculovirus represents a multifunctional platform with potential for biomedical applications including disease therapies. The importance of F3, a tumor-homing peptide, in baculovirus transduction was previously recognized by the ability of F3 to augment viral binding and gene delivery to human cancer cells following display on the viral envelope. Here, F3 was utilized as a molecular tool to expand understanding of the poorly characterized baculovirus-mammalian cell interactions. Baculovirus-mediated transduction of HepG2 hepatocarcinoma cells was strongly inhibited by coincubating the virus with synthetic F3 or following incorporation of F3 into viral nucleocapsid by genetic engineering, the former suggesting direct interaction of the soluble peptide with the virus particles. Since internalization and nuclear accumulation of the virus were significantly inhibited or delayed, but the kinetics of viral binding, initial uptake, and endosomal release were unaffected, F3 likely interferes with cytoplasmic trafficking and subsequent nuclear transport of the virus. A polyclonal antibody raised against nucleolin, the internalizing receptor of F3, failed to inhibit cellular binding, but considerably reduced viral transduction efficiency, proposing the involvement of nucleolin in baculovirus entry. Together, these results render the F3 peptide a tool for elucidating the mechanism and molecular details conferring to baculovirus-mediated gene transduction in mammalian cells.
MeSH term(s)	Animals ; Baculoviridae/genetics ; Biological Transport/drug effects ; Blotting, Western ; Cell Line ; Cell Line, Tumor ; Genetic Vectors/genetics ; Genetic Vectors/pharmacokinetics ; Humans ; Kinetics ; Microscopy, Confocal ; Peptides/chemical synthesis ; Peptides/metabolism ; Peptides/pharmacology ; Phosphoproteins/genetics ; Phosphoproteins/metabolism ; RNA-Binding Proteins/genetics ; RNA-Binding Proteins/metabolism ; Spodoptera ; Transduction, Genetic ; Nucleolin
Chemical Substances	Peptides ; Phosphoproteins ; RNA-Binding Proteins
Language	English
Publishing date	2008-01-18
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	843647-2
ISSN	1873-4863 ; 0168-1656 ; 1389-0352
ISSN (online)	1873-4863
ISSN	0168-1656 ; 1389-0352
DOI	10.1016/j.jbiotec.2007.12.010
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Article: The baculovirus display technology--an evolving instrument for molecular screening and drug delivery.

Mäkelä, Anna R / Oker-Blom, Christian

Combinatorial chemistry & high throughput screening

2008 Volume 11, Issue 2, Page(s) 86–98

Abstract: High throughput screening is a core technology in drug discovery. During the past decade, several strategies have been developed to screen (poly)peptide libraries for diverse applications including disease diagnosis and profiling, imaging, as well as ... ...

Abstract	High throughput screening is a core technology in drug discovery. During the past decade, several strategies have been developed to screen (poly)peptide libraries for diverse applications including disease diagnosis and profiling, imaging, as well as therapy. The recently established baculovirus display vector system (BDVS) represents a eukaryotic screening platform that combines the positive attributes of both cell and virus-based display approaches, allowing presentation of complex polypeptides on cellular and viral surfaces. Compared to microbial display systems, the BDVS has the advantage of correct protein folding and post-translational modifications similar to those in mammals, facilitating expression and analysis of proteins with therapeutic interest. The applicability of the system is further expanded by the availability of genetically engineered insect cell lines capable of performing e.g. mammalianized glycosylation in combination with high level of expression. In addition to insect cells, baculovirus can mediate delivery and expression of heterologous genes in a broad spectrum of primary and established mammalian cells. Currently, a variety of baculovirus-based assays aiming at routine high throughput identification of agents targeting cell surface receptors or studies on ligand-receptor interactions are under construction. Here, the advancements and future prospects of the baculovirus display technologies with emphasis on molecular screening and drug delivery applications using insect cell display, mammalian cell display, and virion display are described.
MeSH term(s)	Adjuvants, Immunologic/pharmacology ; Animals ; Baculoviridae/genetics ; Drug Evaluation, Preclinical/methods ; Gene Library ; Gene Transfer Techniques ; Genetic Vectors/genetics ; Humans ; Insecta/virology
Chemical Substances	Adjuvants, Immunologic
Language	English
Publishing date	2008-02-22
Publishing country	United Arab Emirates
Document type	Journal Article ; Review
ZDB-ID	2064785-2
ISSN	1875-5402 ; 1386-2073
ISSN (online)	1875-5402
ISSN	1386-2073
DOI	10.2174/138620708783744525
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Article ; Online: Baculovirus-based display and gene delivery systems.

Mäkelä, Anna R / Ernst, Wolfgang / Grabherr, Reingard / Oker-Blom, Christian

Cold Spring Harbor protocols

2010 Volume 2010, Issue 3, Page(s) pdb.top72

Abstract: The baculovirus expression vector system has been used extensively to produce numerous proteins originating from both prokaryotic and eukaryotic sources. In addition to easy cloning techniques and abundant viral propagation, the system's insect cell ... ...

Abstract	The baculovirus expression vector system has been used extensively to produce numerous proteins originating from both prokaryotic and eukaryotic sources. In addition to easy cloning techniques and abundant viral propagation, the system's insect cell environment provides eukaryotic post-translational modification machinery. The recently established eukaryotic molecular biology tool, the baculovirus display vector system (BDVS), allows the combination of genotype with phenotype, enabling presentation of foreign peptides or even complex proteins on the baculoviral envelope or capsid. This strategy is important because it can be used to enhance viral binding and entry to mammalian cells as well as to produce antibodies against the displayed antigen. In addition, the technology should enable modifications of intracellular behavior, that is, trafficking of recombinant "nanoparticles," a highly relevant feature for studies of targeted gene or protein delivery. This article discusses the design and potential uses of insect-derived baculoviral display vectors.
MeSH term(s)	Animals ; Baculoviridae/genetics ; Cell Line ; Gene Expression ; Gene Transfer Techniques ; Genetic Vectors ; Insecta ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Viral Proteins/genetics ; Viral Proteins/metabolism
Chemical Substances	Recombinant Proteins ; Viral Proteins
Language	English
Publishing date	2010-03
Publishing country	United States
Document type	Journal Article ; Review
ISSN	1559-6095
ISSN (online)	1559-6095
DOI	10.1101/pdb.top72
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Article ; Online: Immunofluorescence analysis of baculovirus-displayed viral proteins on infected insect cells.

Mäkelä, Anna R / Ernst, Wolfgang / Grabherr, Reingard / Oker-Blom, Christian

Cold Spring Harbor protocols

2010 Volume 2010, Issue 3, Page(s) pdb.prot5395

Abstract	The baculovirus expression vector system has been used extensively to produce numerous proteins originating from both prokaryotic and eukaryotic sources. In addition to easy cloning techniques and abundant viral propagation, the system's insect cell environment provides eukaryotic post-translational modification machinery. The baculovirus display vector system provides a number of advantages over prokaryotic systems, allowing the combination of genotype with phenotype, enabling presentation of foreign peptides or even complex proteins on the baculoviral envelope or capsid. Baculoviruses permit larger gene insertions, are easily propagated, and can be grown to high titers. Furthermore, the eukaryotic system allows for post-translational modifications, and surface modifications of the viral capsid enable specific targeting. This strategy can be used to enhance viral binding and entry to a wide variety of both dividing and nondividing mammalian cells, as well as to produce antibodies against the displayed antigen. In addition, the technology should enable modifications of intracellular behavior, i.e., trafficking of recombinant "nanoparticles," a highly relevant feature for studies of targeted gene or protein delivery. After generating the display viral stock, it is important to confirm the presence and functionality of the displayed peptides or proteins on the viral particles before proceeding to further experiments. Accordingly, infected insect cells and budded virions can be analyzed by a variety of methods using appropriate antibodies. This protocol describes a standard immunofluorescence technique in detail.
MeSH term(s)	Animals ; Baculoviridae/genetics ; Cell Line ; Fluorescent Antibody Technique/methods ; Gene Expression ; Genetic Vectors ; Insecta ; Recombinant Proteins/analysis ; Viral Proteins/analysis ; Virion/chemistry
Chemical Substances	Recombinant Proteins ; Viral Proteins
Language	English
Publishing date	2010-03
Publishing country	United States
Document type	Journal Article
ISSN	1559-6095
ISSN (online)	1559-6095
DOI	10.1101/pdb.prot5395
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Article ; Online: Determination of recombinant baculovirus display viral titer.

Mäkelä, Anna R / Ernst, Wolfgang / Grabherr, Reingard / Oker-Blom, Christian

Cold Spring Harbor protocols

2010 Volume 2010, Issue 3, Page(s) pdb.prot5394

Abstract	The baculovirus expression vector system has been used extensively to produce numerous proteins originating from both prokaryotic and eukaryotic sources. In addition to easy cloning techniques and abundant viral propagation, the system's insect cell environment provides eukaryotic post-translational modification machinery. The baculovirus display vector system provides a number of advantages over prokaryotic systems, allowing the combination of genotype with phenotype, enabling presentation of foreign peptides or even complex proteins on the baculoviral envelope or capsid. Baculoviruses permit larger gene insertions, are easily propagated, and can be grown to high titers. Furthermore, surface modifications of the viral capsid enable specific targeting. This strategy can be used to enhance viral binding and entry to a wide variety of both dividing and nondividing mammalian cells, as well as to produce antibodies against the displayed antigen. In addition, the technology should enable modifications of intracellular behavior, i.e., trafficking of recombinant "nanoparticles," a highly relevant feature for studies of targeted gene or protein delivery. Although baculovirus titer can be determined by standard methods such as classical plaque assays or end-point dilution assays, such methods often are tedious and time-consuming. The protocol described here is rapid and can be performed directly using marker genes such as green fluorescent protein or beta-galactosidase regulated by baculovirus-specific promoters, or indirectly as an immunoassay with baculovirus-specific antibodies (e.g., anti-gp64).
MeSH term(s)	Animals ; Antibodies, Viral ; Antigens, Viral/analysis ; Baculoviridae/isolation & purification ; Genes, Reporter ; Genetic Vectors ; Green Fluorescent Proteins/genetics ; Green Fluorescent Proteins/metabolism ; Immunoassay/methods ; Staining and Labeling/methods ; Viral Load ; beta-Galactosidase/genetics ; beta-Galactosidase/metabolism
Chemical Substances	Antibodies, Viral ; Antigens, Viral ; enhanced green fluorescent protein ; Green Fluorescent Proteins (147336-22-9) ; beta-Galactosidase (EC 3.2.1.23)
Language	English
Publishing date	2010-03
Publishing country	United States
Document type	Journal Article
ISSN	1559-6095
ISSN (online)	1559-6095
DOI	10.1101/pdb.prot5394
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Article ; Online: Monitoring baculovirus-mediated efficiency of gene delivery.

Mäkelä, Anna R / Ernst, Wolfgang / Grabherr, Reingard / Oker-Blom, Christian

Cold Spring Harbor protocols

2010 Volume 2010, Issue 3, Page(s) pdb.prot5397

Abstract	The baculovirus expression vector system has been used extensively to produce numerous proteins originating from both prokaryotic and eukaryotic sources. In addition to easy cloning techniques and abundant viral propagation, the system's insect cell environment provides eukaryotic post-translational modification machinery. The baculovirus display vector system provides a number of advantages over prokaryotic systems, allowing the combination of genotype with phenotype, enabling presentation of foreign peptides or even complex proteins on the baculoviral envelope or capsid. Baculoviruses permit larger gene insertions, are easily propagated, and can be grown to high titers. Furthermore, surface modifications of the viral capsid enable specific targeting. This strategy can be used to enhance viral binding and entry to a wide variety of both dividing and nondividing mammalian cells, as well as to produce antibodies against the displayed antigen. In addition, the technology should enable modifications of intracellular behavior, that is, trafficking of recombinant "nanoparticles," a highly relevant feature for studies of targeted gene or protein delivery. Also, the ability to incorporate reporter genes under transcriptional regulation of mammalian promoters enables transduction efficiency to be monitored in mammalian cells in vitro and in tissues in vivo. Luciferase molecules in particular are nontoxic and emit light in direct proportion to their number in mammalian cells. This provides a sensitive and rapid assay for quantification of transgene expression without the need for illumination with an external excitation source.
MeSH term(s)	Animals ; Baculoviridae/genetics ; Cell Line ; Genes, Reporter ; Genetic Vectors ; Insecta ; Luciferases/genetics ; Luciferases/metabolism ; Mammals ; Recombinant Proteins/biosynthesis ; Staining and Labeling/methods ; Transduction, Genetic ; Transgenes
Chemical Substances	Recombinant Proteins ; Luciferases (EC 1.13.12.-)
Language	English
Publishing date	2010-03
Publishing country	United States
Document type	Journal Article
ISSN	1559-6095
ISSN (online)	1559-6095
DOI	10.1101/pdb.prot5397
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Article ; Online: Immunoelectron microscopy analysis of recombinant baculovirus display viruses.

Mäkelä, Anna R / Ernst, Wolfgang / Grabherr, Reingard / Oker-Blom, Christian

Cold Spring Harbor protocols

2010 Volume 2010, Issue 3, Page(s) pdb.prot5396

Abstract	The baculovirus expression vector system has been used extensively to produce numerous proteins originating from both prokaryotic and eukaryotic sources. In addition to easy cloning techniques and abundant viral propagation, the system's insect cell environment provides eukaryotic post-translational modification machinery. The baculovirus display vector system provides a number of advantages over prokaryotic systems, allowing the combination of genotype with phenotype, enabling presentation of foreign peptides or even complex proteins on the baculoviral envelope or capsid. Baculoviruses permit larger gene insertions, are easily propagated, and can be grown to high titers. Furthermore, surface modifications of the viral capsid enable specific targeting. This strategy can be used to enhance viral binding and entry to a wide variety of both dividing and nondividing mammalian cells, as well as to produce antibodies against the displayed antigen. In addition, the technology should enable modifications of intracellular behavior, i.e., trafficking of recombinant "nanoparticles," a highly relevant feature for studies of targeted gene or protein delivery. After generating the display viral stock, it is important to confirm the presence and functionality of the displayed peptides or proteins on the viral particles before proceeding to further experiments. Accordingly, infected insect cells and budded virions can be analyzed by a variety of methods using appropriate antibodies. This protocol describes a standard immunoelectron microscopy technique in detail.
MeSH term(s)	Animals ; Baculoviridae/genetics ; Cell Line ; Gene Expression ; Genetic Vectors ; Insecta ; Microscopy, Immunoelectron/methods ; Recombinant Proteins/analysis ; Viral Proteins/analysis ; Virion/chemistry
Chemical Substances	Recombinant Proteins ; Viral Proteins
Language	English
Publishing date	2010-03
Publishing country	United States
Document type	Journal Article
ISSN	1559-6095
ISSN (online)	1559-6095
DOI	10.1101/pdb.prot5396
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Article ; Online: Creation of baculovirus display libraries.

Mäkelä, Anna R / Ernst, Wolfgang / Grabherr, Reingard / Oker-Blom, Christian

Cold Spring Harbor protocols

2010 Volume 2010, Issue 3, Page(s) pdb.prot5393

Abstract	The baculovirus expression vector system has been used extensively to produce numerous proteins originating from both prokaryotic and eukaryotic sources. In addition to easy cloning techniques and abundant viral propagation, the system's insect cell environment provides eukaryotic post-translational modification machinery. The baculovirus display vector system provides a number of advantages over prokaryotic systems, allowing the combination of genotype with phenotype, enabling presentation of foreign peptides or even complex proteins on the baculoviral envelope or capsid. Baculoviruses permit larger gene insertions, are easily propagated, and can be grown to high titers. Furthermore, surface modifications of the viral capsid enable specific targeting. This strategy can be used to enhance viral binding and entry to a wide variety of both dividing and nondividing mammalian cells as well as to produce antibodies against the displayed antigen. In addition, the technology should enable modifications of intracellular behavior, i.e., trafficking of recombinant "nanoparticles," a highly relevant feature for studies of targeted gene or protein delivery. It is important to note that, although the viruses do not replicate in mammalian cells, they are not entirely transcriptionally silent. They can also be highly antigenic when used in vivo, limiting their therapeutic use. This protocol describes methods for generating display libraries.
MeSH term(s)	Animals ; Baculoviridae/genetics ; Cell Line ; Cloning, Molecular/methods ; Gene Expression ; Genetic Vectors ; Insecta ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Viral Proteins/genetics ; Viral Proteins/metabolism
Chemical Substances	Recombinant Proteins ; Viral Proteins
Language	English
Publishing date	2010-03
Publishing country	United States
Document type	Journal Article
ISSN	1559-6095
ISSN (online)	1559-6095
DOI	10.1101/pdb.prot5393
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Article ; Online: Early succession of bacterial biofilms in paper machines.

Tiirola, Marja / Lahtinen, Tomi / Vuento, Matti / Oker-Blom, Christian

Journal of industrial microbiology & biotechnology

2009 Volume 36, Issue 7, Page(s) 929–937

Abstract: Formation of biofilms causes severe problems in paper machines, and hence financial costs. It would be preferable to prevent attachment of the primary-colonizing bacteria than to control the growth of secondary communities, which are sheltered by ... ...

Abstract	Formation of biofilms causes severe problems in paper machines, and hence financial costs. It would be preferable to prevent attachment of the primary-colonizing bacteria than to control the growth of secondary communities, which are sheltered by exopolysaccharide slime layers. We have therefore investigated the early succession of paper-machine biofilms by incubating stainless-steel test coupons in the process water-flow lines in two paper machines operating in slightly alkaline conditions in temperatures (45 and 49 degrees C) supporting thermophilic microbes. Microbial succession was profiled using length heterogeneity analysis of PCR-amplified 16S rRNA genes (LH-PCR) and linking the sequence data of the created 16S rRNA gene libraries to the dominant LH-PCR peaks. Although the bacterial fingerprints obtained from the attached surface communities varied slightly in different samples, the biomarker signals of the dominating primary-colonizing bacterial groups remained high over time in each paper machine. Most of the 16S rRNA gene copies in the early biofilms were assigned to the genera Rhodobacter, Tepidimonas, and Cloacibacterium. The dominance of these sequence types decreased in the developing biofilms. Finally, as phylogenetically identical primary-colonizers were detected in the two different paper mills, the machines evidently had similar environmental conditions for bacterial growth and potentially a common source of contamination.
MeSH term(s)	Bacteria/classification ; Bacteria/genetics ; Bacteria/growth & development ; Biodiversity ; Biofilms/growth & development ; Environmental Microbiology ; Genes, rRNA ; Industrial Microbiology ; Molecular Sequence Data ; Paper ; Phylogeny ; RNA, Bacterial/genetics ; RNA, Ribosomal, 16S/genetics ; Sequence Analysis, DNA
Chemical Substances	RNA, Bacterial ; RNA, Ribosomal, 16S
Language	English
Publishing date	2009-04-24
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1482484-X
ISSN	1476-5535 ; 1367-5435
ISSN (online)	1476-5535
ISSN	1367-5435
DOI	10.1007/s10295-009-0571-6
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