scholarly journals Recombinant human BMP-2/-7 heterodimer protein expression for bone tissue engineering using recombinant baculovirus expression system

2016 ◽  
Vol 32 (2) ◽  
pp. 49-53
Author(s):  
Seung-Won Park ◽  
Tae-Won Goo ◽  
Seong Ryul Kim ◽  
Kwang-Ho Choi
Keyword(s):  
Tissue Engineering ◽  
Protein Expression ◽  
Bone Tissue Engineering ◽  
Bone Tissue ◽  
Expression System ◽  
Recombinant Baculovirus ◽  
Baculovirus Expression System ◽  
Baculovirus Expression

Interaction of hepatic microsomal epoxide hydrolase derived from a recombinant baculovirus expression system with an azarene oxide and an aziridine substrate analog

Biochemistry ◽  
1993 ◽  
Vol 32 (10) ◽  
pp. 2610-2616 ◽  
Author(s):  
Gerard M. Lacourciere ◽  
Vikram N. Vakharia ◽  
Carina P. Tan ◽  
Diane I. Morris ◽  
Gerard H. Edwards ◽  
...  
Keyword(s):  
Epoxide Hydrolase ◽  
Expression System ◽  
Recombinant Baculovirus ◽  
Baculovirus Expression System ◽  
Microsomal Epoxide Hydrolase ◽  
Substrate Analog ◽  
Baculovirus Expression

Protein Expression of the Human Norovirus Capsid Gene using the Baculovirus Expression System

2011 ◽  
Vol 41 (3) ◽  
pp. 183 ◽  
Author(s):  
Ji-Young Jin ◽  
Chul Jong Park ◽  
Seung-Won Park ◽  
Soon-Young Paik
Keyword(s):  
Protein Expression ◽  
Expression System ◽  
Baculovirus Expression System ◽  
Capsid Gene ◽  
Human Norovirus ◽  
Baculovirus Expression

scholarly journals Expression, Purification and Sublocalization of SARS-CoV Nucleocapsid Protein in Insect Cells

2004 ◽  
Vol 36 (11) ◽  
pp. 754-758 ◽  
Author(s):  
Ai-Xia Ren ◽  
You-Hua Xie ◽  
Yu-Ying Kong ◽  
Guan-Zhen Yang ◽  
Yao-Zhou Zhang ◽  
...  
Keyword(s):  
Nucleocapsid Protein ◽  
Trichoplusia Ni ◽  
Insect Cells ◽  
Expression System ◽  
Recombinant Baculovirus ◽  
Baculovirus Expression System ◽  
Functional Study ◽  
Expression And Purification ◽  
N Protein ◽  
Baculovirus Expression

Abstract The causative agent of severe acute respiratory syndrome (SARS) is a previously unidentified coronavirus, SARS-CoV. The nucleocapsid (N) protein of SARS-CoV is a major viral protein recognized by acute and early convalescent sera from SARS patients. To facilitate the studies on the function and structure of the N protein, this report describe the expression and purification of recombinant SARS-CoV N protein using the baculovirus expression system. Recombinant hexa-histidine-tagged N protein with a molecular mass of 47 kD was produced in insect cells. Recombinant N protein was purified to near homogeneity by Ni2+-NTA affinity chromatography. In addition, we examined the subcellular localization of the N protein by confocal microscopy in Trichoplusia ni BT1 Tn 5B1–4 cells infected with recombinant baculovirus. The N protein was found localized in the cytoplasm as well as in the nucleolus. The purified recombinant N protein can be used in further functional study of SARS-CoV.

scholarly journals Lead Discovery for Human Kynurenine 3-Monooxygenase by High-Throughput RapidFire Mass Spectrometry

2013 ◽  
Vol 19 (4) ◽  
pp. 508-515 ◽  
Author(s):  
Denise M. Lowe ◽  
Michelle Gee ◽  
Carl Haslam ◽  
Bill Leavens ◽  
Erica Christodoulou ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Solid Phase ◽  
Expression System ◽  
Recombinant Baculovirus ◽  
Baculovirus Expression System ◽  
Lead Discovery ◽  
Human Form ◽  
Baculovirus Expression ◽  
Substrate Conversion ◽  
Assay Interference

Kynurenine 3-monooxygenase (KMO) is a therapeutically important target on the eukaryotic tryptophan catabolic pathway, where it converts L-kynurenine (Kyn) to 3-hydroxykynurenine (3-HK). We have cloned and expressed the human form of this membrane protein as a full-length GST-fusion in a recombinant baculovirus expression system. An enriched membrane preparation was used for a directed screen of approximately 78,000 compounds using a RapidFire mass spectrometry (RF-MS) assay. The RapidFire platform provides an automated solid-phase extraction system that gives a throughput of approximately 7 s per well to the mass spectrometer, where direct measurement of both the substrate and product allowed substrate conversion to be determined. The RF-MS methodology is insensitive to assay interference, other than where compounds have the same nominal mass as Kyn or 3-HK and produce the same mass transition on fragmentation. These instances could be identified by comparison with the product-only data. The screen ran with excellent performance (average Z′ value 0.8) and provided several tractable hit series for further investigation.

Characterization of hepatitis C virus structural proteins with a recombinant baculovirus expression system

Hepatology ◽  
1993 ◽  
Vol 17 (5) ◽  
pp. 763-771
Author(s):  
Henry H. Hsu ◽  
Mikhail Donets ◽  
Harry B. Greenberg ◽  
Stephen M. Feinstone
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Expression System ◽  
Recombinant Baculovirus ◽  
Baculovirus Expression System ◽  
Structural Proteins ◽  
Baculovirus Expression

scholarly journals Development of a Combined Genetic Engineering Vaccine for Porcine Circovirus Type 2 and Mycoplasma Hyopneumoniae by a Baculovirus Expression System

2019 ◽  
Vol 20 (18) ◽  
pp. 4425 ◽  
Author(s):  
Yu Tao ◽  
Gaojian Li ◽  
Wenqian Zheng ◽  
Jianhong Shu ◽  
Jian Chen ◽  
...  
Keyword(s):  
Genetic Engineering ◽  
Expression System ◽  
Recombinant Baculovirus ◽  
Baculovirus Expression System ◽  
Mycoplasma Hyopneumoniae ◽  
Porcine Circovirus Type ◽  
Porcine Circovirus Type 2 ◽  
Porcine Circovirus ◽  
Baculovirus Expression

Mycoplasma hyopneumoniae (Mhp) and porcine circovirus type 2 (PCV2) are the main pathogens for mycoplasmal pneumonia of swine (MPS) and post-weaning multisystemic wasting syndrome (PMWS), respectively. Infection by these pathogens often happens together and causes great economic losses. In this study, a kind of recombinant baculovirus that can display P97R1P46P42 chimeric protein of Mhp and the capsid (Cap) protein of PCV2 was developed, and the protein location was identified. Another recombinant baculovirus was constructed without tag proteins (EGFP, mCherry) and was used to evaluate the immune effect in experiments with BALB/c mice and domestic piglets. Antigen proteins P97R1P46P42 and Cap were expressed successfully; both were anchored on the plasma membrane of cells and the viral envelope. It should be emphasized that in piglet immunization, the recombinant baculovirus vaccine achieved similar immunological effects as the mixed commercial vaccine. Both the piglet and mouse experiments showed that the recombinant baculovirus was able to induce humoral and cellular responses effectively. The results of this study indicate that this recombinant baculovirus is a potential candidate for the further development of more effective combined genetic engineering vaccines against MPS and PMWS. This experiment also provides ideas for vaccine development for other concomitant diseases using the baculovirus expression system.

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