Secretion of the Antibacterial Recombinant Protein Enbocin

2008 ◽  
Vol 63 (3-4) ◽  
pp. 284-288 ◽  
Author(s):  
Tae Won Goo ◽  
Eun Young Yun ◽  
Sung Wan Kim ◽  
Kwang Ho Choi ◽  
Seok Woo Kang ◽  
...  
Keyword(s):  
Recombinant Proteins ◽  
Gene Fusion ◽  
Large Scale ◽  
Biologically Active ◽  
Vector System ◽  
Fusion Partner ◽  
Scale Production ◽  
Baculovirus Expression ◽  
Large Scale Production ◽  
Baculovirus Expression Vector

The insect baculovirus expression vector system (BEVS) is useful for the production of biologically active recombinant proteins. However, the overexpression of foreign proteins in this system often results in misfolded proteins and the formation of protein aggregates. To overcome this limitation, we have developed a versatile baculovirus expression and secretion system using the Bombyx mori protein disulfide isomerase (bPDI) as a fusion partner. bPDI gene fusion improved the secretion and antibacterial activity of recombinant enbocin proteins. Thus, bPDI gene fusion is a useful addition to the BEVS for the large-scale production of bioactive recombinant proteins

scholarly journals Plant expression systems for production of hemagglutinin as a vaccine against influenza virus.

2014 ◽  
Vol 61 (3) ◽  
Author(s):  
Patrycja Redkiewicz ◽  
Agnieszka Sirko ◽  
Katarzyna Anna Kamel ◽  
Anna Góra-Sochacka
Keyword(s):  
Influenza Virus ◽  
Large Scale ◽  
Immunological Response ◽  
Biologically Active ◽  
Scale Production ◽  
Expression Systems ◽  
Lethal Challenge ◽  
Subunit Vaccines ◽  
Large Scale Production ◽  
Major Surface

Many examples of a successful application of plant-based expression systems for production of biologically active recombinant proteins exist in the literature. These systems can function as inexpensive platforms for the large scale production of recombinant pharmaceuticals or subunit vaccines. Hemagglutinin (HA) is a major surface antigen of the influenza virus, thus it is in the centre of interests of various subunit vaccine engineering programs. Large scale production of recombinant HA in traditional expression systems, such as mammalian or insect cells, besides other limitations, is expensive and time-consuming. These difficulties stimulate an ever-increasing interest in plant-based production of this recombinant protein. Over the last few years many successful cases of HA production in plants, using both transient and stable expression systems have been reported. Various forms of recombinant HA, including monomers, trimers, virus like particles (VLPs) or chimeric proteins containing its fusion with other polypeptides were obtained and shown to maintain a proper antigenicity. Immunizations of animals (mice, ferrets, rabbits or chickens) with some of these plant-derived hemagglutinin variants were performed, and their effectiveness in induction of immunological response and protection against lethal challenge with influenza virus demonstrated. Plant-produced recombinant subunit vaccines and plant-made VLPs were successfully tested in clinical trials (Phase I and II) that confirmed their tolerance and immunogenicity.

Dimroth´s Rearrangement as a Synthetic Strategy Towards New Heterocyclic Compounds

2020 ◽  
Vol 24 (17) ◽  
pp. 1999-2018
Author(s):  
Vitor F. Ferreira ◽  
Thais de B. da Silva ◽  
Fernanda P. Pauli ◽  
Patricia G. Ferreira ◽  
Luana da S. M. Forezi ◽  
...  
Keyword(s):  
Bioactive Compounds ◽  
Heterocyclic Compounds ◽  
Large Scale ◽  
Molecular Diversity ◽  
Biologically Active ◽  
Scale Production ◽  
Dimroth Rearrangement ◽  
Synthetic Strategy ◽  
Large Scale Production ◽  
Synthetic Approaches

Molecular rearrangements are important tools to increase the molecular diversity of new bioactive compounds, especially in the class of heterocycles. This review deals specifically with a very famous and widely applicable rearrangement known as the Dimroth Rearrangement. Although it has originally been observed for 1,2,3-triazoles, its amplitude was greatly expanded to other heterocycles, as well as from laboratory to large scale production of drugs and intermediates. The reactions that were discussed in this review were selected with the aim of demonstrating the windows that may be open by the Dimroth's rearrangement, especially in what regards the development of new synthetic approaches toward biologically active compounds.

Plants as factories for production of biopharmaceutical and bioindustrial proteins: lessons from cell biologyThis review is one of a selection of papers published in the Special Issue on Plant Cell Biology.

2006 ◽  
Vol 84 (4) ◽  
pp. 679-694 ◽  
Author(s):  
Allison R. Kermode
Keyword(s):  
Recombinant Proteins ◽  
Protein Function ◽  
Cell Biology ◽  
Large Scale ◽  
Production Systems ◽  
Plant Cells ◽  
Scale Production ◽  
Functional Protein ◽  
Large Scale Production ◽  
Engineer Plant

Transgenic plants, seeds, and cultured plant cells are potentially one of the most economical systems for large-scale production of recombinant proteins for industrial and pharmaceutical uses. Biochemical, technical, and economic concerns with current production systems have generated enormous interest in developing plants as alternative production systems. However, various challenges must be met before plant systems can fully emerge as suitable, viable alternatives to current animal-based systems for large-scale production of biopharmaceuticals and other products. Aside from regulatory issues and developing efficient methods for downstream processing of recombinant proteins, there are at least two areas of challenge: (1) Can we engineer plant cells to accumulate recombinant proteins to sufficient levels? (2) Can we engineer plant cells to post-translationally modify recombinant proteins so that they are structurally and functionally similar to the native proteins? Attempts to improve the accumulation of a recombinant protein in plant cells require an appreciation of the processes of gene transcription, mRNA stability, processing, and export, and translation initiation and efficiency. Likewise, many post-translational factors must be considered, including protein stability, protein function and activity, and protein targeting. Moreover, we need to understand how the various processes leading from the gene to the functional protein are interdependent and functionally linked. Manipulation of the post-translational processing machinery of plant cells, especially that for N-linked glycosylation and glycan processing, is a challenging and exciting area. The functions of N-glycan heterogeneity and microheterogeneity, especially with respect to protein function, stability, and transport, are poorly understood and this represents an important area of cell biology.

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