Recombinant expression systems

2016 ◽  
pp. 224-301 ◽  
Keyword(s):  
Recombinant Expression ◽  
Expression Systems

scholarly journals The multifunctionality of expression systems in Bacillus subtilis: Emerging devices for the production of recombinant proteins

2021 ◽  
pp. 153537022110301
Author(s):  
Caio Coutinho de Souza ◽  
Jander Matos Guimarães ◽  
Soraya dos Santos Pereira ◽  
Luis André Morais Mariúba
Keyword(s):  
Bacillus Subtilis ◽  
Recombinant Proteins ◽  
Large Scale ◽  
Recombinant Expression ◽  
Academic Research ◽  
Future Research ◽  
Expression Systems ◽  
Bioactive Substances ◽  
Exogenous Dna ◽  
Chemical Inducers

Bacillus subtilis is a successful host for producing recombinant proteins. Its GRAS (generally recognized as safe) status and its remarkable innate ability to absorb and incorporate exogenous DNA into its genome make this organism an ideal platform for the heterologous expression of bioactive substances. The factors that corroborate its value can be attributed to the scientific knowledge obtained from decades of study regarding its biology that has fostered the development of several genetic engineering strategies, such as the use of different plasmids, engineering of constitutive or double promoters, chemical inducers, systems of self-inducing expression with or without a secretion system that uses a signal peptide, and so on. Tools that enrich the technological arsenal of this expression platform improve the efficiency and reduce the costs of production of proteins of biotechnological importance. Therefore, this review aims to highlight the major advances involving recombinant expression systems developed in B. subtilis, thus sustaining the generation of knowledge and its application in future research. It was verified that this bacterium is a model in constant demand and studies of the expression of recombinant proteins on a large scale are increasing in number. As such, it represents a powerful bacterial host for academic research and industrial purposes.

Recombinant expression systems for the production of collagen

2000 ◽  
Vol 28 (4) ◽  
pp. 350 ◽  
Author(s):  
N.J. Bulleid ◽  
D.C.A. John ◽  
K.E. Kadler
Keyword(s):  
Recombinant Expression ◽  
Expression Systems

scholarly journals Recombinant expression systems: the obstacle to helminth vaccines?

2007 ◽  
Vol 23 (11) ◽  
pp. 527-532 ◽  
Author(s):  
Peter Geldhof ◽  
Veerle De Maere ◽  
Jozef Vercruysse ◽  
Edwin Claerebout
Keyword(s):  
Recombinant Expression ◽  
Expression Systems

Comparative production of human interleukin-2 fused with green fluorescent protein in several recombinant expression systems

2005 ◽  
Vol 24 (3) ◽  
pp. 225-233 ◽  
Author(s):  
Hyung Joon Cha ◽  
Hwa Sung Shin ◽  
Hye Jung Lim ◽  
Hye Sook Cho ◽  
Nimish N. Dalal ◽  
...  
Keyword(s):  
Green Fluorescent Protein ◽  
Fluorescent Protein ◽  
Recombinant Expression ◽  
Interleukin 2 ◽  
Expression Systems ◽  
Green Fluorescent

Oxidation of L-tryptophan in biology: a comparison between tryptophan 2,3-dioxygenase and indoleamine 2,3-dioxygenase

2009 ◽  
Vol 37 (2) ◽  
pp. 408-412 ◽  
Author(s):  
Sara A. Rafice ◽  
Nishma Chauhan ◽  
Igor Efimov ◽  
Jaswir Basran ◽  
Emma Lloyd Raven
Keyword(s):  
Structural Information ◽  
Recombinant Expression ◽  
Kynurenine Pathway ◽  
Expression Systems ◽  
Indoleamine 2,3 Dioxygenase ◽  
Rate Limiting Step ◽  
Limiting Step ◽  
The Family ◽  
And Function ◽  
Rate Limiting

The family of haem dioxygenases catalyse the initial oxidative cleavage of L-tryptophan to N-formylkynurenine, which is the first, rate-limiting, step in the L-kynurenine pathway. In the present paper, we discuss and compare structure and function across the family of haem dioxygenases by focusing on TDO (tryptophan 2,3-dioxygenase) and IDO (indoleamine 2,3-dioxygenase), including a review of recent structural information for both enzymes. The present paper describes how the recent development of recombinant expression systems has informed our more detailed understanding of the substrate binding, catalytic activity and mechanistic properties of these haem dioxygenases.

scholarly journals The Collagen V Homotrimer[α1(V)]3Production Is Unexpectedly Favored over the Heterotrimer[α1(V)]2α2(V)in Recombinant Expression Systems

2010 ◽  
Vol 2010 ◽  
pp. 1-13 ◽  
Author(s):  
Muriel Roulet ◽  
Merja Välkkilä ◽  
Hélène Chanut-Delalande ◽  
Eija-Riitta Hämäläinen ◽  
Efrat Kessler ◽  
...  
Keyword(s):  
Mammalian Cells ◽  
Molecular Form ◽  
Recombinant Expression ◽  
Expression Systems ◽  
Key Factors ◽  
Double Immunofluorescence ◽  
Hek 293 ◽  
Transfected Cells ◽  
Biomedical Device ◽  
Cell Expression

Collagen V, a fibrillar collagen with important functions in tissues, assembles into distinct chain associations. The most abundant and ubiquitous molecular form is the heterotrimer[α1(V)]2α2(V). In the attempt to produce high levels of recombinant collagen V heterotrimer for biomedical device uses, and to identify key factors that drive heterotrimeric chain association, several cell expression systems (yeast, insect, and mammalian cells) have been assayed by cotransfecting the human proα1(V) and proα2(V) chain cDNAs. Suprisingly, in all recombinant expression systems, the formation of[α1(V)]3homotrimers was considerably favored over the heterotrimer. In addition, pepsin-sensitive proα2(V) chains were found in HEK-293 cell media indicating that these cells lack quality control proteins preventing collagen monomer secretion. Additional transfection withHsp47cDNA, encoding the collagen-specific chaperone Hsp47, did not increase heterotrimer production. Double immunofluorescence with antibodies against collagen Vα-chains showed that, contrary to fibroblasts, collagen Vα-chains did not colocalized intracellularly in transfected cells. Monensin treatment had no effect on the heterotrimer production. The heterotrimer production seems to require specific machinery proteins, which are not endogenously expressed in the expression systems. The different constructs and transfected cells we have generated represent useful tools to further investigate the mechanisms of collagen trimer assembly.

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