Online citations, reference lists, and bibliographies.

Upstream Strategies To Minimize Proteolytic Degradation Upon Recombinant Production In Escherichia Coli.

M. Murby, M. Uhlén, S. Ståhl
Published 1996 · Biology, Medicine

Cite This
Download PDF
Analyze on Scholarcy
Share
Proteolytic degradation of recombinant proteins represents a major problem related to production of gene products in heterologous hosts. Recombinant DNA technology offers several alternative strategies for stabilization of expressed gene products. These strategies can often give dramatic stabilization effects and can be combined with strategies involving optimization of fermentation conditions or downstream processing schemes. In this review, various genetic approaches to improve the stability of recombinant proteins will be discussed, including (i) choice of host cell strain, (ii) product localization, (iii) use of gene fusion partners, and (iv) product engineering. In addition, the solubility of the gene product can be influenced by factors such as growth temperature, promoter strength, fusion partners, and site-directed changes. Altogether, a battery of approaches can be used to obtain stable gene products.
This paper references
The mechanism and functions of ATP - suppression of phytochrome aggregation by the GroE chaper - dependent proteases in bacterial and animal cells . Eur . J . Bio - onins in Escherichia coli
A. L. Goldberg (1992)
10.1016/0167-7799(94)90021-3
Recent developments in heterologous protein production in Escherichia coli.
R. Hockney (1994)
10.1073/pnas.79.6.1830
Cellular location affects protein stability in Escherichia coli.
K. Talmadge (1982)
Meyer , enzymatic characterization of a protein A - b - lactamase hybrid protein
I. Suominen
10.1016/0378-1119(81)90154-2
Stabilization of a degradable protein by its overexpression in Escherichia coli.
Y. Cheng (1981)
during purification
B. Jansson (1990)
relation to their location in Escherichia coli cells
M. Hansson (1994)
protein A deletion mutants
B. Hammarberg (1990)
10.1016/0167-7799(92)90256-U
Control of in vivo proteolysis in the production of recombinant proteins.
S. Enfors (1992)
10.1016/0167-7799(94)90080-9
Engineering proteins to facilitate bioprocessing.
P. Nygren (1994)
10.1146/annurev.ge.23.120189.001115
Genetics of proteolysis in Escherichia coli*.
S. Gottesman (1989)
10.1002/j.1460-2075.1985.tb03741.x
Immobilization and purification of enzymes with staphylococcal protein A gene fusion vectors.
B. Nilsson (1985)
Power , erichia coli
M. Murby
10.1093/nar/14.18.7487
Secretion of heterologous gene products to the culture medium of Escherichia coli.
L. Abrahmsén (1986)
10.1038/nbt1189-1141
Production of Soluble Recombinant Proteins in Bacteria
C. Schein (1989)
10.1038/nbt0394-285
Single–Step Recovery of a Secreted Recombinant Protein by Expanded Bed Adsorption
M. Hansson (1994)
10.1128/mmbr.56.4.592-621.1992
Regulation by proteolysis: energy-dependent proteases and their targets.
S. Gottesman (1992)
Involvement of the riol . 174 , 771 - – 79 . chaperonin DnaK in the rapid degradation of a mutant protein in Escherichia coli
M. Y. Sherman (1992)
Schen - Genetic solutions
E. R. LaVallie
10.1038/nbt0289-165
Different Approaches to Stabilize a Recombinant Fusion Protein
H. Hellebust (1989)
10.1016/0378-1119(87)90111-9
Extracellular production of cloned α-amylase by Escherichia coli
I. Suominen (1987)
10.1128/jb.170.3.1245-1253.1988
ompT encodes the Escherichia coli outer membrane protease that cleaves T7 RNA polymerase during purification.
J. Grodberg (1988)
Mutation strain JM 101
L. E. Lindler (1991)
Purification and characterization of re - Biotechnol
M. Hartmanis (1991)
Binding activities of a repertoire of single immunoglob - Biophys
E. S. Ward (1989)
Covar - production in Escherichia coli
P. Carter
10.1073/pnas.82.21.7212
Synthesis and secretion of human epidermal growth factor by Escherichia coli.
T. Oka (1985)
10.1021/bk-1990-0427.ch013
Site-Specific Proteolysis of Fusion Proteins
Paul Carter (1990)
Augmentation of protein pro - scale , in ‘ ‘ Principles and Practice of Protein Folding ’ ’ ( Cleland , duction by a combination of the T 7 RNA polymerase system and J . L . , and
M. H. M. Koken
10.1016/0076-6879(90)85008-C
Use of T7 RNA polymerase to direct expression of cloned genes.
F. W. Studier (1990)
Proteases and protein degradation in Esch - state in bacteria
M. R. Maurizi (1992)
Character - affinity fusion approach and its use to express recombinant hu - ization of degP , a gene required for proteolysis in the cell enve - man insulin - like growth factor II
K. L. Strauch (1989)
High level Escherichia coli expres - protection from proteolysis
D. Henner (1992)
Identification of C-terminal extensions that protect proteins from intracellular proteolysis.
J. U. Bowie (1989)
10.1128/jb.173.8.2696-2703.1991
Construction and characterization of Escherichia coli strains deficient in multiple secreted proteases: protease III degrades high-molecular-weight substrates in vivo.
F. Baneyx (1991)
10.1016/0958-1669(93)90012-L
Solubility and secretability.
C. Schein (1993)
, Painton , for the recovery and purification of recombinant proteins
M. R. Ladish
laria blood - stage antigen Ag 332
T. Moks (1987)
Protein secretion pathway in Escherichia coli.
M. Blight (1994)
Dev . 2 , 1851 – 1858 . Ubiquitin fusion augments the yield of cloned gene products in 48
T. R. Butt (1989)
10.1128/aem.57.6.1669-1674.1991
Factors influencing inclusion body formation in the production of a fused protein in Escherichia coli.
L. Strandberg (1991)
10.1016/0378-1119(89)90451-4
Growth at sub-optimal temperatures allows the production of functional, antigen-binding Fab fragments in Escherichia coli.
S. Cabilly (1989)
10.1093/protein/5.6.519
Improved insulin stability through amino acid substitution.
D. Brems (1992)
10.1038/nbt1194-1107
Construction and Characterization of a Set of E. coli Strains Deficient in All Known Loci Affecting the Proteolytic Stability of Secreted Recombinant Proteins
H. J. Meerman (1994)
10.1007/BF00262455
Low temperatures stabilize interferon α-2 against proteolysis in Methylophilus methylotrophus and Escherichia coli
J. A. Chesshyre (1989)
10.1021/bi00180a013
Enhanced in vitro refolding of insulin-like growth factor I using a solubilizing fusion partner.
E. Samuelsson (1994)
Degradation of secreted proteins in Escherichia coli.
F. Baneyx (1992)



This paper is referenced by
10.1016/j.peptides.2004.09.014
Heterologous expression, characterization and structural studies of a hydrophobic peptide from the HIV-1 p24 protein
P. Castilho (2005)
10.1016/J.CES.2005.03.031
Production of recombinant proteins by high cell density culture of Escherichia coli
J. Choi (2006)
10.1007/s10989-019-09904-5
Production of a Recombinant Peptide (Lasioglossin LL ΙΙΙ) and Assessment of Antibacterial and Antioxidant Activity
Abbas Tanhaeian (2019)
SUBSTITUTIONSDE PENICILLIN-BINDING PROTEINS INTERVENANTDANS LA RESISTANCE AUX -LACTAMINES CHEZSTREPTOCOCCUS PNEUMONIAE
R. Carapito (2007)
Bacterial expression of self-assembling peptide hydrogelators
Cem Sonmez (2014)
10.1002/9781118801512.CH7
The Impact of Six Critical Impurities on Recombinant Protein Recovery and Purification from Plant Hosts
Chelsea K. Dixon (2018)
10.1016/S0022-1759(03)00011-5
From EST to IHC: human antibody pipeline for target research.
C. Frisch (2003)
10.1016/J.PEP.2005.01.010
Temperature, media, and point of induction affect the N-terminal processing of interleukin-1beta.
J. C. Covalt (2005)
10.1016/j.pep.2005.03.016
SUMO fusion technology for difficult-to-express proteins
T. Butt (2005)
CARACTERISATION EXHAUSTIVE DES SUBSTITUTIONS DE PENICILLIN-BINDING PROTEINS INTERVENANT DANS LA RESISTANCE AUX β-LACTAMINES CHEZ STREPTOCOCCUS PNEUMONIAE
R. Carapito (2006)
10.1016/J.PROCBIO.2013.01.004
Enhancement of the yield of long helical structure of recombinant nucleocapsid protein of Newcastle
C. F. Yap (2013)
10.1016/j.ymben.2008.04.001
Cell-free metabolic engineering promotes high-level production of bioactive Gaussia princeps luciferase.
A. Goerke (2008)
10.1385/MB:19:3:251
Understanding the art of producing protein and nonprotein molecules in Escherichia coli
P. Balbás (2001)
Control of Proteolysis of Recombinant Proteins in Escherichia coli
A. Rozkov (2001)
10.1006/BBRC.2001.4777
Constitutive expression of protective antigen gene of Bacillus anthracis in Escherichia coli.
Virander S. Chauhan (2001)
10.1016/J.PROCBIO.2004.12.024
Production of a new sea anemone neurotoxin by recombinant Escherichia coli: Optimization of culture conditions using response surface methodology
Yong-hua Wang (2005)
10.1007/s12033-018-0138-8
The Effect of Methyl Jasmonate and Temperature on the Transient Expression of Recombinant Proteins in Cucurbita pepo L.
Vahid Karimzadegan (2018)
10.1016/j.neunet.2005.07.015
A bio-basis function neural network for protein peptide cleavage activity characterisation
Z. Yang (2006)
10.1007/B95567
Analysis and control of proteolysis of recombinant proteins in Escherichia coli.
A. Rozkov (2004)
The production and purification of the 1 , 4-dihydroxy-2-naphthoate octaprenyl-transferase enzyme from Escherichia coli
Emelie Szabo (2012)
Cellulose degradation system of Cytophaga hutchinsonii
Chao-Kuo Liu (2012)
10.1016/J.JBIOTEC.2004.07.011
An efficient expression system for the production of functionally active human LKB1.
J. Martínez-Torrecuadrada (2005)
10.1002/btpr.2377
Bioprocess development workflow: Transferable physiological knowledge instead of technological correlations
Wieland N Reichelt (2017)
10.1016/j.pep.2015.08.017
Antigenic assessment of a recombinant human CD90 protein expressed in prokaryotic expression system.
Narges Yousefi-Rad (2015)
10.1007/s10295-011-1034-4
Increasing recombinant protein production in Escherichia coli through metabolic and genetic engineering
Hendrik Waegeman (2011)
10.1007/s12088-012-0260-4
Cloning of a Family 11 Xylanase Gene from Bacillus amyloliquefaciens CH51 Isolated from Cheonggukjang
C. U. Baek (2012)
10.1134/S207905971606006X
Genetically modified microorganisms as producers of biologically active compounds
M. Padkina (2016)
10.1016/S0021-9673(99)00374-X
Histidines in affinity tags and surface clusters for immobilized metal-ion affinity chromatography of trimeric tumor necrosis factor alpha.
V. Gaberc-Porekar (1999)
10.1007/S00343-011-0282-5
Statistical optimization of medium composition and culture condition for the production of recombinant anti-lipopolysaccharide factor of Eriocheir sinensis in Escherichia coli
Shan Jiang (2011)
Periplasmic expression of D1.3 Fab antibody in E. coli
Shaghayegh Arasteh (2012)
10.1186/1472-6750-14-3
Solubility of recombinant Src homology 2 domains expressed in E. coli can be predicted by TANGO
T. C. B. Andersen (2014)
Improved methods for production and characterisation of Jembrana disease virus proteins
Judhi Rachmat (2010)
See more
Semantic Scholar Logo Some data provided by SemanticScholar