Strategies for Optimizing the Production of Proteins and Peptides with Multiple Disulfide Bonds
Abstract
:1. Introduction
2. Host Strains for the Overexpression of Target Proteins
3. Location of Expression
4. Vector Selection for Expression
5. Signal Peptide in Fusion Expression
6. Co-Expression of Chaperones
7. Soluble and Insoluble Expression
8. Purification
9. Conclusions
Author Contributions
Funding
Acknowledgments
Conflicts of Interest
References
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Advantages | Disadvantages |
---|---|
Rapid expression | Proteins with disulfide bonds are difficult to express |
High yields | Production of unglycosylated proteins |
Ease of culture and genome modifications | Proteins with endotoxins are produced |
Inexpensive | Acetate formation results in cell toxicity |
Rapid mass production and cost-effective | Proteins produced as inclusion bodies are inactive; thus, refolding is required. |
Advantages | Disadvantages |
---|---|
High yield | N or O-linked glycosylation pattern (different from higher eukaryote) Hypermannosylation Proteolytic degradation |
Stable production strains | |
Durability | |
Cost-effective | |
High-density growth | |
High productivity | |
Suitable for isotopically labeled protein production | |
Rapid growth in chemically defined media | |
Product processing similar to mammalian cells | |
Can handle S–S-rich proteins | |
Can assist in protein folding | |
Can glycosylate proteins |
Host | Recombinant Protein | Reference |
---|---|---|
E. coli | venom proteins | [83,84] |
P. pastoris S. cerevisiae | lipase r27RC rat protein disulfide isomerase | [85] [86] |
L. lactis | Merozoite antigens | [87] |
Advantage | Disadvantage | |
---|---|---|
Cytoplasmic | Higher expression level, simple plasmid construction | Inclusion body may be formed, unfavorable conditions for S-S bond formation, higher proteolysis |
Periplasmic | Less proteolysis, improved folding, simple purification | Inclusion body may be formed, the signal does not always facilitate export |
Extracellular | Least extensive proteolysis, simpler purification (fewer protein species), improved folding | Usually no secretion is observed, purification may be complex (protein dilution) |
Vector | Induction (IPTG) | Level of Expression | Key Feature |
---|---|---|---|
lac | 0.2 mM | Low to moderate levels; 15–30% of total cell proteins | Weak, regulated, suitable for gene products at very low intracellular level; comparatively expensive induction |
Trc and tac | 0.2 mM | Moderately high | High-level, but lower than T7 system; regulated expression still possible; comparatively expensive induction; high basal level |
T7 RNA polymerase | 0.2 mM | Very high; 40–50% of total cell proteins | Utilizes T7 RNA polymerase; high-level inducible overexpression; T7lac system for tight control of induction needed for more toxic clones; relatively expensive induction; basal level depends on used strain (pLys) |
Phage promoter PL | Shifting the temperature from 30 to 42 °C (45 °C) | Moderately high | Temperature-sensitive host required; lower likelihood of “leaky” non-induced expression; basal level, high basal level by temperatures below 30 °C |
Peptide | Disulfide Number |
---|---|
Beta-defensin | 3 |
hepcidin | 3/4 |
DkTx | 6 |
ASPA | 3 |
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Ma, Y.; Lee, C.-J.; Park, J.-S. Strategies for Optimizing the Production of Proteins and Peptides with Multiple Disulfide Bonds. Antibiotics 2020, 9, 541. https://doi.org/10.3390/antibiotics9090541
Ma Y, Lee C-J, Park J-S. Strategies for Optimizing the Production of Proteins and Peptides with Multiple Disulfide Bonds. Antibiotics. 2020; 9(9):541. https://doi.org/10.3390/antibiotics9090541
Chicago/Turabian StyleMa, Yunqi, Chang-Joo Lee, and Jang-Su Park. 2020. "Strategies for Optimizing the Production of Proteins and Peptides with Multiple Disulfide Bonds" Antibiotics 9, no. 9: 541. https://doi.org/10.3390/antibiotics9090541