A comprehensive review of signal peptides: Structure, roles, and applications

Owji, Hajar; Nezafat, Navid; Negahdaripour, Manica; Hajiebrahimi, Ali; Ghasemi, Younes

doi:10.1016/j.ejcb.2018.06.003

Cited by 286 publications

(239 citation statements)

References 197 publications

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“…Regarding these facts, when the net positive charge of the n region lowered to zero or get a negative value the rate of transportation across the membrane can significantly decrease. (Freudl, 2018, Owji et al, 2018. The net positive charge for most of the studied signal peptides was +2, and AMY_BACAM had the highest net positive charge in this study.…”

Section: Discussionmentioning

confidence: 52%

“…Replacing of Ala at these positions with other residues, specifically at position -1, disturbs the cleavage site (Owji et al, 2018). Exceptionally, as PPBD_BACSU have a D-scores 0.348, it is not applicable for the secretion of the α-amylase protein.…”

Section: Discussionmentioning

confidence: 99%

“…The most significant normal secretion pathways in B. subtilis are twin-arginine translocation (Tat) pathway, Sec pathway and ATP-binding cassette (ABC) pathway (Tjalsma et al, 2004, Anné et al, 2016. Signal peptides mark the proteins to follow the appropriate secretion pathway (Owji et al, 2018). Three separate domains of H, N, and C are observed in signal peptides.…”

Section: Introductionmentioning

confidence: 99%

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In silico analysis of signal peptides for secretory production of a-amylase in Bacillus subtilis

Asadi

Taheri-Anganeh

Jamali

et al. 2019

APJMBB

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α-Amylases are important commercial enzymes and have a broad application in industrial processes and medicine. Gram-positive bacteria such as Bacillus subtilis are possible host organisms for α-amylases secretory production. Secretion of α-amylases to the culture medium versus intracellular production has several advantages such as prevention of inclusion bodies accumulation, higher product stability and solubility. Signal peptides are considered as one of the most essential elements for successful secretory synthesis of the recombinant proteins. Therefore, by the selection of an efficient signal peptide, secretion of the recombinant protein can be enhanced. The goal of this investigation was the in silico evaluation of several peptides to find the most suitable leader peptides for secretory production of α-amylase in B. subtilis. In present work, 30 signal peptides were selected, and numerous online servers such as SignalP, ProtParam, SOLpro, PRED-TAT and ProtComp was used for investigation of suitable signal peptides. According to in silico predictions all other signal peptides connected to α-amylase were stable and soluble except PPBD_BACSU. PPBD_BACSU because of having D-score below cut-off could not be recognized as a suitable signal peptide for α-amylase. Computational analysis identified QOX2_BACSU may direct protein into transmembrane location and was ignored. All 28 remained were predicted as secretory signal peptides which can excrete protein out of the bacteria. The signal peptides recommended by the present study are valuable for rational designing of secretory soluble α-amylase. Although, such information can be useful for future experimental production of these mentioned secretory proteins.

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Section: Discussionmentioning

confidence: 52%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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In silico analysis of signal peptides for secretory production of a-amylase in Bacillus subtilis

Asadi

Taheri-Anganeh

Jamali

et al. 2019

APJMBB

Self Cite

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“…To efficiently direct a protein for secretion via the ER, it is normally necessary to use of an optimal signal peptide (SP). A comprehensive review on the structure, features, and application of SPs has been published (Owji et al 2018). In principle, SPs derived from efficiently secreted enzymes of the host should be suitable.…”

Section: Optimization Of Protein Secretion: Still a Black Boxmentioning

confidence: 99%

Strategies and Challenges for the Development of Industrial Enzymes Using Fungal Cell Factories

Arnau

Yaver

Hjort

2020

Grand Challenges in Biology and Biotechnology

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“…As this variant occurs in the SP of IL-22BP protein, its potential effect on structural aspects pertinent to SP biological function per se was assessed in more detail by in silico methods. Coding SNPs in signal peptides may alter translocation efficiency, cleavage sites, as well as post-cleavage events [43]. We analyzed the charge, the hydrophobicity, and the helix-breaker amino acid residues comprised in the SP of IL-22PB, as well as the modifications introduced by the p.Leu16Pro variant (Figure 3).…”

Section: In Silico Analysis Of the Pleu16pro Variantmentioning

confidence: 99%

The Rare IL22RA2 Signal Peptide Coding Variant rs28385692 Decreases Secretion of IL-22BP Isoform-1, -2 and -3 and Is Associated with Risk for Multiple Sclerosis

Gómez-Fernández

Portilla

Astobiza

et al. 2020

Cells

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The IL22RA2 locus is associated with risk for multiple sclerosis (MS) but causative variants are yet to be determined. In a single nucleotide polymorphism (SNP) screen of this locus in a Basque population, rs28385692, a rare coding variant substituting Leu for Pro at position 16 emerged significantly (p = 0.02). This variant is located in the signal peptide (SP) shared by the three secreted protein isoforms produced by IL22RA2 (IL-22 binding protein-1(IL-22BPi1), IL-22BPi2 and IL-22BPi3). Genotyping was extended to a Europe-wide case-control dataset and yielded high significance in the full dataset (p = 3.17 × 10−4). Importantly, logistic regression analyses conditioning on the main known MS-associated SNP at this locus, rs17066096, revealed that this association was independent from the primary association signal in the full case-control dataset. In silico analysis predicted both disruption of the alpha helix of the H-region of the SP and decreased hydrophobicity of this region, ultimately affecting the SP cleavage site. We tested the effect of the p.Leu16Pro variant on the secretion of IL-22BPi1, IL-22BPi2 and IL-22BPi3 and observed that the Pro16 risk allele significantly lowers secretion levels of each of the isoforms to around 50%–60% in comparison to the Leu16 reference allele. Thus, our study suggests that genetically coded decreased levels of IL-22BP isoforms are associated with augmented risk for MS.

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A comprehensive review of signal peptides: Structure, roles, and applications

Cited by 286 publications

References 197 publications

In silico analysis of signal peptides for secretory production of a-amylase in Bacillus subtilis

In silico analysis of signal peptides for secretory production of a-amylase in Bacillus subtilis

Strategies and Challenges for the Development of Industrial Enzymes Using Fungal Cell Factories

The Rare IL22RA2 Signal Peptide Coding Variant rs28385692 Decreases Secretion of IL-22BP Isoform-1, -2 and -3 and Is Associated with Risk for Multiple Sclerosis

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