Plant cell-secreted stem cell factor stimulates expansion and differentiation of hematopoietic stem cells

Wang, Xiaoting; Karki, Uddhab; Abeygunaratne, Hasara; Unnold-Cofre, Carmela; Xu, Jianfeng

doi:10.1016/j.procbio.2020.09.029

Cited by 16 publications

(10 citation statements)

References 37 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…For instance, when enhanced green fluorescence protein (EGFP) was expressed as a fusion with (SP) 32 , consisting of 32 repeats of the SP dipeptide, a substantial increase in yields was observed (Dolan et al 2014 ). Also, the inclusion of 20 tandem repeats of SP dipeptide remarkably increased the total expression level and the secretory yield without affecting the function of the stem cell factor (Wang et al 2021 ). Consistently, this current investigation demonstrated that the expression level of untagged rGn, driven by the pBK19 construct, remained below the detection threshold (Fig.…”

Section: Discussionmentioning

confidence: 99%

Gn protein expressed in plants for diagnosis of severe fever with thrombocytopenia syndrome virus

Chang,

Shimoda,

Jiang

et al. 2024

Appl Microbiol Biotechnol

View full text Add to dashboard Cite

Severe fever with thrombocytopenia syndrome virus (SFTSV) causes the highly fatal disease in humans. To facilitate diagnosis, the native form of subunit glycoprotein (Gn), a prime target for potential vaccines and therapies, was produced in Nicotiana benthamiana using a Bamboo mosaic virus-based vector system. By fusion with secretory signal tags, SSExt, derived from the extension protein, and the (SP)10 motif, the yield of the recombinant Gn (rGn) was remarkably increased to approximately 7 mg/kg infiltrated leaves. Ultimately, an rGn-based ELISA was successfully established for the detection of SFTSV-specific antibodies in serum samples from naturally infected monkeys. As validated with the reference method, the specificity and sensitivity of rGn-ELISA were 94% and 96%, respectively. In conclusion, utilizing well-suited fusion tags facilitates rGn production and purification in substantial quantities while preserving its antigenic properties. The rGn-ELISA, characterized by its commendable sensitivity and specificity could serve as a viable alternative diagnostic method for assessing SFTSV seroprevalence. Key points • SFTSV Gn, fused with secretory signal tags, was expressed by the BaMV-based vector. • The plant fusion tags increased expression levels and eased the purification of rGn. • The rGn-ELISA was established and validated; its specificity and sensitivity > 94%.

show abstract

Section: Discussionmentioning

confidence: 99%

Gn protein expressed in plants for diagnosis of severe fever with thrombocytopenia syndrome virus

Chang,

Shimoda,

Jiang

et al. 2024

Appl Microbiol Biotechnol

View full text Add to dashboard Cite

show abstract

“…Codon optimization of recombinant protein sequences in favor of the codon usage of the expression hosts has been shown in numerous studies as an effective means of increasing translation efficiency and protein yield. In a recent study, codon optimization led to a 25-to 30-fold increase in the yield of a recombinant stem cell factor (SCF) protein in tobacco BY-2 cells [42]. In contrast, there are also contradictory reports of the effects of codon optimization.…”

Section: Codon Optimizationmentioning

confidence: 99%

“…Similarly, through a parallel comparison with several commonly used SP sequences, the native extensin secretory signal NbSS Ext was highlighted to be the most efficient one in terms of recombinant protein yield and secretion in N. benthamiana [84]. However, its closest counterpart, the NtSS Ext /SS tob from N. tabacum (differing from NbSS Ext by only one amino acid residue, Table 2), was not included in this comparison considering the successful stories of the NtSS Ext /SS tob used for the expression of various recombinant pharmaceutical proteins [42,[85][86][87]. Interestingly, some mammal native SPs can also be recognized and accurately processed in plant cells.…”

Section: Apoplastmentioning

confidence: 99%

“…Different HypGP designs have been reported for the production of various biopharmaceutical proteins. The utilization of AGP-derived tandem repeat of (SP) n (n usually ranges from 10 to 32) tags has led to high secretion yields of active recombinant therapeutic proteins in tobacco BY-2 cell culture, such as human interferon α2b (IFNα2) [85], human growth hormone (hGH) [86], and human stem cell factor (SCF) [42]. Another AGPstyle tag (AP) 20 has also been tested and showed similar potential to increase the secreted yield of the recombinant human α1-antitrypsin (AAT) in tobacco BY-2 cell culture [103].…”

Section: Fusion Of Protein Partners/carriers/peptide Tagsmentioning

confidence: 99%

See 1 more Smart Citation

Improving Protein Quantity and Quality—The Next Level of Plant Molecular Farming

Liu

Timko

2022

IJMS

View full text Add to dashboard Cite

Plants offer several unique advantages in the production of recombinant pharmaceuticals for humans and animals. Although numerous recombinant proteins have been expressed in plants, only a small fraction have been successfully put into use. The hugely distinct expression systems between plant and animal cells frequently cause insufficient yield of the recombinant proteins with poor or undesired activity. To overcome the issues that greatly constrain the development of plant-produced pharmaceuticals, great efforts have been made to improve expression systems and develop alternative strategies to increase both the quantity and quality of the recombinant proteins. Recent technological revolutions, such as targeted genome editing, deconstructed vectors, virus-like particles, and humanized glycosylation, have led to great advances in plant molecular farming to meet the industrial manufacturing and clinical application standards. In this review, we discuss the technological advances made in various plant expression platforms, with special focus on the upstream designs and milestone achievements in improving the yield and glycosylation of the plant-produced pharmaceutical proteins.

show abstract

“…The codon optimization process uses synonymous codons without altering the protein amino acid sequence to increase translational efficiency ( Webster et al., 2017 ). For instance, through codon optimization, the expression of stem cell factor (SCF) for ex vivo RBC production increased 25- to 30-fold in tobacco Bright Yellow-2 (BY-2) cells ( Wang et al., 2021 ). In another study, a codon-optimized BvLz was stably expressed in sugarcane culms ( Damaj et al., 2020 ).…”

Section: Heterologous Expression Of Recombinant Proteins In Plantsmentioning

confidence: 99%

Plant-based expression platforms to produce high-value metabolites and proteins

Kulshreshtha¹,

Sharma

Padilla³

et al. 2022

Front. Plant Sci.

View full text Add to dashboard Cite

Plant-based heterologous expression systems can be leveraged to produce high-value therapeutics, industrially important proteins, metabolites, and bioproducts. The production can be scaled up, free from pathogen contamination, and offer post-translational modifications to synthesize complex proteins. With advancements in molecular techniques, transgenics, CRISPR/Cas9 system, plant cell, tissue, and organ culture, significant progress has been made to increase the expression of recombinant proteins and important metabolites in plants. Methods are also available to stabilize RNA transcripts, optimize protein translation, engineer proteins for their stability, and target proteins to subcellular locations best suited for their accumulation. This mini-review focuses on recent advancements to enhance the production of high-value metabolites and proteins necessary for therapeutic applications using plants as bio-factories.

show abstract

Plant cell-secreted stem cell factor stimulates expansion and differentiation of hematopoietic stem cells

Cited by 16 publications

References 37 publications

Gn protein expressed in plants for diagnosis of severe fever with thrombocytopenia syndrome virus

Gn protein expressed in plants for diagnosis of severe fever with thrombocytopenia syndrome virus

Improving Protein Quantity and Quality—The Next Level of Plant Molecular Farming

Plant-based expression platforms to produce high-value metabolites and proteins

Contact Info

Product

Resources

About