ArticleBMC biotechnology2021
A novel approach of recombinant laterosporulin production using the N-SH2 domain of SHP-2.
Article in BMC biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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5 authors at 1 institution in 1 country.
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Abstract
backgroundThe current study was aimed at evaluating the role of the N-SH2 domain of SHP-2 as a partner protein in the expression of a toxic peptide, laterosporulin (LTS). We also investigated its effects on the formation of the disulfide bond and functional folding of the peptide in vitro. The N-SH2-LTS protein was expressed as a His-tagged fusion protein, capable of undergoing enzymatic cleavage.
resultsBased on the data presented herein, the total yield of the folded fusion protein from inclusion bodies was found to be about 105 mg/l, demonstrating a high-level of heterologous expression. After enzymatic cleavage, 1.5 mg of the folded recombinant laterosporulin was obtained from each 10 mg of the fusion protein. The purity of the recombinant laterosporulin was analyzed by RP-HPLC, to yield peptides with suitable purity (85%).
conclusionsOur findings indicated the advantages of using the N-SH2 domain of SHP-2 as a rapid and easy approach not only in producing easy target proteins but also in its function as a chaperone. N-SH2 domain of SHP-2 can influence on the purification of laterosporulin at reasonable yield and in a cost-effective fashion. The N-SH2 domain of SHP-2 as a protein chaperone may be potentially favorable to produce other proteins with disulfide bonds.
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