Identification of secretion domain of Neospora caninum profilin

Suhaimi, Hamizah and Xu, Jian and Kato, Tatsuya and Doddy, Irawan Setyo Utomo (2019) Identification of secretion domain of Neospora caninum profilin. Biochemistry Biophysics Resources Community, 522 (1). pp. 8-13.

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Profilin (PROF) is a small actin-binding protein presented in apicomplexan protozoa. It was previously reported that Neospora caninum profilin (NcPROF) is secreted into the hemolymph of silkworm larvae regardless of the lack of an identified regular secretion signal peptide. To date, which domain is required for its secretion still remains unknown. To this end, we express a fluorescent protein (mCherry) fused with NcPROF at its N-terminus or C-terminus. Both fusion proteins were expressed and secreted into the culture supernatant from Bm5 cells or hemolymph from silkworm larvae, respectively. To further narrow down the C-terminal minimal domain required for its secretion, we constructed three truncated C-terminal domain constructions, ΔN (aa41-163), ΔN1 (aa50-163), and ΔN2 (aa144-163) respectively. All three fusion proteins were detected in the culture supernatant of Bm5 cells and silkworm hemolymph. Surprisingly, a 20-aa C-terminal α-helix domain facilitates the secretion of mCherry, allowing purification of ΔN2-mCherry from silkworm larval hemolymph by affinity chromatography. Taken together, the secretion domain from NcPROF was identified, indicating that can be utilized for the secretory expression of recombinant proteins in the future.

Item Type: Article
Additional Information: DDC'23: 572.6
Uncontrolled Keywords: Neospora caninum profilin; Secretion domain; Truncation; Protein expression
Subjects: Medicine & Biology
Divisions: OR Kesehatan > Bahan_Baku_Obat_dan_Obat_Tradisiona
Depositing User: Rasty -
Date Deposited: 15 Dec 2022 03:00
Last Modified: 15 Dec 2022 03:00

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