期刊
TOXINS
卷 14, 期 7, 页码 -出版社
MDPI
DOI: 10.3390/toxins14070449
关键词
plant toxin; ribosome-inactivating protein (RIP); type I RIP; rRNA glycosylase activity (EC 3; 2; 2; 22); protein isolation; protein sequencing; mass spectrometry
资金
- Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) [422686308]
- Open Access Publication Fund of the Freie Universitat Berlin
This study identified two new isoforms of type I ribosome-inactivating proteins, sapovaccarin-S1 and -S2, which exhibited higher thermostability and anti-cancer activity. These findings suggest that sapovaccarin-S1 and -S2 are promising candidates for targeted anti-cancer therapy.
Type I ribosome-inactivating proteins (RIPs) are plant toxins that inhibit protein synthesis by exerting rRNA N-glycosylase activity (EC 3.2.2.22). Due to the lack of a cell-binding domain, type I RIPs are not target cell-specific. However once linked to antibodies, so called immunotoxins, they are promising candidates for targeted anti-cancer therapy. In this study, sapovaccarin-S1 and -S2, two newly identified type I RIP isoforms differing in only one amino acid, were isolated from the seeds of Saponaria vaccaria L. Sapovaccarin-S1 and -S2 were purified using ammonium sulfate precipitation and subsequent cation exchange chromatography. The determined molecular masses of 28,763 Da and 28,793 Da are in the mass range typical for type I RIPs and the identified amino acid sequences are homologous to known type I RIPs such as dianthin 30 and saporin-S6 (79% sequence identity each). Sapovaccarin-S1 and -S2 showed adenine-releasing activity and induced cell death in Huh-7 cells. In comparison to other type I RIPs, sapovaccarin-S1 and -S2 exhibited a higher thermostability as shown by nano-differential scanning calorimetry. These results suggest that sapovaccarin-S1 and -S2 would be optimal candidates for targeted anti-cancer therapy.
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