Biocontrol Potential of Sodin 5, Type 1 Ribosome-Inactivating Protein from Salsola soda L. Seeds

被引:1
|
作者
Babic, Monika Novak [1 ]
Ragucci, Sara [2 ]
Leonardi, Adrijana [3 ]
Pavsic, Miha [4 ]
Landi, Nicola [2 ,5 ]
Krizaj, Igor [3 ]
Gunde-Cimerman, Nina [1 ]
Sepcic, Kristina [1 ]
Di Maro, Antimo [2 ]
机构
[1] Univ Ljubljana, Biotech Fac, Dept Biol, Ljubljana 1000, Slovenia
[2] Univ Campania Luigi Vanvitelli, Dept Environm Biol & Pharmaceut Sci & Technol DiST, I-81100 Caserta, Italy
[3] Jozef Stefan Inst, Dept Mol & Biomed Sci, Ljubljana 1000, Slovenia
[4] Univ Ljubljana, Fac Chem & Chem Technol, Dept Chem & Biochem, Ljubljana 1000, Slovenia
[5] Inst Crystallog, Inst Crystallo, I-81100 Caserta, Italy
关键词
agretti; antifungal activity; bioinsecticide; halophilic fungi; mass spectrometry; ribosome-inactivating protein; ADENOSINE GLYCOSIDASE; PLANT; SEQUENCE; FUNGI; POLYNUCLEOTIDE; SALTERNS; ECOLOGY; CHAIN; DNA;
D O I
10.3390/biom14030336
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Sodin 5 is a type 1 ribosome-inactivating protein isolated from the seeds of Salsola soda L., an edible halophytic plant that is widespread in southern Europe, close to the coast. This plant, known as 'agretti', is under consideration as a new potential crop on saline soils. Considering a possible defence role of sodin 5 in the plant, we report here its antifungal activity against different halophilic and halotolerant fungi. Our results show that sodin 5 at a concentration of 40 mu g/mL (1.4 mu M) was able to inhibit the growth of the fungi Trimmatostromma salinum (35.3%), Candida parapsilosis (24.4%), Rhodotorula mucilaginosa (18.2%), Aspergillus flavus (12.2%), and Aureobasidium melanogenum (9.1%). The inhibition observed after 72 h was concentration-dependent. On the other hand, very slight growth inhibition was observed in the fungus Hortaea werneckii (4.2%), which commonly inhabits salterns. In addition, sodin 5 showed a cytotoxic effect on the Sf9 insect cell line, decreasing the survival of these cells to 63% at 1.0 mu g/mL (34.5 nM). Structural analysis of sodin 5 revealed that its N-terminal amino acid residue is blocked. Using mass spectrometry, sodin 5 was identified as a homologous to type 1 polynucleotide:adenosine glycosylases, commonly known as ribosome-inactivating proteins from the Amaranthaceae family. Twenty-three percent of its primary structure was determined, including the catalytic site.
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页数:16
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