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https://doi.org/10.3390/ijms131115162
Title: | The characterization of SaPIN2b, a plant trichome-localized proteinase inhibitor from Solanum americanum | Authors: | Luo, M Ding, L.-W Ge, Z.-J Wang, Z.-Y Hu, B.-L Yang, X.-B Sun, Q.-Y Xu, Z.-F |
Keywords: | chymotrypsin hybrid protein proteinase inhibitor 2a proteinase inhibitor 2b serine proteinase inhibitor subtilisin trypsin unclassified drug PIN2 protein, Solanum americanum recombinant protein serine proteinase inhibitor vegetable protein amino acid sequence article controlled study enzyme inhibition Escherichia coli gene overexpression Helicoverpa armigera homozygosity IC 50 insect resistance mortality nonhuman nucleotide sequence plant defense plant gene plant pathogen interaction polymerase chain reaction promoter region protein expression protein function protein inhibitor 2 gene protein purification pupation sequence alignment Solanum Solanum americanum tobacco transgenic plant trichome upregulation Western blotting wild type animal chemistry dose response enzymology gene expression genetics isolation and purification molecular genetics moth parasitology Amino Acid Sequence Animals Dose-Response Relationship, Drug Gene Expression Molecular Sequence Data Moths Plant Proteins Plants, Genetically Modified Recombinant Proteins Sequence Alignment Serine Proteinase Inhibitors Solanum Tobacco Trichomes |
Issue Date: | 2012 | Citation: | Luo, M, Ding, L.-W, Ge, Z.-J, Wang, Z.-Y, Hu, B.-L, Yang, X.-B, Sun, Q.-Y, Xu, Z.-F (2012). The characterization of SaPIN2b, a plant trichome-localized proteinase inhibitor from Solanum americanum. International Journal of Molecular Sciences 13 (11) : 15162-15176. ScholarBank@NUS Repository. https://doi.org/10.3390/ijms131115162 | Rights: | Attribution 4.0 International | Abstract: | Proteinase inhibitors play an important role in plant resistance of insects and pathogens. In this study, we characterized the serine proteinase inhibitor SaPIN2b, which is constitutively expressed in Solanum americanum trichomes and contains two conserved motifs of the proteinase inhibitor II (PIN2) family. The recombinant SaPIN2b (rSaPIN2b), which was expressed in Escherichia coli, was demonstrated to be a potent proteinase inhibitor against a panel of serine proteinases, including subtilisin A, chymotrypsin and trypsin. Moreover, rSaPIN2b also effectively inhibited the proteinase activities of midgut trypsin-like proteinases that were extracted from the devastating pest Helicoverpa armigera. Furthermore, the overexpression of SaPIN2b in transgenic tobacco plants resulted in enhanced resistance against H. armigera. Taken together, our results demonstrated that SaPIN2b is a potent serine proteinase inhibitor that may act as a protective protein in plant defense against insect attacks. © 2012 by the authors; licensee MDPI, Basel, Switzerland. | Source Title: | International Journal of Molecular Sciences | URI: | https://scholarbank.nus.edu.sg/handle/10635/183243 | ISSN: | 16616596 | DOI: | 10.3390/ijms131115162 | Rights: | Attribution 4.0 International |
Appears in Collections: | Staff Publications Elements |
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