Please use this identifier to cite or link to this item: 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
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