Pathogen-induced expression of a cecropin A-melittin antimicrobial peptide gene confers antifungal resistance in transgenic tobacco

2005 ◽  
Vol 56 (416) ◽  
pp. 1685-1695 ◽  
Author(s):  
Dmytro P. Yevtushenko ◽  
Rafael Romero ◽  
Benjamin S. Forward ◽  
Robert E. Hancock ◽  
William W. Kay ◽  
...  
2021 ◽  
Author(s):  
Zie Wang ◽  
Jie Deng ◽  
Tingting Liang ◽  
Linlin Su ◽  
Lilei Zheng ◽  
...  

Abstract Background: WRKY transcription factors (TFs) play vital roles in plant growth and development, secondary metabolite synthesis, and response to biotic and abiotic stresses. In a previous transcriptome sequencing analysis of Lilium regale Wilson, we identified multiple WRKY TFs that respond to exogenous methyl jasmonate treatment and lily Fusarium wilt (Fusarium oxysporum).Results: In the present study, the WRKY TF LrWRKY3 was further analyzed to reveal its function in defense response to F. oxysporum. The LrWRKY3 protein was localized in the plant cell nucleus, and LrWRKY3 transgenic tobacco lines showed higher resistance to F. oxysporum compared with wild-type (WT) tobacco. In addition, some genes related to jasmonic acid (JA) biosynthesis, salicylic acid (SA) signal transduction, and disease resistance had higher transcriptional levels in the LrWRKY3 transgenic tobacco lines than in the WT. On the contrary, L. regale scales transiently expressing LrWRKY3 RNA interference fragments showed higher sensitivity to F. oxysporum infection. Moreover, a F. oxysporum-induced defensin gene, Def1, was isolated from L. regale, and the recombinant protein LrDef1 isolated and purified from Escherichia coli possessed antifungal activity to several phytopathogens, including F. oxysporum. Furthermore, co-expression of LrWRKY3 and the LrDef1 promoter in tobacco evidently up-regulated the expression activity of the LrDef1 promoter.Conclusions: These results clearly indicate that LrWRKY3 is an important positive regulator in response to F. oxysporum infection, and one of its targets is the antimicrobial peptide gene LrDef1.


2000 ◽  
Vol 13 (8) ◽  
pp. 860-868 ◽  
Author(s):  
Ichiro Mitsuhara ◽  
Hiroki Matsufuru ◽  
Masahiro Ohshima ◽  
Hisatoshi Kaku ◽  
Yuki Nakajima ◽  
...  

We demonstrate here that induced expression of sarcotoxin IA, a bactericidal peptide from Sarcophaga peregrina, enhanced the resistance of transgenic tobacco plants to both bacterial and fungal pathogens. The peptide was produced with a modified PR1a promoter, which is further activated by salicylic acid treatment and necrotic lesion formation by pathogen infection. Host resistance to infection of bacteria Erwinia carotovora subsp. carotovora and Pseudomonas syringae pv. tabaci was shown to be dependent on the amounts of sarcotoxin IA expressed. Since we found antifungal activity of the peptide in vitro, transgenic seedlings were also inoculated with fungal pathogens Rhizoctonia solani and Pythium aphanidermatum. Transgenic plants expressing higher levels of sarcotoxin were able to withstand fungal infection and remained healthy even after 4 weeks, while control plants were dead by fungal infection after 2 weeks.


2003 ◽  
Vol 23 (22) ◽  
pp. 8272-8281 ◽  
Author(s):  
Hanna Uvell ◽  
Ylva Engström

ABSTRACT Innate immune reactions are crucial processes of metazoans to protect the organism against overgrowth of faster replicating microorganisms. Drosophila melanogaster is a precious model for genetic and molecular studies of the innate immune system. In response to infection, the concerted action of a battery of antimicrobial peptides ensures efficient killing of the microbes. The induced gene expression relies on translocation of the Drosophila Rel transcription factors Relish, Dif, and Dorsal to the nucleus where they bind to κB-like motifs in the promoters of the inducible genes. We have identified another putative promoter element, called region 1 (R1), in a number of antimicrobial peptide genes. Site-directed mutagenesis of the R1 site diminished Cecropin A1 (CecA1) expression in transgenic Drosophila larvae and flies. Infection of flies induced a nuclear R1-binding activity that was unrelated to the κB-binding activity in the same extracts. Although the R1 motif was required for Rel protein-mediated CecA1 expression in cotransfection experiments, our data argue against it being a direct target for the Drosophila Rel proteins. We propose that the R1 and κB motifs are targets for distinct regulatory complexes that act in concert to promote high levels of antimicrobial peptide gene expression in response to infection.


2014 ◽  
Vol 14 (1) ◽  
pp. 102 ◽  
Author(s):  
Mireia Bundó ◽  
Laura Montesinos ◽  
Esther Izquierdo ◽  
Sonia Campo ◽  
Delphine Mieulet ◽  
...  

Oncotarget ◽  
2017 ◽  
Vol 8 (17) ◽  
pp. 27943-27952 ◽  
Author(s):  
Xi Chen ◽  
Guangying Qi ◽  
Mingqun Qin ◽  
Yantao Zou ◽  
Kanghua Zhong ◽  
...  

2021 ◽  
Vol 88 ◽  
pp. 108543
Author(s):  
Babajide A. Ojo ◽  
Peiran Lu ◽  
Sanmi E. Alake ◽  
Bryant Keirns ◽  
Kendall Anderson ◽  
...  

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