A lipid transfer protein has antifungal and antioxidant activity and suppresses Fusarium head blight disease and DON accumulation in transgenic wheat

2020 ◽  
Author(s):  
John E McLaughlin ◽  
Noura Al Darwish ◽  
Jeffrey Garcia-Sanchez ◽  
Neerja Tyagi ◽  
Harold N Trick ◽  
...  
Keyword(s):  
Antioxidant Activity ◽  
Fusarium Head Blight ◽  
Lipid Transfer Protein ◽  
Field Testing ◽  
Transgenic Wheat ◽  
Lesion Size ◽  
Lipid Transfer ◽  
Head Blight ◽  
Transfer Protein ◽  
Field Suppression

Trichothecene mycotoxins such as deoxynivalenol (DON), are virulence factors of Fusarium graminearum, which causes Fusarium head blight (FHB), one of the most important diseases of small grain cereals. We previously identified a non-specific lipid transfer protein (nsLTP) gene, AtLTP4.4, which was overexpressed in an activation tagged Arabidopsis line resistant to trichothecin (Tcin), a type B trichothecene in the same class as DON. Here we show that overexpression of AtLTP4.4 in transgenic wheat significantly reduced F. graminearum growth in Bobwhite and RB07 lines in the greenhouse and reduced fungal lesion size in detached leaf assays. Hydrogen peroxide accumulation was attenuated upon exposure of transgenic wheat plants to DON, indicating that AtLTP4.4 may confer resistance by inhibiting oxidative stress. Field testing indicated that disease severity was significantly reduced in two transgenic Bobwhite lines expressing AtLTP4.4. DON accumulation was significantly reduced in four different transgenic Bobwhite lines expressing AtLTP4.4 or a wheat nsLTP, TaLTP3, which was previously shown to have antioxidant activity. Recombinant AtLTP4.4 purified from Pichia pastoris exhibited potent antifungal activity against F. graminearum. These results demonstrate that overexpression of AtLTP4.4 in transgenic wheat suppresses DON accumulation in the field. Suppression of DON induced reactive oxygen species by AtLTP4.4 might be the mechanism by which fungal spread and mycotoxin accumulation are inhibited in the transgenic wheat plants.

scholarly journals Wheat Apoplast-Localized Lipid Transfer Protein TaLTP3 Enhances Defense Responses Against Puccinia triticina

2021 ◽  
Vol 12 ◽  
Author(s):  
Jiaojie Zhao ◽  
Weishuai Bi ◽  
Shuqing Zhao ◽  
Jun Su ◽  
Mengyu Li ◽  
...  
Keyword(s):  
Leaf Rust ◽  
Lipid Transfer Protein ◽  
Puccinia Triticina ◽  
Defense Responses ◽  
Transgenic Wheat ◽  
Lipid Transfer ◽  
Transfer Protein ◽  
Pathogenesis Related ◽  
Rust Pathogen ◽  
Wheat Lines

Plant apoplast serves as the frontier battlefield of plant defense in response to different types of pathogens. Many pathogenesis-related (PR) proteins are accumulated in apoplastic space during the onset of plant–pathogen interaction, where they act to suppress pathogen infection. In this study, we found the expression of Triticum aestivum lipid transfer protein 3 (TaLTP3) gene was unregulated during incompatible interaction mediated by leaf rust resistance genes Lr39/41 at the early infection stage. Stable transgenic wheat lines overexpressing TaLTP3 exhibited enhanced resistance to leaf rust pathogen Puccinia triticina. Transcriptome analysis revealed that overexpression of TaLTP3 specifically activated the transcription of pathogenesis-related protein 1a (TaPR1a) and multiple plant hormone pathways, including salicylic acid (SA), jasmonic acid (JA), and auxin, in response to the infection of the model bacterial pathogen Pseudomonas syringae pv. tomato DC3000. Further investigation indicated that TaLTP3 physically associated with wheat TaPR1a protein in the apoplast. Transgenic wheat lines overexpressing TaLTP3 and TaPR1a showed higher accumulations of reactive oxygen species (ROS) during plant defense responses. All these findings suggested that TaLTP3 is involved in wheat resistance against leaf rust pathogen infection and forming a TaLTP3-TaPR1a complex in apoplast against this pathogen, which provides new insights into the functional roles of PR proteins.

scholarly journals The key to the allergenicity of lipid transfer protein (LTP) ligands: A structural characterization

2021 ◽  
pp. 158928
Author(s):  
Zulema Gonzalez-Klein ◽  
Bruno Cuevas-Zuviria ◽  
Andrea Wangorsch ◽  
Guadalupe Hernandez-Ramirez ◽  
Diego Pazos-Castro ◽  
...  
Keyword(s):  
Structural Characterization ◽  
Lipid Transfer Protein ◽  
Lipid Transfer ◽  
Transfer Protein

scholarly journals Structural Characterization of Act c 10.0101 and Pun g 1.0101—Allergens from the Non-Specific Lipid Transfer Protein Family

Molecules ◽  
2021 ◽  
Vol 26 (2) ◽  
pp. 256
Author(s):  
Andrea O’Malley ◽  
Swanandi Pote ◽  
Ivana Giangrieco ◽  
Lisa Tuppo ◽  
Anna Gawlicka-Chruszcz ◽  
...  
Keyword(s):  
Immunoglobulin E ◽  
Lipid Transfer Protein ◽  
Mass Spectrometry Analysis ◽  
Lipid Transfer ◽  
Helical Structures ◽  
Spectrometry Analysis ◽  
X Ray Crystallography ◽  
Transfer Protein ◽  
Specific Lipid

(1) Background: Non-specific lipid transfer proteins (nsLTPs), which belong to the prolamin superfamily, are potent allergens. While the biological role of LTPs is still not well understood, it is known that these proteins bind lipids. Allergen nsLTPs are characterized by significant stability and resistance to digestion. (2) Methods: nsLTPs from gold kiwifruit (Act c 10.0101) and pomegranate (Pun g 1.0101) were isolated from their natural sources and structurally characterized using X-ray crystallography (3) Results: Both proteins crystallized and their crystal structures were determined. The proteins have a very similar overall fold with characteristic compact, mainly α-helical structures. The C-terminal sequence of Act c 10.0101 was updated based on our structural and mass spectrometry analysis. Information on proteins’ sequences and structures was used to estimate the risk of cross-reactive reactions between Act c 10.0101 or Pun g 1.0101 and other allergens from this family of proteins. (4) Conclusions: Structural studies indicate a conformational flexibility of allergens from the nsLTP family and suggest that immunoglobulin E binding to some surface regions of these allergens may depend on ligand binding. Both Act c 10.0101 and Pun g 1.0101 are likely to be involved in cross-reactive reactions involving other proteins from the nsLTP family.

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