Bacterial Immobilization and Toxicity Induced by a Bean Plant Immune System

Author(s):  
Bret Cooper ◽  
Hunter S. Beard ◽  
Ronghui Yang ◽  
Wesley M. Garrett ◽  
Kimberly B. Campbell
Science ◽  
2013 ◽  
Vol 341 (6147) ◽  
pp. 746-751 ◽  
Author(s):  
Jeffery L. Dangl ◽  
Diana M. Horvath ◽  
Brian J. Staskawicz

Diverse and rapidly evolving pathogens cause plant diseases and epidemics that threaten crop yield and food security around the world. Research over the last 25 years has led to an increasingly clear conceptual understanding of the molecular components of the plant immune system. Combined with ever-cheaper DNA-sequencing technology and the rich diversity of germ plasm manipulated for over a century by plant breeders, we now have the means to begin development of durable (long-lasting) disease resistance beyond the limits imposed by conventional breeding and in a manner that will replace costly and unsustainable chemical controls.


2021 ◽  
Author(s):  
Florent Delplace ◽  
Carine Huard‐Chauveau ◽  
Richard Berthomé ◽  
Dominique Roby

2006 ◽  
Vol 22 (12) ◽  
pp. 662-670 ◽  
Author(s):  
P TIFFIN ◽  
D MOELLER

2013 ◽  
Vol 14 (3) ◽  
pp. 155-155
Author(s):  
Mary Muers

Insects ◽  
2020 ◽  
Vol 11 (9) ◽  
pp. 582
Author(s):  
Jinghua Zhu ◽  
Kunmiao Zhu ◽  
Liang Li ◽  
Zengxin Li ◽  
Weiwei Qin ◽  
...  

Honeydew is a watery fluid excreted by plant sap-feeding insects. It is a waste product for the insect hosts. However, it plays important roles for other organisms, such as serving as a nutritional source for beneficial insects and bacteria, as well as elicitors and effectors modulating plant responses. In this study, shotgun LC–MS/MS analyses were used to identify the proteins in the honeydew from two important rice hemipteran pests, the brown planthopper (Nilaparvata lugens, BPH) and green rice leafhopper (Nephotettix cincticeps, GRH). A total of 277 and 210 proteins annotated to insect proteins were identified in the BPH and GRH honeydews, respectively. These included saliva proteins that may have similar functions as the saliva proteins, such as calcium-binding proteins and apolipophorin, involved in rice plant defenses. Additionally, a total of 52 and 32 Oryza proteins were identified in the BPH and GRH honeydews, respectively, some of which are involved in the plant immune system, such as Pathogen-Related Protein 10, ascorbate peroxidase, thioredoxin and glutaredoxin. Coincidently, 570 and 494 bacteria proteins were identified from the BPH and GRH honeydews, respectively, which included several well-known proteins involved in the plant immune system: elongation factor Tu, flagellin, GroEL and cold-shock proteins. The results of our study indicate that the insect honeydew is a complex fluid cocktail that contains abundant proteins from insects, plants and microbes, which may be involved in the multitrophic interactions of plants–insects–microbes.


2011 ◽  
Vol 286 (41) ◽  
pp. 35834-35842 ◽  
Author(s):  
Laurence S. Boutemy ◽  
Stuart R. F. King ◽  
Joe Win ◽  
Richard K. Hughes ◽  
Thomas A. Clarke ◽  
...  

Phytopathogens deliver effector proteins inside host plant cells to promote infection. These proteins can also be sensed by the plant immune system, leading to restriction of pathogen growth. Effector genes can display signatures of positive selection and rapid evolution, presumably a consequence of their co-evolutionary arms race with plants. The molecular mechanisms underlying how effectors evolve to gain new virulence functions and/or evade the plant immune system are poorly understood. Here, we report the crystal structures of the effector domains from two oomycete RXLR proteins, Phytophthora capsici AVR3a11 and Phytophthora infestans PexRD2. Despite sharing <20% sequence identity in their effector domains, they display a conserved core α-helical fold. Bioinformatic analyses suggest that the core fold occurs in ∼44% of annotated Phytophthora RXLR effectors, both as a single domain and in tandem repeats of up to 11 units. Functionally important and polymorphic residues map to the surface of the structures, and PexRD2, but not AVR3a11, oligomerizes in planta. We conclude that the core α-helical fold enables functional adaptation of these fast evolving effectors through (i) insertion/deletions in loop regions between α-helices, (ii) extensions to the N and C termini, (iii) amino acid replacements in surface residues, (iv) tandem domain duplications, and (v) oligomerization. We hypothesize that the molecular stability provided by this core fold, combined with considerable potential for plasticity, underlies the evolution of effectors that maintain their virulence activities while evading recognition by the plant immune system.


2017 ◽  
Vol 8 ◽  
Author(s):  
Yi Zhang ◽  
Yuhan Gao ◽  
Yingbo Liang ◽  
Yijie Dong ◽  
Xiufen Yang ◽  
...  

Science ◽  
2011 ◽  
Vol 333 (6042) ◽  
pp. 596-601 ◽  
Author(s):  
M. S. Mukhtar ◽  
A.-R. Carvunis ◽  
M. Dreze ◽  
P. Epple ◽  
J. Steinbrenner ◽  
...  

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