English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Plant pathology has entered the era where it seems possible to understand the basis of pathogenicity in molecular terms. The key has been the identification of the role of pathogen effectors, proteins secreted at infection sites, some of which enter host cells to dampen host immunity and modify metabolism to pathogens’ advantage. Knowledge of how effectors function and how their contributions to plant disease can be blocked promises ways of controlling crop diseases (1). Fungal and oomycete pathogens (filamentous eukaryotic microbes) that are the major pathogens of rice, corn, wheat, soybeans, and potatoes, the big 5 crops feeding the world, secrete effectors that enter plant cells to reach their site of action. How do effectors cross the host membrane, and what is their function inside of host cells? Studies with the effectors Avirulence protein 3a (AVR3a) from Phytophthora infestans and Avirulence protein 1b (AVR1b) from P. sojae, pathogens of potato and soybean, respectively, have provided important insights. Both effectors carry an uptake signal motif with consensus sequence arginine, any amino acid, leucine, arginine (RXLR) that is common to a large repertoire of oomycete effectors and located near each protein's N terminus, which directs effector uptake by plants (2, 3). However, the identification of this signal did not reveal the mechanism of effector uptake by host cells. In the work by Kale et al. (4), data were presented indicating that the RXLR domain mediates binding of AVR1b to phosphatidyl inositol phosphates (PIPs). The experimental evidence for this hypothesis was …

Showdown at the RXLR motif: Serious differences of opinion in how effector proteins from filamentous eukaryotic pathogens enter plant cells