ArticleFrontiers in plant science2011
At the Frontier; RXLR Effectors Crossing the Phytophthora-Host Interface.
Article in Frontiers in plant science, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 20 citations in OpenAlex.
- Delivered complementation in planta (DCIP) enables measurement of peptide-mediated protein delivery efficiency in plants.Communications biology · 2023Article
- The broad host range pathogen Sclerotinia sclerotiorum produces multiple effector proteins that induce host cell death intracellularly.Molecular plant pathology · 2023Article
- Multiple Mechanisms Drive the Evolutionary Adaptation ofJournal of fungi (Basel, Switzerland) · 2021Article
- Oomycetes Used in Arabidopsis Research.The arabidopsis book · 2019Article
- Arms race: diverse effector proteins with conserved motifs.Plant signaling & behavior · 2019Article
- The Cell Death Triggered by the Nuclear Localized RxLR Effector PITG_22798 from Phytophthora infestans Is Suppressed by the Effector AVR3b.International journal of molecular sciences · 2017Article
- Enhancing crop innate immunity: new promising trends.Frontiers in plant science · 2014Review
- De novo transcriptome sequencing and analysis for Venturia inaequalis, the devastating apple scab pathogen.PloS one · 2013Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Plants are constantly beset by pathogenic organisms. To successfully infect their hosts, plant pathogens secrete effector proteins, many of which are translocated to the inside of the host cell where they manipulate normal physiological processes and undermine host defense. The way by which effectors cross the frontier to reach the inside of the host cell varies among different classes of pathogens. For oomycete plant pathogens - like the potato late blight pathogen Phytophthora infestans - it has been shown that effector translocation to the host cell cytoplasm is dependent on conserved amino acid motifs that are present in the N-terminal part of effector proteins. One of these motifs, known as the RXLR motif, has a strong resemblance with a host translocation motif found in effectors secreted by Plasmodium species. These malaria parasites, that reside inside specialized vacuoles in red blood cells, make use of a specific protein translocation complex to export effectors from the vacuole into the red blood cell. Whether or not also oomycete RXLR effectors require a translocation complex to cross the frontier is still under investigation. For one P. infestans RXLR effector named IPI-O we have found a potential host target that could play a role in establishing the first contact between this effector and the host cell. This membrane spanning lectin receptor kinase, LecRK-I.9, interacts with IPI-O via the tripeptide RGD that overlaps with the RXLR motif. In animals, RGD is a well-known cell adhesion motif; it binds to integrins, which are membrane receptors that regulate many cellular processes and which can be hijacked by pathogens for either effector translocation or pathogen entry into host cells.
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