External Lipid PI3P Mediates Entry of Eukaryotic Pathogen Effectors into Plant and Animal Host Cells

Kale, Shiv D.; Gu, Bin; Capelluto, Daniel G. S.; Dou, Daolong; Feldman, Emily R.; Rumore, Amanda; Arredondo, Francisco; Hanlon, Regina; Fudal, Isabelle; Rouxel, Thierry; Lawrence, Christopher B.; Shan, Weixing; Tyler, Brett M.

doi:10.1016/j.cell.2010.08.035

Cited by 125 publications

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“…This signal contains an N-terminal RXLR motif which recognizes PI(3)P on the outer plasma membrane of both plant and human cells. 81 Besides the well-known intracellular functions of PI(3)P, PI(3)P was detected on the cell surface of soybean roots and human lung epithelial cells, with the exposure of PI(3)P found to be necessary for Avr1b binding and entry in both cell types 81 (Figure 2e). Furthermore, another effector protein from the same species, Avh5, was found to enter soybean root and human lung epithelial cells via PI(3)P binding, with both the RXLR motif as well as a lysine-rich region shown to be required for cell entry.…”

Section: Pathogenic Entry Via the Host Extracellular Phospholipid Codementioning

confidence: 97%

“…lycopersici) and AvrLm6 (Leptosphaeria maculans) containing the RXLR motif were also shown to bind PI(3)P and facilitate protein entry into soybean root cells. 81 Interestingly, Helicobacter pylori can modify the host phospholipid code by inducing PS exposure on epithelial cells via its bacterial Type IV secretion system upon initial membrane contact. Exposure of PS then facilitates translocation of CagA, a secreted virulence factor that interacts directly with PS via its N-terminal region, into host cells.…”

Section: Pathogenic Entry Via the Host Extracellular Phospholipid Codementioning

confidence: 99%

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The phospholipid code: a key component of dying cell recognition, tumor progression and host–microbe interactions

2015

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A significant effort is made by the cell to maintain certain phospholipids at specific sites. It is well described that proteins involved in intracellular signaling can be targeted to the plasma membrane and organelles through phospholipid-binding domains. Thus, the accumulation of a specific combination of phospholipids, denoted here as the 'phospholipid code', is key in initiating cellular processes. Interestingly, a variety of extracellular proteins and pathogen-derived proteins can also recognize or modify phospholipids to facilitate the recognition of dying cells, tumorigenesis and host-microbe interactions. In this article, we discuss the importance of the phospholipid code in a range of physiological and pathological processes.

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Section: Pathogenic Entry Via the Host Extracellular Phospholipid Codementioning

confidence: 97%

Section: Pathogenic Entry Via the Host Extracellular Phospholipid Codementioning

confidence: 99%

The phospholipid code: a key component of dying cell recognition, tumor progression and host–microbe interactions

2015

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“…GroEL and GUS His-fusion proteins were developed as described in SI Appendix, Materials and Methods. Proteins were expressed and purified using a nickel-NTA column (QIAGEN) as described previously (54). Eluted GroEL protein was further fractionated using anion exchange chromatography by AthenaES (Athena Enzyme Systems Group).…”

Section: Methodsmentioning

confidence: 99%

GroEL from the endosymbiont Buchnera aphidicola betrays the aphid by triggering plant defense

Chaudhary

Atamian

Shen

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

180

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Significance Aphids are sap-feeding plant pests of great agricultural importance. Aphid saliva is known to modulate plant immune responses, but limited information exists about the composition of aphid saliva. By means of mass spectrometry, we identified 105 proteins in the saliva of the potato aphid Macrosiphum euphorbiae . Among these proteins were some originating from the proteobacterium Buchnera aphidicola , which lives endosymbiotically within bacteriocytes in the hemocoel of the aphid. We demonstrate that one of these endosymbiont-derived proteins, the chaperonin GroEL, is recognized by the plant immune surveillance system and activates pattern-triggered immunity. Our findings indicate that the outcome of plant–aphid interactions critically depends on a third element, the aphid endosymbiotic prokaryotic component, which induces plant immunity.

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“…RXLR motifs in oomycete effectors, and RXLR-like motifs in some fungal effectors, have been reported to be required for host-cell translocation and binding to phosphatidylinositol 3-phosphate (PI3P). Based on these findings, Kale et al (15) proposed that oomycete and fungal effector proteins are translocated into the host cytoplasm after binding to PI3P associated with the external face of the cell, in a process that involves lipid raft-mediated endocytosis. However, this view has recently been challenged by reports showing that the C-terminal Significance Fungal and oomycete pathogens cause devastating diseases in crop plants and facilitate infection by delivering effector molecules into the plant cell.…”

mentioning

confidence: 99%

“…Delivery of effectors into host cells by eukaryotic pathogens has been demonstrated in several plant pathogen systems (7-12), and, in some cases, fungal and oomycete host-cell translocation can occur in the absence of the pathogen (7,(12)(13)(14)(15)(16), suggesting that a hostencoded transport machinery is responsible for internalization of the effectors. Conserved short N-terminal motifs such as RXLR and LXLFLAK have been identified in oomycete-effector protein families (17), and they have been shown to be both necessary and sufficient for plant-cell entry (9,16,18).…”

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confidence: 99%

Structures of the flax-rust effector AvrM reveal insights into the molecular basis of plant-cell entry and effector-triggered immunity

Williams

Catanzariti

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

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Fungal and oomycete pathogens cause some of the most devastating diseases in crop plants, and facilitate infection by delivering a large number of effector molecules into the plant cell. AvrM is a secreted effector protein from flax rust (Melampsora lini) that can internalize into plant cells in the absence of the pathogen, binds to phosphoinositides (PIPs), and is recognized directly by the resistance protein M in flax (Linum usitatissimum), resulting in effector-triggered immunity. We determined the crystal structures of two naturally occurring variants of AvrM, AvrM-A and avrM, and both reveal an L-shaped fold consisting of a tandem duplicated four-helix motif, which displays similarity to the WY domain core in oomycete effectors. In the crystals, both AvrM variants form a dimer with an unusual nonglobular shape. Our functional analysis of AvrM reveals that a hydrophobic surface patch conserved between both variants is required for internalization into plant cells, whereas the C-terminal coiled-coil domain mediates interaction with M. AvrM binding to PIPs is dependent on positive surface charges, and mutations that abrogate PIP binding have no significant effect on internalization, suggesting that AvrM binding to PIPs is not essential for transport of AvrM across the plant membrane. The structure of AvrM and the identification of functionally important surface regions advance our understanding of the molecular mechanisms underlying how effectors enter plant cells and how they are detected by the plant immune system. innate immunity | plant cell internalization | plant disease resistance | avirulence protein | lipid binding F ilamentous eukaryotic microbes such as fungi and oomycetes cause devastating diseases in many economically important crop plants, including rice, corn, wheat, soybean, and potato. During infection, oomycetes and biotrophic fungal pathogens establish a physical interaction with their host through specialized feeding structures, known as haustoria, which facilitate secretion of a vast array of effector proteins to overcome plant defenses and promote host colonization (1-3). The effectors are generally highly divergent even among related species, and generally lack similarity to proteins currently available in the databases, making it difficult to predict biological function from sequence alone. Some of the effectors accumulate in the plant intercellular space (apoplast), whereas others are translocated into the host cell. At present, the host targets and virulence mechanisms of fungal and oomycete effectors are poorly understood. A subset of the planttranslocated effectors called avirulence (Avr) proteins are recognized directly or indirectly and with high specificity by plant disease resistance (R) proteins (4-6). This recognition event leads to activation of effector-triggered immunity (ETI), which usually includes rapid localized host cell death at the site of infectiontermed the hypersensitive response (HR)-and results in the plants being immune to pathogen infection.The question of how...

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External Lipid PI3P Mediates Entry of Eukaryotic Pathogen Effectors into Plant and Animal Host Cells

Cited by 125 publications

References 0 publications

The phospholipid code: a key component of dying cell recognition, tumor progression and host–microbe interactions

The phospholipid code: a key component of dying cell recognition, tumor progression and host–microbe interactions

GroEL from the endosymbiont Buchnera aphidicola betrays the aphid by triggering plant defense

Structures of the flax-rust effector AvrM reveal insights into the molecular basis of plant-cell entry and effector-triggered immunity

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