scholarly journals Plant pathogens convergently evolved to counteract redundant nodes of an NLR immune receptor network

PLoS Biology ◽  
2021 ◽  
Vol 19 (8) ◽  
pp. e3001136
Author(s):  
Lida Derevnina ◽  
Mauricio P. Contreras ◽  
Hiroaki Adachi ◽  
Jessica Upson ◽  
Angel Vergara Cruces ◽  
...  
Keyword(s):  
Cell Death ◽  
Membrane Trafficking ◽  
Plant Pathogens ◽  
Nucleotide Binding ◽  
Cyst Nematode ◽  
Binding Domain ◽  
Nucleotide Binding Domain ◽  
Hypersensitive Cell Death ◽  
Immune Receptor ◽  
Pathogen Effectors

In plants, nucleotide-binding domain and leucine-rich repeat (NLR)-containing proteins can form receptor networks to confer hypersensitive cell death and innate immunity. One class of NLRs, known as NLR required for cell death (NRCs), are central nodes in a complex network that protects against multiple pathogens and comprises up to half of the NLRome of solanaceous plants. Given the prevalence of this NLR network, we hypothesised that pathogens convergently evolved to secrete effectors that target NRC activities. To test this, we screened a library of 165 bacterial, oomycete, nematode, and aphid effectors for their capacity to suppress the cell death response triggered by the NRC-dependent disease resistance proteins Prf and Rpi-blb2. Among 5 of the identified suppressors, 1 cyst nematode protein and 1 oomycete protein suppress the activity of autoimmune mutants of NRC2 and NRC3, but not NRC4, indicating that they specifically counteract a subset of NRC proteins independently of their sensor NLR partners. Whereas the cyst nematode effector SPRYSEC15 binds the nucleotide-binding domain of NRC2 and NRC3, the oomycete effector AVRcap1b suppresses the response of these NRCs via the membrane trafficking-associated protein NbTOL9a (Target of Myb 1-like protein 9a). We conclude that plant pathogens have evolved to counteract central nodes of the NRC immune receptor network through different mechanisms. Coevolution with pathogen effectors may have driven NRC diversification into functionally redundant nodes in a massively expanded NLR network.

scholarly journals Plant pathogens convergently evolved to counteract redundant nodes of an NLR immune receptor network

2021 ◽  
Author(s):  
Lida Derevnina ◽  
Mauricio P. Contreras ◽  
Hiroaki Adachi ◽  
Jessica Upson ◽  
Angel Vergara Cruces ◽  
...  
Keyword(s):  
Cell Death ◽  
Membrane Trafficking ◽  
Plant Pathogens ◽  
Nucleotide Binding ◽  
Cyst Nematode ◽  
Binding Domain ◽  
Nucleotide Binding Domain ◽  
Hypersensitive Cell Death ◽  
Immune Receptor ◽  
Pathogen Effectors

ABSTRACTIn plants, NLR (nucleotide-binding domain and leucine-rich repeat-containing) proteins can form receptor networks to confer hypersensitive cell death and innate immunity. One class of NLRs, known as NRCs (NLR required for cell death), are central nodes in a complex network that protects against multiple pathogens and comprises up to half of the NLRome of solanaceous plants. Given the prevalence of this NLR network, we hypothesized that pathogens convergently evolved to secrete effectors that target NRC activities. To test this, we screened a library of 167 bacterial, oomycete, nematode and aphid effectors for their capacity to suppress the cell death response triggered by the NRC-dependent disease resistance proteins Prf and Rpi-blb2. Among five of the identified suppressors, one cyst nematode protein and one oomycete protein suppress the activity of autoimmune mutants of NRC2 and NRC3, but not NRC4, indicating that they specifically counteract a subset of NRC proteins independently of their sensor NLR partners. Whereas the cyst nematode effector SPRYSEC15 binds the nucleotide-binding domain of NRC2 and NRC3, the oomycete effector AVRcap1b suppresses the response of these NRCs via the membrane trafficking-associated protein NbTOL9a (Target of Myb 1-like protein 9a). We conclude that plant pathogens have evolved to counteract central nodes of the NRC immune receptor network through different mechanisms. Coevolution with pathogen effectors may have driven NRC diversification into functionally redundant nodes in a massively expanded NLR network.

scholarly journals Osteoblasts Express NLRP3, a Nucleotide-Binding Domain and Leucine-Rich Repeat Region Containing Receptor Implicated in Bacterially Induced Cell Death

2007 ◽  
Vol 23 (1) ◽  
pp. 30-40 ◽  
Author(s):  
Samuel H McCall ◽  
Mahnaz Sahraei ◽  
Amy B Young ◽  
Charles S Worley ◽  
Joseph A Duncan ◽  
...  
Keyword(s):  
Cell Death ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Leucine Rich Repeat ◽  
Repeat Region ◽  
Nucleotide Binding Domain

Mutations in the nucleotide-binding domain of MutS homologs uncouple cell death from cell survival

DNA Repair ◽  
2004 ◽  
Vol 3 (7) ◽  
pp. 729-742 ◽  
Author(s):  
Karin Drotschmann ◽  
Ryan P. Topping ◽  
Jill E. Clodfelter ◽  
Freddie R. Salsbury
Keyword(s):  
Cell Death ◽  
Cell Survival ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Nucleotide Binding Domain

scholarly journals Inflammasome Components Coordinate Autophagy and Pyroptosis as Macrophage Responses to Infection

mBio ◽  
2013 ◽  
Vol 4 (1) ◽  
Author(s):  
Brenda G. Byrne ◽  
Jean-Francois Dubuisson ◽  
Amrita D. Joshi ◽  
Jenny J. Persson ◽  
Michele S. Swanson
Keyword(s):  
Cell Death ◽  
Legionella Pneumophila ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Mouse Genetics ◽  
Leucine Rich Repeat ◽  
Nucleotide Binding Domain ◽  
Caspase 1 ◽  
Primary Mouse ◽  
Mouse Macrophages

ABSTRACTWhen microbes contaminate the macrophage cytoplasm, leukocytes undergo a proinflammatory death that is initiated by nucleotide-binding-domain-, leucine-rich-repeat-containing proteins (NLR proteins) that bind and activate caspase-1. We report that these inflammasome components also regulate autophagy, a vesicular pathway to eliminate cytosolic debris. In response to infection with flagellateLegionella pneumophila, C57BL/6J mouse macrophages equipped with caspase-1 and the NLR proteins NAIP5 and NLRC4 stimulated autophagosome turnover. A second trigger of inflammasome assembly, K+efflux, also rapidly activated autophagy in macrophages that produced caspase-1. Autophagy protects infected macrophages from pyroptosis, since caspase-1-dependent cell death occurred more frequently when autophagy was dampened pharmacologically by either 3-methyladenine or an inhibitor of the Atg4 protease. Accordingly, in addition to coordinating pyroptosis, both (pro-) caspase-1 protein and NLR components of inflammasomes equip macrophages to recruit autophagy, a disposal pathway that raises the threshold of contaminants necessary to trigger proinflammatory leukocyte death.IMPORTANCEAn exciting development in the innate-immunity field is the recognition that macrophages enlist autophagy to protect their cytoplasm from infection. Nutrient deprivation has long been known to induce autophagy; how infection triggers this disposal pathway is an active area of research. Autophagy is encountered by many of the intracellular pathogens that are known to trigger pyroptosis, an inflammatory cell death initiated when nucleotide-binding-domain-, leucine-rich-repeat-containing proteins (NLR proteins) activate caspase-1 within inflammasome complexes. Therefore, we tested the hypothesis that NLR proteins and caspase-1 also coordinate autophagy as a barrier to cytosolic infection. By exploiting classical bacterial and mouse genetics and kinetic assays of autophagy, we demonstrate for the first time that, when confronted with cytosolic contamination, primary mouse macrophages rely not only on the NLR proteins NAIP5 and NLRC4 but also on (pro-)caspase-1 protein to mount a rapid autophagic response that wards off proinflammatory cell death.

scholarly journals The Tomato Nucleotide-binding Leucine-rich Repeat Immune Receptor I-2 Couples DNA-binding to Nucleotide-binding Domain Nucleotide Exchange

2015 ◽  
Vol 291 (3) ◽  
pp. 1137-1147 ◽  
Author(s):  
Stepan Fenyk ◽  
Christopher H. Dixon ◽  
William H. Gittens ◽  
Philip D. Townsend ◽  
Gary J. Sharples ◽  
...  
Keyword(s):  
Dna Binding ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Leucine Rich Repeat ◽  
Nucleotide Exchange ◽  
Nucleotide Binding Domain ◽  
Immune Receptor

scholarly journals A possible nucleotide-binding domain in the tertiary fold of phosphoribosyltransferases.

1983 ◽  
Vol 258 (10) ◽  
pp. 6450-6457 ◽  
Author(s):  
P Argos ◽  
M Hanei ◽  
J M Wilson ◽  
W N Kelley
Keyword(s):  
Nucleotide Binding ◽  
Binding Domain ◽  
Nucleotide Binding Domain

Mutational Analysis of the Nucleotide Binding Domain of the Mismatch Repair Enzyme hMSH-2

1996 ◽  
Vol 229 (1) ◽  
pp. 147-153 ◽  
Author(s):  
Adrian Whitehouse ◽  
Rekha Parmar ◽  
Jayne Deeble ◽  
Graham R. Taylor ◽  
Simon E.V. Phillips ◽  
...  
Keyword(s):  
Mismatch Repair ◽  
Mutational Analysis ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Nucleotide Binding Domain ◽  
Repair Enzyme
Sign in / Sign up

Export Citation Format

Share Document