CoChat
Sign Up
PreprintCited by 4Plant Pathogenic Bacteria StudiesPlant-Microbe Interactions and ImmunityRNA and protein synthesis mechanisms

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Bacteria use processing body condensates to attenuate host translation during infection

Open access
González-Fuente, Manuel, Schulz, Nico, Abdrakhmanov, Alibek, Izzati, Gaiea, Zhu, Shanshuo, Langin, Gautier, Gouguet, Paul, Franz-Wachtel, Mirita, Macek, Boris, Hafrén, Anders, Dagdas, Yasin, Üstün, Suayib·2025·Science Advances
DOI 10.1101/2025.01.09.632196PMC PMC13108548

Preprint — published as 10.1126/sciadv.aec4477

Open this paper in CoChat — free account

Abstract

Pathogens employ sophisticated strategies to modulate host protein homeostasis by targeting proteolytic pathways, but their impact on protein synthesis remains elusive. We report that pathogenic bacteria Pseudomonas syringae ( Pst ) targets ribonucleoprotein condensates, known as processing bodies (P-bodies), to attenuate host translation through two effectors with liquid-like properties. We uncovered a previously unknown link that Pst -mediated repression of the ER stress response is required for P-body assembly. Furthermore, we identify a novel intersection between P-bodies and autophagy, demonstrating that autophagic clearance of P-bodies is crucial for maintaining the balance between translationally active and inactive mRNAs. Altogether, our discoveries provide novel insights on how host translation is attenuated by bacteria to dampen plant immunity and uncover unknown connections between ER stress responses and autophagy with P-body dynamics.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1101/2025.01.09.632196

Cites

1 of 1 references verified0 citation errors · 0 not checkable

Statistics

Figures

Fig. 1. P. syringae induces P-body formation in an effector-dependent manner. (A to C) Confocal microscopy pictures of A. thaliana leaves expressing P-body markers DCP1-GFP [(A) to (C)] and DCP5-GFP (B) infected with indicated Pst strains or mock at different time points (A) or 24 hours [(B) and (C)]. Accompanying boxplots represent the number of fluorescent foci present per focal plane from at least two independent experiments. Scale bars, 50 μm. Different letters indicate statistical groups determined using one-way analysis of variance (ANOVA) test (P < 0.05). (D) Coimmunoprecipitation of YFP-DCP1, DCP5-GFP, or GFP with HA-tagged HopM1 and YFP-HopN1 or GFP with HA-DCP1 or DCP5 transiently expressed in N. benthamiana. GFP blot was split for visualization purposes. Asterisks indicate HA-tagged HopM1 and DCP5. IP, immunoprecipitation. (E) Confocal microscopy of transiently coexpressed YFP N-terminal fragment (nYFP)–tagged DCP1 and DCP5 with YFP C-terminal fragment (cYFP)–tagged HopM1 and HopN1 in N. benthamiana. Scale bars, 50 μm. (F) Confocal microscopy pictures of transiently coexpressed nYFP-tagged DCP1 and DCP5 with cYFP-tagged HopM1 and HopN1 and RFP-XRN4 in N. benthamiana epidermal cells. White arrows indicate colocalization of YFP and RFP signals. Scale bars, 50 μm. (G) Confocal microscopy pictures of transiently coexpressed YFP-DCP1 with HopM1-RFP or YFP-HopN1 with RFP-DCP5 in N. benthamiana. White arrows indicate colocalization of YFP and RFP signals. Scale bars, 25 μm. (H) Representative confocal microscopy images and time-course plot of the fluorescence signal recovery of HopM1-RFP (left) and YFP-HopN1 (right) foci after photobleaching. Recovery was quantified as the percentage of fluorescence intensity compared to before photobleaching. The data represented are the means, and error bars represent the standard error of the mean (n > 10). Scale bars, 5 μm. (I) Confocal microscopy time frames of HopM1-RFP and YFP-DCP1 foci fusing when transiently expressed in N. benthamiana. Scale bars, 5 μm.
Fig. 1. P. syringae induces P-body formation in an effector-dependent manner. (A to C) Confocal microscopy pictures of A. thaliana leaves expressing P-body markers DCP1-GFP [(A) to (C)] and DCP5-GFP (B) infected with indicated Pst strains or mock at different time points (A) or 24 hours [(B) and (C)]. Accompanying boxplots represent the number of fluorescent foci present per focal plane from at least two independent experiments. Scale bars, 50 μm. Different letters indicate statistical groups determined using one-way analysis of variance (ANOVA) test (P < 0.05). (D) Coimmunoprecipitation of YFP-DCP1, DCP5-GFP, or GFP with HA-tagged HopM1 and YFP-HopN1 or GFP with HA-DCP1 or DCP5 transiently expressed in N. benthamiana. GFP blot was split for visualization purposes. Asterisks indicate HA-tagged HopM1 and DCP5. IP, immunoprecipitation. (E) Confocal microscopy of transiently coexpressed YFP N-terminal fragment (nYFP)–tagged DCP1 and DCP5 with YFP C-terminal fragment (cYFP)–tagged HopM1 and HopN1 in N. benthamiana. Scale bars, 50 μm. (F) Confocal microscopy pictures of transiently coexpressed nYFP-tagged DCP1 and DCP5 with cYFP-tagged HopM1 and HopN1 and RFP-XRN4 in N. benthamiana epidermal cells. White arrows indicate colocalization of YFP and RFP signals. Scale bars, 50 μm. (G) Confocal microscopy pictures of transiently coexpressed YFP-DCP1 with HopM1-RFP or YFP-HopN1 with RFP-DCP5 in N. benthamiana. White arrows indicate colocalization of YFP and RFP signals. Scale bars, 25 μm. (H) Representative confocal microscopy images and time-course plot of the fluorescence signal recovery of HopM1-RFP (left) and YFP-HopN1 (right) foci after photobleaching. Recovery was quantified as the percentage of fluorescence intensity compared to before photobleaching. The data represented are the means, and error bars represent the standard error of the mean (n > 10). Scale bars, 5 μm. (I) Confocal microscopy time frames of HopM1-RFP and YFP-DCP1 foci fusing when transiently expressed in N. benthamiana. Scale bars, 5 μm.CC BY-NC · PubMed Central
Fig. 2. P-bodies promote susceptibility through modulation of the ER stress response. (A) Confocal images of epidermal cells from 4-week-old A. thaliana leaves expressing DCP1-GFP in Col-0 or dcp5-1 24 hours after mesophyll infiltration with P. syringae [Pst, 107 colony-forming units (CFU)/ml] or MgCl2 mock. Boxplots show DCP1-GFP foci per focal plane from ≥2 independent experiments. Scale bar, 50 μm. Letters indicate statistically distinct groups (one-way ANOVA, P < 0.05). (B) Bacterial growth in Col-0 and dcp5-1 leaves 3 days after dipping with Pst (107 CFU/ml). Data from three independent experiments (Student’s t test, P < 0.05). (C) Number of differentially expressed genes (DEGs) reflecting treatment effects (Pst versus mock) and genotype effects (dcp5-1 versus Col-0) 24 hours after infiltration. Colors indicate up- (red) and down-regulated (blue) genes (|log2FC| > 1.5, adjusted P < 0.05). (D and E) Heatmaps showing log2 fold changes (log2FCs) of all DEGs (D) or ER stress–related DEGs (E). (F) Immunoblot analysis of ER stress markers BIP1/2 in leaves 24 hours after mock or Pst infiltration. Rubisco (Ponceau S) serves as loading control. Numbers indicate normalized band intensities. (G) Quantification of DCP1-GFP foci in leaves treated with Pst or mock and either TM or dimethyl sulfoxide (DMSO). TM was applied 24 hours before imaging and Pst 8 hours before imaging. Data from two experiments (two-way ANOVA, P < 0.05). (H) Bacterial growth in Col-0, dcp5-1, bzip17/60, and bzip28/60 plants infiltrated with Pst (104 CFU/ml) and TM or DMSO. Bacteria were quantified 3 days postinfection. Data from four experiments (two-way ANOVA, P < 0.05). (I) Immunoblot analysis of BIP1/2 and PDIL1-1 after infection with wild-type or mutant Pst strains. (J and K) Immunoblot analysis of BIP1/2 and RFP-BZIP28 in N. benthamiana leaves transiently expressing RFP-BZIP28 and infected with Pst or treated with TM. (L) Quantification of RFP-BZIP28 nuclear localization. dy denotes the difference in fluorescence intensity between nuclear and cytoplasmic regions, calculated from line intensity profiles. Error bars indicate SEM. Data from two independent experiments. SF, Stain-Free.
Fig. 2. P-bodies promote susceptibility through modulation of the ER stress response. (A) Confocal images of epidermal cells from 4-week-old A. thaliana leaves expressing DCP1-GFP in Col-0 or dcp5-1 24 hours after mesophyll infiltration with P. syringae [Pst, 107 colony-forming units (CFU)/ml] or MgCl2 mock. Boxplots show DCP1-GFP foci per focal plane from ≥2 independent experiments. Scale bar, 50 μm. Letters indicate statistically distinct groups (one-way ANOVA, P < 0.05). (B) Bacterial growth in Col-0 and dcp5-1 leaves 3 days after dipping with Pst (107 CFU/ml). Data from three independent experiments (Student’s t test, P < 0.05). (C) Number of differentially expressed genes (DEGs) reflecting treatment effects (Pst versus mock) and genotype effects (dcp5-1 versus Col-0) 24 hours after infiltration. Colors indicate up- (red) and down-regulated (blue) genes (|log2FC| > 1.5, adjusted P < 0.05). (D and E) Heatmaps showing log2 fold changes (log2FCs) of all DEGs (D) or ER stress–related DEGs (E). (F) Immunoblot analysis of ER stress markers BIP1/2 in leaves 24 hours after mock or Pst infiltration. Rubisco (Ponceau S) serves as loading control. Numbers indicate normalized band intensities. (G) Quantification of DCP1-GFP foci in leaves treated with Pst or mock and either TM or dimethyl sulfoxide (DMSO). TM was applied 24 hours before imaging and Pst 8 hours before imaging. Data from two experiments (two-way ANOVA, P < 0.05). (H) Bacterial growth in Col-0, dcp5-1, bzip17/60, and bzip28/60 plants infiltrated with Pst (104 CFU/ml) and TM or DMSO. Bacteria were quantified 3 days postinfection. Data from four experiments (two-way ANOVA, P < 0.05). (I) Immunoblot analysis of BIP1/2 and PDIL1-1 after infection with wild-type or mutant Pst strains. (J and K) Immunoblot analysis of BIP1/2 and RFP-BZIP28 in N. benthamiana leaves transiently expressing RFP-BZIP28 and infected with Pst or treated with TM. (L) Quantification of RFP-BZIP28 nuclear localization. dy denotes the difference in fluorescence intensity between nuclear and cytoplasmic regions, calculated from line intensity profiles. Error bars indicate SEM. Data from two independent experiments. SF, Stain-Free.CC BY-NC · PubMed Central
Fig. 3. P-bodies are required for Pst-mediated attenuation of translation. (A) Immunoblot analysis of puromycin-labeled peptides in Col-0 and dcp5-1 24 hours after mock or Pst infiltration. Rubisco detected by Stain-Free imaging serves as a loading control. Numbers indicate puromycin signal intensities normalized to loading. (B) Immunoblot analysis of RPS6A phosphorylation at S237 and S240 in Col-0 and dcp5-1 24 hours after mock or Pst infiltration. Rubisco visible through Stain-Free (SF) imaging serves as loading control. Numbers indicate ratios of phospho-RPS6A to total RPS6A. (C and D) Immunoblot analysis of puromycin-labeled peptides in Col-0, dcp5-1 (C), and atg5-1 (D) 24 hours after infiltration with either mock or indicated Pst strains. Rubisco visible through Stain-Free imaging serves as loading control. Numbers indicate puromycin signal intensities normalized to loading. (E) Bacterial population A. thaliana leaves of Col-0 and dcp5-1 plants 3 days after Pst infection with CHX (+) or DMSO (−) treatment. Different letters indicate statistical groups determined using two-way ANOVA test (P < 0.05). (F) Scheme of the isolation of ribosome-enriched fractions and identities of the three sampling fractions: total extract (TOTAL), supernatant after ultracentrifugation (SUPER.) and ribosomal-enriched pellet (RIBO.) (G) Immunoblot analysis of ribosomal proteins RPS6, RPL13, and RPL10, and proteasome subunit RPN10 present in the different fractions extracted from Col-0 and dcp5-1 A. thaliana 24 hours after infiltration with either mock or Pst. Rubisco visible through Stain-Free imaging serves as loading control. (H) Ratio of the enrichment of FLS2, BIK1, EDS1, MPK3, ATG8, and NBR1 transcripts in ribosomal-enriched fraction compared to total extracts in Col-0 or dcp5-1 plants 24 hours after infection with Pst compared to mock. Normalized to PP2A. Error bars depict the standard error of the mean. Data from three independent experiments. Different letters indicate statistical groups determined using Student t test (P < 0.05).
Fig. 3. P-bodies are required for Pst-mediated attenuation of translation. (A) Immunoblot analysis of puromycin-labeled peptides in Col-0 and dcp5-1 24 hours after mock or Pst infiltration. Rubisco detected by Stain-Free imaging serves as a loading control. Numbers indicate puromycin signal intensities normalized to loading. (B) Immunoblot analysis of RPS6A phosphorylation at S237 and S240 in Col-0 and dcp5-1 24 hours after mock or Pst infiltration. Rubisco visible through Stain-Free (SF) imaging serves as loading control. Numbers indicate ratios of phospho-RPS6A to total RPS6A. (C and D) Immunoblot analysis of puromycin-labeled peptides in Col-0, dcp5-1 (C), and atg5-1 (D) 24 hours after infiltration with either mock or indicated Pst strains. Rubisco visible through Stain-Free imaging serves as loading control. Numbers indicate puromycin signal intensities normalized to loading. (E) Bacterial population A. thaliana leaves of Col-0 and dcp5-1 plants 3 days after Pst infection with CHX (+) or DMSO (−) treatment. Different letters indicate statistical groups determined using two-way ANOVA test (P < 0.05). (F) Scheme of the isolation of ribosome-enriched fractions and identities of the three sampling fractions: total extract (TOTAL), supernatant after ultracentrifugation (SUPER.) and ribosomal-enriched pellet (RIBO.) (G) Immunoblot analysis of ribosomal proteins RPS6, RPL13, and RPL10, and proteasome subunit RPN10 present in the different fractions extracted from Col-0 and dcp5-1 A. thaliana 24 hours after infiltration with either mock or Pst. Rubisco visible through Stain-Free imaging serves as loading control. (H) Ratio of the enrichment of FLS2, BIK1, EDS1, MPK3, ATG8, and NBR1 transcripts in ribosomal-enriched fraction compared to total extracts in Col-0 or dcp5-1 plants 24 hours after infection with Pst compared to mock. Normalized to PP2A. Error bars depict the standard error of the mean. Data from three independent experiments. Different letters indicate statistical groups determined using Student t test (P < 0.05).CC BY-NC · PubMed Central
Fig. 4. Pst-induced autophagy modulates P-body dynamics. (A) Confocal microscopy pictures and boxplots representing the number and size of fluorescent foci per plane observed in epidermal cells of A. thaliana leaves expressing YFP-DCP1 in the Col-0 and atg5-1 after infiltration with Pst or mock. Scale bars, 50 μm. Data from two independent experiments. Different letters indicate statistical groups determined using two-way ANOVA test (P < 0.05). (B) Immunoblot analysis of YFP-tagged protein levels in A. thaliana leaves expressing YFP-DCP1 in Col-0 and atg5-1 backgrounds 24 hours after mock or Pst infiltration. Rubisco visible through Stain-Free imaging revelation serves as loading control. Numbers indicate the band intensity of YFP-DCP1 normalized to each sample loading (top) and the ratio of YFP/YFP-DCP1 band intensity (bottom, depicted as “ratio”). (C) Confocal microscopy pictures of A. thaliana leaves expressing YFP-DCP1 and mCherry-ATG8E 24 hours after infiltration with mock or Pst together with concanamycin A (ConA). Scale bars, 5 μM. White arrows highlight colocalization. (D) Volcano plot representing the results of the IP-MS/MS proteome analysis of proteins immunoprecipitating with YFP-DCP1 in atg5-1 compared to Col-0. Highlighted in green are known P-body components, and in purple, autophagy-related proteins. (E) Confocal microscopy pictures of A. thaliana leaves expressing YFP-DCP1 in Col-0 or atg5-1 backgrounds infiltrated with mock or Pst 24 hours before imaging, and vacuum-infiltrated with 20 μM CHX or equivalent water volume 4 hours before imaging. Scale bars, 50 μm. (F) Model for Pst-mediated P-body induction and translational repression: P. syringae delivers HopM1 and HopN1, which interact with DCP1 and DCP5 to promote P-body assembly and suppress translation, facilitating infection. This process requires repression of ER stress responses and activation of autophagy.
Fig. 4. Pst-induced autophagy modulates P-body dynamics. (A) Confocal microscopy pictures and boxplots representing the number and size of fluorescent foci per plane observed in epidermal cells of A. thaliana leaves expressing YFP-DCP1 in the Col-0 and atg5-1 after infiltration with Pst or mock. Scale bars, 50 μm. Data from two independent experiments. Different letters indicate statistical groups determined using two-way ANOVA test (P < 0.05). (B) Immunoblot analysis of YFP-tagged protein levels in A. thaliana leaves expressing YFP-DCP1 in Col-0 and atg5-1 backgrounds 24 hours after mock or Pst infiltration. Rubisco visible through Stain-Free imaging revelation serves as loading control. Numbers indicate the band intensity of YFP-DCP1 normalized to each sample loading (top) and the ratio of YFP/YFP-DCP1 band intensity (bottom, depicted as “ratio”). (C) Confocal microscopy pictures of A. thaliana leaves expressing YFP-DCP1 and mCherry-ATG8E 24 hours after infiltration with mock or Pst together with concanamycin A (ConA). Scale bars, 5 μM. White arrows highlight colocalization. (D) Volcano plot representing the results of the IP-MS/MS proteome analysis of proteins immunoprecipitating with YFP-DCP1 in atg5-1 compared to Col-0. Highlighted in green are known P-body components, and in purple, autophagy-related proteins. (E) Confocal microscopy pictures of A. thaliana leaves expressing YFP-DCP1 in Col-0 or atg5-1 backgrounds infiltrated with mock or Pst 24 hours before imaging, and vacuum-infiltrated with 20 μM CHX or equivalent water volume 4 hours before imaging. Scale bars, 50 μm. (F) Model for Pst-mediated P-body induction and translational repression: P. syringae delivers HopM1 and HopN1, which interact with DCP1 and DCP5 to promote P-body assembly and suppress translation, facilitating infection. This process requires repression of ER stress responses and activation of autophagy.CC BY-NC · PubMed Central

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Research works printed but not linked: 55

  1. 10.1016/j.tplants.2023.01.013 · DOI
  2. 10.1146/annurev-phyto-021622-110443 · DOI
  3. 10.1146/annurev-arplant-060324-094912 · DOI
  4. 10.1146/annurev-arplant-060223-030224 · DOI
  5. 10.1016/j.molcel.2022.10.012 · DOI
  6. 10.1146/annurev-phyto-082718-100026 · DOI
  7. 10.1146/annurev-phyto-121423-041908 · DOI
  8. 10.1104/pp.111.182295 · DOI
  9. 10.1038/nature22371 · DOI
  10. 10.1016/j.cell.2022.06.037 · DOI
  11. 10.1021/acs.biochem.7b01162 · DOI
  12. 10.1104/pp.17.01468 · DOI
  13. 10.1016/j.semcdb.2022.11.008 · DOI
  14. C. L. Riggs , N. Kedersha , P. Ivanov , P. Anderson , Mammalian stress granules and P bodies at a glance. J Cell Sci 133 (2020). · DOI
  15. 10.1016/j.fgb.2011.10.003 · DOI
  16. 10.1016/j.celrep.2019.07.054 · DOI
  17. 10.1111/pce.15344 · DOI
  18. 10.1016/j.cell.2006.02.047 · DOI
  19. 10.1126/science.1082320 · DOI
  20. 2015, Pseudomonas syringae pv, tomato DC3000 Type III Secretion Effector Polymutants Reveal an Interplay between HopAD1 and AvrPtoB. Cell Host Microbe, 17, 752
  21. 10.1104/pp.16.00808 · DOI
  22. 10.1111/j.1462-5822.2012.01749.x · DOI
  23. 10.1038/s44318-024-00090-9 · DOI
  24. 10.1105/tpc.109.070078 · DOI
  25. 10.1038/s44319-024-00344-x · DOI
  26. 10.1104/pp.17.01414 · DOI
  27. J. E. Lee , P. I. Cathey , H. Wu , R. Parker , G. K. Voeltz , Endoplasmic reticulum contact sites regulate the dynamics of membraneless organelles. Science (1979) 367 (2020). · DOI
  28. 10.1016/j.chom.2022.02.006 · DOI
  29. 10.1105/tpc.106.050021 · DOI
  30. 10.1534/genetics.119.302376 · DOI
  31. 10.1094/MPMI-03-18-0062-R · DOI
  32. 10.1038/s41467-025-57231-9 · DOI
  33. 10.1186/s13007-016-0120-z · DOI
  34. 10.1146/annurev-arplant-043014-114648 · DOI
  35. 10.1038/s41586-021-03315-7 · DOI
  36. 10.1105/tpc.17.00815 · DOI
  37. 10.1242/dev.01096 · DOI
  38. 10.1104/pp.105.060673 · DOI · Paper page
  39. 10.1016/S0092-8674(03)00364-7 · DOI
  40. 10.7554/eLife.12248 · DOI
  41. 10.1016/j.it.2024.11.010 · DOI
  42. 10.1101/2024.11.20.624400 · DOI
  43. 10.1371/journal.ppat.1011080 · DOI
  44. Y. Gwon , B. A. Maxwell , R.-M. Kolaitis , P. Zhang , H. J. Kim , J. P. Taylor , Ubiquitination of G3BP1 mediates stress granule disassembly in a context-specific manner. Science (1979) 372 (2021). · DOI
  45. 10.1016/j.cell.2013.05.037 · DOI · Paper page
  46. 10.1093/nar/gkz205 · DOI
  47. 10.1186/s13059-014-0550-8 · DOI · Paper page
  48. 10.1101/2023.12.11.571118 · DOI
  49. 10.1016/j.molp.2024.10.003 · DOI
  50. 10.1038/nmeth.4228 · DOI
  51. 10.1186/s12864-019-5556-x · DOI
  52. J. X. Leong , M. Raffeiner , D. Spinti , G. Langin , M. Franz-Wachtel , A. R. Guzman , J. Kim , P. Pandey , A. E. Minina , B. Macek , A. Hafrén , T. O. Bozkurt , M. B. Mudgett , F. Börnke , D. Hofius , S. Üstün , A bacterial effector counteracts host autophagy by promoting degradation of an autophagy component. EMBO J 41 (2022). · DOI · Paper page
  53. 10.1093/BIOINFORMATICS/BTZ931 · DOI · Paper page
  54. 10.1093/NAR/GKAC1000 · DOI · Paper page
  55. 10.1101/gr.1239303 · DOI · Paper page

Metadata

Authors
González-Fuente, M., Schulz, N., Abdrakhmanov, A., Izzati, G., Zhu, S., Langin, G., Gouguet, P., Franz-Wachtel, M., Macek, B., Hafrén, A., Dagdas, Y., & Üstün, S.
Affiliations
  • Faculty of Biology and Biotechnology, Ruhr-University Bochum; Bochum, 44780, Germany
  • Ruhr University Bochum (DE)
  • University of Vienna (AT)
  • University of Tübingen (DE)
  • Proteome Center Tübingen, Interfaculty Institute for Cell Biology, University of Tübingen; Tübingen, 72076, Germany
  • Swedish University of Agricultural Sciences (SE)
  • Gregor Mendel Institute of Molecular Plant Biology (AT)
ORCID
Venue
Science Advances
Publisher
openRxiv
Published
2025-01-14
Volume
12
Issue
17
Pages
eaec4477-eaec4477
ISSN
2375-2548 (ISSN-L)
DOI
10.1101/2025.01.09.632196
PMC
PMC13108548
OpenAlex
W7155491829
Cited by
4
References
1
Citations by year
2026: 1 · 2025: 3
FWCI
3.70
Type
journal article
Language
en
Open access
Licence
Locations
  • Science Advances (publishedVersion, cc-by-nc)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
  • PubMed Central (publishedVersion, cc-by-nc)
  • PubMed (publishedVersion)
Funders
  • European Commission
  • Deutsche Forschungsgemeinschaft (INST 37/965‐1 FUGG, UE188/2‐1, INST 213/1180-1 FUGG, DFG INST 37/819-1 FUGG, GO 3479/1-1)
  • University of Toronto
  • Université de Strasbourg
  • Vetenskapsrådet (2022-03846)
  • Boehringer Ingelheim Stiftung
  • European Research Council (948996 DIVERSIPHAGY)
Topics
  • Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Pathogenic Bacteria Studies
  • Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant-Microbe Interactions and Immunity
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
Keywords
Pseudomonas syringae, P-bodies, ribonucleoprotein condensates, bacterial effector proteins, endoplasmic reticulum stress response, autophagy, plant immunity, plant-pathogen interaction, mRNA degradation
MeSH terms
Biomolecular Condensates, Autophagy, Plant Diseases, Ribonucleoproteins, RNA, Messenger, Protein Biosynthesis, Arabidopsis, Pseudomonas syringae, Host-Pathogen Interactions, Plant Immunity, Endoplasmic Reticulum Stress

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review