Cited by 329Plant-Microbe Interactions and ImmunityImmune Response and InflammationPlant Virus Research Studies

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A Novel Role for the TIR Domain in Association with Pathogen-Derived Elicitors

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Burch-Smith, Tessa M, Schiff, Michael, Caplan, Jeffrey L, Tsao, Jeffrey, Czymmek, Kirk, Dinesh-Kumar, Savithramma P·2007·PLoS Biology

Abstract

Plant innate immunity is mediated by Resistance (R) proteins, which bear a striking resemblance to animal molecules of similar function. Tobacco N is a TIR-NB-LRR R gene that confers resistance to Tobacco mosaic virus, specifically the p50 helicase domain. An intriguing question is how plant R proteins recognize the presence of pathogen-derived Avirulence (Avr) elicitor proteins. We have used biochemical cell fraction and immunoprecipitation in addition to confocal fluorescence microscopy of living tissue to examine the association between N and p50. Surprisingly, both N and p50 are cytoplasmic and nuclear proteins, and N's nuclear localization is required for its function. We also demonstrate an in planta association between N and p50. Further, we show that N's TIR domain is critical for this association, and indeed, it alone can associate with p50. Our results differ from current models for plant innate immunity that propose detection is mediated solely through the LRR domains of these molecules. The data we present support an intricate process of pathogen elicitor recognition by R proteins involving multiple subcellular compartments and the formation of multiple protein complexes.

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Crossref · 10.1371/journal.pbio.0050068

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  • TIR-like proteins, among which are Toll receptors, are major regulators of phagocytosis and pathogen-response in animals.

    “TIR-like proteins, among which are Toll receptors, are major regulators of phagocytosis and pathogen-response in animals [54,66-68].”

    From Genome-wide transcriptional changes induced by phagocytosis or growth on bacteria in Dictyostelium (2008) · cites this paper as [66]

    The Introduction identifies Toll and Toll-like receptors as TIR-domain proteins involved in animal innate immunity and says mammalian TLRs recognize pathogen-associated molecular patterns. It does not address phagocytosis, so that part of the attributed claim is unsupported. The passages provided do not give page numbers. (LLM, conf=0.84)

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  • Intracellular effectors with TIR-like domains have been recently shown to enter the nucleus and to regulate immune-like response in plants, acting on WRKY transcription factors, which negatively regulate such response.

    “Interestingly, intracellular effectors with TIR-like domains have been recently shown to enter the nucleus and to regulate immune-like response in plants, acting on WRKY transcription factors, which negatively regulate such response [54,66,68].”

    From Genome-wide transcriptional changes induced by phagocytosis or growth on bacteria in Dictyostelium (2008) · cites this paper as [66]

    The Results and Discussion (page unavailable) show that the TIR-containing tobacco resistance protein N localizes to the nucleus and that its nuclear localization is required for a defense response. The Discussion mentions a WRKY DNA-binding domain in another resistance protein, but does not show N acting on WRKY transcription factors or establish that they negatively regulate the response. It also identifies N as a plant resistance protein, not an intracellular pathogen effector. (LLM, conf=0.88)

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Metadata

Authors
Burch-Smith, T. M., Schiff, M., Caplan, J. L., Tsao, J., Czymmek, K., & Dinesh-Kumar, S. P.
Affiliations
  • Yale University (US)
  • Delaware Biotechnology Institute (US)
Venue
PLoS Biology
Published
2007-02-13
Volume
5
Issue
3
Pages
e68
ISSN
  • 1544-9173 (ISSN-L)
  • 1545-7885
OpenAlex
W2089370030
Cited by
329
References
0
Citations by year
2026: 4 · 2025: 4 · 2024: 19 · 2023: 6 · 2022: 10 · 2021: 17 · 2020: 8 · 2019: 11 · 2018: 8 · 2017: 18 · 2016: 13 · 2015: 15 · 2014: 17 · 2013: 39 · 2012: 18
FWCI
41.72
Type
journal article
Language
en
Open access
Locations
  • PLoS Biology (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
  • eScholarship (California Digital Library) (submittedVersion)
  • eScholarship (California Digital Library) (submittedVersion, cc-by)
  • Figshare (submittedVersion, cc-by)
Funders
  • National Institutes of Health
  • National Institute of General Medical Sciences (GM62625, R01GM062625)
Topics
  • Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant-Microbe Interactions and Immunity
  • Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
  • Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Virus Research Studies
Keywords
TIR domain, tobacco mosaic virus, plant innate immunity, protein-protein interaction, nuclear localization, subcellular localization, protein complexes
MeSH terms
Amino Acid Sequence, Immunity, Innate, Plant Proteins, Plants, Tobacco Mosaic Virus, Virulence, Polymerase Chain Reaction

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