The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
A Bacterial Virulence Protein Suppresses Host Innate Immunity to Cause Plant Disease
Abstract
Plants have evolved a powerful immune system to defend against infection by most microbial organisms. However, successful pathogens, such as Pseudomonas syringae , have developed countermeasures and inject virulence proteins into the host plant cell to suppress immunity and cause devastating diseases. Despite intensive research efforts, the molecular targets of bacterial virulence proteins that are important for plant disease development have remained obscure. Here, we show that a conserved P. syringae virulence protein, HopM1, targets an immunity-associated protein, AtMIN7, in Arabidopsis thaliana . HopM1 mediates the destruction of AtMIN7 via the host proteasome. Our results illustrate a strategy by which a bacterial pathogen exploits the host proteasome to subvert host immunity and causes infection in plants.
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Citations
Cites
Host-Microbe Interactions: Shaping the Evolution of the Plant Immune Response
Chisholm, S. T., Coaker, G., Day, B., & Staskawicz, B. J. (2006) · Cell · doi:10.1016/j.cell.2006.02.008 · Cited by 2,957
Cited by
Jones, J. D. G., & Dangl, J. L. (2006) · Nature · doi:10.1038/nature05286 · Cited by 13,177
Self-citationIntervention of Phytohormone Pathways by Pathogen Effectors
Kazan, K., & Lyons, R. (2014) · The Plant Cell · doi:10.1105/tpc.114.125419 · Cited by 488
(2024) · doi:10.1126/sciadv.ado9516 · Cited by 19
Zheng, S., Noack, L. C., Khammy, O., De Meyer, A., Khan, G. A., De Winne, N., Eeckhout, D., Van Damme, D., & Persson, S. (2025) · Nature Communications · doi:10.1038/s41467-025-56192-3 · Cited by 18
Metadata
- Authors
- Nomura, K., DebRoy, S., Lee, Y. H., Pumplin, N., Jones, J., & He, S. Y.
- Venue
- Science
- Published
- 2006-07-14
- Volume
- 313
- Issue
- 5784
- Pages
- 220-223
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1981620052
- Cited by
- 494
- References
- 1
- FWCI
- 41.82
- Type
- journal article
- Language
- en
- Open access
- closed
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