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Host inhibition of a bacterial virulence effector triggers immunity to infection
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Ntoukakis, Vardis, Mucyn, T. S., Gimenez-Ibanez, S., Chapman, H. C., Gutierrez, J. R., Balmuth, Alexi L., Jones, Alexandra M. and Rathjen, J. P. (2009) Host inhibition of a bacterial virulence effector triggers immunity to infection. Science, Volume 324 (Number 5928). pp. 784-787. doi:10.1126/science.1169430 ISSN 0036-8075.
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Official URL: http://dx.doi.org/10.1126/science.1169430
Abstract
Plant pathogenic bacteria secrete effector proteins that attack the host signaling machinery to suppress immunity. Effectors can be recognized by hosts leading to immunity. One such effector is AvrPtoB of Pseudomonas syringae, which degrades host protein kinases, such as tomato Fen, through an E3 ligase domain. Pto kinase, which is highly related to Fen, recognizes AvrPtoB in conjunction with the resistance protein Prf. Here we show that Pto is resistant to AvrPtoB-mediated degradation because it inactivates the E3 ligase domain. AvrPtoB ubiquitinated Fen within the catalytic cleft, leading to its breakdown and loss of the associated Prf protein. Pto avoids this by phosphorylating and inactivating the AvrPtoB E3 domain. Thus, inactivation of a pathogen virulence molecule is one mechanism by which plants resist disease.
Item Type: | Journal Article | ||||
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Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) | ||||
Journal or Publication Title: | Science | ||||
Publisher: | American Association for the Advancement of Science | ||||
ISSN: | 0036-8075 | ||||
Official Date: | 8 May 2009 | ||||
Dates: |
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Volume: | Volume 324 | ||||
Number: | Number 5928 | ||||
Page Range: | pp. 784-787 | ||||
DOI: | 10.1126/science.1169430 | ||||
Status: | Peer Reviewed | ||||
Publication Status: | Published | ||||
Access rights to Published version: | Restricted or Subscription Access |
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