Host inhibition of a bacterial virulence effector triggers immunity to infection

Vardis Ntoukakis; Tatiana S. Mucyn; Selena Gimenez-Ibanez; Helen C. Chapman; Jose R. Gutierrez; Alexi L. Balmuth; Alexandra M.E. Jones; John P. Rathjen

doi:10.1126/science.1169430

Host inhibition of a bacterial virulence effector triggers immunity to infection

Vardis Ntoukakis, Tatiana S. Mucyn, Selena Gimenez-Ibanez, Helen C. Chapman, Jose R. Gutierrez, Alexi L. Balmuth, Alexandra M.E. Jones, John P. Rathjen

Research output: Contribution to journal › Article › peer-review

101 Citations (Scopus)

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.

Original language	English
Pages (from-to)	784-787
Number of pages	4
Journal	Science
Volume	324
Issue number	5928
DOIs	https://doi.org/10.1126/science.1169430
Publication status	Published - 8 May 2009
Externally published	Yes

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title = "Host inhibition of a bacterial virulence effector triggers immunity to infection",

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.",

author = "Vardis Ntoukakis and Mucyn, {Tatiana S.} and Selena Gimenez-Ibanez and Chapman, {Helen C.} and Gutierrez, {Jose R.} and Balmuth, {Alexi L.} and Jones, {Alexandra M.E.} and Rathjen, {John P.}",

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AU - Ntoukakis, Vardis

AU - Mucyn, Tatiana S.

AU - Gimenez-Ibanez, Selena

AU - Chapman, Helen C.

AU - Gutierrez, Jose R.

AU - Balmuth, Alexi L.

AU - Jones, Alexandra M.E.

AU - Rathjen, John P.

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AB - 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.

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Host inhibition of a bacterial virulence effector triggers immunity to infection

Abstract

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