Host Inhibition of a Bacterial Virulence Effector Triggers Immunity to Infection

被引：96

作者：

Ntoukakis, Vardis ^{[1
]}

Mucyn, Tatiana S. ^{[1
]}

Gimenez-lbanez, Selena ^{[1
]}

Chapman, Helen C. ^{[1
]}

Gutierrez, Jose R. ^{[1
]}

Balmuth, Alexi L. ^{[1
]}

Jones, Alexandra M. E. ^{[1
]}

Rathjen, John P. ^{[1
]}

机构：

[1] Sainsbury Lab, Norwich NR4 7UH, Norfolk, England

来源：

SCIENCE | 2009年 / 324卷 / 5928期

关键词：

E3 UBIQUITIN LIGASE; PROGRAMMED CELL-DEATH; SYRINGAE PV. TOMATO; PLANT IMMUNITY; III EFFECTOR; NEGATIVE REGULATION; PROTEIN-KINASE; PTO KINASE; AVRPTOB; PHOSPHORYLATION;

D O I：

10.1126/science.1169430

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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.

引用

页码：784 / 787

页数：4

共 24 条

[1] Type III effector AvrPtoB requires intrinsic E3 ubiquitin ligase activity to suppress plant cell death and immunity [J].