The bacterial type III-secreted protein AvrRps4 is a bipartite effector.

Bacterial effector proteins secreted into host plant cells manipulate those cells to the benefit of the pathogen, but effector-triggered immunity (ETI) occurs when effectors are recognized by host resistance proteins. The RPS4/RRS1 pair recognizes the Pseudomonas syringae pv. pisi effector AvrRps4....

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Main Authors: Morgan K Halane, Sang Hee Kim, Benjamin J Spears, Christopher M Garner, Conner J Rogan, Elizabeth C Okafor, Jianbin Su, Saikat Bhattacharjee, Walter Gassmann
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2018-03-01
Series:PLoS Pathogens
Online Access:http://europepmc.org/articles/PMC5895054?pdf=render
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spelling doaj-7cad1d34fc87405d9a35a6ac39603cbe2020-11-25T02:02:15ZengPublic Library of Science (PLoS)PLoS Pathogens1553-73661553-73742018-03-01143e100698410.1371/journal.ppat.1006984The bacterial type III-secreted protein AvrRps4 is a bipartite effector.Morgan K HalaneSang Hee KimBenjamin J SpearsChristopher M GarnerConner J RoganElizabeth C OkaforJianbin SuSaikat BhattacharjeeWalter GassmannBacterial effector proteins secreted into host plant cells manipulate those cells to the benefit of the pathogen, but effector-triggered immunity (ETI) occurs when effectors are recognized by host resistance proteins. The RPS4/RRS1 pair recognizes the Pseudomonas syringae pv. pisi effector AvrRps4. AvrRps4 is processed in planta into AvrRps4N (133 amino acids), homologous to the N-termini of other effectors including the native P. syringae pv. tomato strain DC3000 effector HopK1, and AvrRps4C (88 amino acids). Previous data suggested that AvrRps4C alone is necessary and sufficient for resistance when overexpressed in heterologous systems. We show that delivering AvrRps4C from DC3000, but not from a DC3000 hopK1- strain, triggers resistance in the Arabidopsis accession Col-0. Delivering AvrRps4C in tandem with AvrRps4N, or as a chimera with HopK1N, fully complements AvrRps4-triggered immunity. AvrRps4N in the absence of AvrRps4C enhances virulence in Col-0. In addition, AvrRps4N triggers a hypersensitive response in lettuce that is attenuated by coexpression of AvrRps4C, further supporting the role of AvrRps4N as a bona fide effector domain. Based on these results we propose that evolutionarily, fusion of AvrRps4C to AvrRps4N may have counteracted recognition of AvrRps4N, and that the plant RPS4/RRS1 resistance gene pair was selected as a countermeasure. We conclude that AvrRps4 represents an unusual chimeric effector, with recognition in Arabidopsis by RPS4/RRS1 requiring the presence of both processed effector moieties.http://europepmc.org/articles/PMC5895054?pdf=render
collection DOAJ
language English
format Article
sources DOAJ
author Morgan K Halane
Sang Hee Kim
Benjamin J Spears
Christopher M Garner
Conner J Rogan
Elizabeth C Okafor
Jianbin Su
Saikat Bhattacharjee
Walter Gassmann
spellingShingle Morgan K Halane
Sang Hee Kim
Benjamin J Spears
Christopher M Garner
Conner J Rogan
Elizabeth C Okafor
Jianbin Su
Saikat Bhattacharjee
Walter Gassmann
The bacterial type III-secreted protein AvrRps4 is a bipartite effector.
PLoS Pathogens
author_facet Morgan K Halane
Sang Hee Kim
Benjamin J Spears
Christopher M Garner
Conner J Rogan
Elizabeth C Okafor
Jianbin Su
Saikat Bhattacharjee
Walter Gassmann
author_sort Morgan K Halane
title The bacterial type III-secreted protein AvrRps4 is a bipartite effector.
title_short The bacterial type III-secreted protein AvrRps4 is a bipartite effector.
title_full The bacterial type III-secreted protein AvrRps4 is a bipartite effector.
title_fullStr The bacterial type III-secreted protein AvrRps4 is a bipartite effector.
title_full_unstemmed The bacterial type III-secreted protein AvrRps4 is a bipartite effector.
title_sort bacterial type iii-secreted protein avrrps4 is a bipartite effector.
publisher Public Library of Science (PLoS)
series PLoS Pathogens
issn 1553-7366
1553-7374
publishDate 2018-03-01
description Bacterial effector proteins secreted into host plant cells manipulate those cells to the benefit of the pathogen, but effector-triggered immunity (ETI) occurs when effectors are recognized by host resistance proteins. The RPS4/RRS1 pair recognizes the Pseudomonas syringae pv. pisi effector AvrRps4. AvrRps4 is processed in planta into AvrRps4N (133 amino acids), homologous to the N-termini of other effectors including the native P. syringae pv. tomato strain DC3000 effector HopK1, and AvrRps4C (88 amino acids). Previous data suggested that AvrRps4C alone is necessary and sufficient for resistance when overexpressed in heterologous systems. We show that delivering AvrRps4C from DC3000, but not from a DC3000 hopK1- strain, triggers resistance in the Arabidopsis accession Col-0. Delivering AvrRps4C in tandem with AvrRps4N, or as a chimera with HopK1N, fully complements AvrRps4-triggered immunity. AvrRps4N in the absence of AvrRps4C enhances virulence in Col-0. In addition, AvrRps4N triggers a hypersensitive response in lettuce that is attenuated by coexpression of AvrRps4C, further supporting the role of AvrRps4N as a bona fide effector domain. Based on these results we propose that evolutionarily, fusion of AvrRps4C to AvrRps4N may have counteracted recognition of AvrRps4N, and that the plant RPS4/RRS1 resistance gene pair was selected as a countermeasure. We conclude that AvrRps4 represents an unusual chimeric effector, with recognition in Arabidopsis by RPS4/RRS1 requiring the presence of both processed effector moieties.
url http://europepmc.org/articles/PMC5895054?pdf=render
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