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Phytophthora infestans RXLR Effector AVR1 Interacts with Exocyst Component Sec5 to Manipulate Plant Immunity.

Identifieur interne : 000D97 ( Main/Exploration ); précédent : 000D96; suivant : 000D98

Phytophthora infestans RXLR Effector AVR1 Interacts with Exocyst Component Sec5 to Manipulate Plant Immunity.

Auteurs : Yu Du [Pays-Bas] ; Mohamed H. Mpina [Pays-Bas] ; Paul R J. Birch [Pays-Bas] ; Klaas Bouwmeester [Pays-Bas] ; Francine Govers [Pays-Bas]

Source :

RBID : pubmed:26336092

Descripteurs français

English descriptors

Abstract

Phytophthora infestans secretes numerous RXLR effectors that modulate host defense and thereby pave the way for successful invasion. Here, we show that the RXLR effector AVR1 is a virulence factor that promotes colonization and suppresses callose deposition, a hallmark of basal defense. To identify host targets of AVR1, we performed yeast two-hybrid screens and selected Sec5 as a candidate. Sec5 is a subunit of the exocyst, a protein complex that is involved in vesicle trafficking. AVR1-like (A-L), a close homolog of AVR1, also acts as a virulence factor, but unlike AVR1, A-L does not suppress CRINKLER2 (CRN2)-induced cell death or interact with Sec5. Compared with AVR1, A-L is shorter and lacks the carboxyl-terminal tail, the T-region that is crucial for CRN2-induced cell death suppression and Sec5 interaction. In planta analyses revealed that AVR1 and Sec5 are in close proximity, and coimmunoprecipitation confirmed the interaction. Sec5 is required for secretion of the pathogenesis-related protein PR-1 and callose deposition and also plays a role in CRN2-induced cell death. Our findings show that P. infestans manipulates an exocyst subunit and thereby potentially disturbs vesicle trafficking, a cellular process that is important for basal defense. This is a novel strategy that oomycete pathogens exploit to modulate host defense.

DOI: 10.1104/pp.15.01169
PubMed: 26336092
PubMed Central: PMC4634092


Affiliations:


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Le document en format XML

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<term>Phytophthora infestans (immunology)</term>
<term>Phytophthora infestans (metabolism)</term>
<term>Phytophthora infestans (pathogenicity)</term>
<term>Plant Diseases (immunology)</term>
<term>Plant Diseases (parasitology)</term>
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<term>Plant Leaves (immunology)</term>
<term>Plant Leaves (parasitology)</term>
<term>Plant Proteins (genetics)</term>
<term>Plant Proteins (metabolism)</term>
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<term>Tobacco (immunology)</term>
<term>Tobacco (parasitology)</term>
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<term>Facteurs de virulence (métabolisme)</term>
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<term>Feuilles de plante (parasitologie)</term>
<term>Glucanes (métabolisme)</term>
<term>Immunité des plantes (MeSH)</term>
<term>Interactions hôte-pathogène (MeSH)</term>
<term>Maladies des plantes (immunologie)</term>
<term>Maladies des plantes (parasitologie)</term>
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<term>Phytophthora infestans (immunologie)</term>
<term>Phytophthora infestans (métabolisme)</term>
<term>Phytophthora infestans (pathogénicité)</term>
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<term>Protéines végétales (métabolisme)</term>
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<term>Tabac (parasitologie)</term>
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<term>Maladies des plantes</term>
<term>Phytophthora infestans</term>
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<term>Tobacco</term>
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<term>Phytophthora infestans</term>
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<term>Interactions hôte-pathogène</term>
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<div type="abstract" xml:lang="en">Phytophthora infestans secretes numerous RXLR effectors that modulate host defense and thereby pave the way for successful invasion. Here, we show that the RXLR effector AVR1 is a virulence factor that promotes colonization and suppresses callose deposition, a hallmark of basal defense. To identify host targets of AVR1, we performed yeast two-hybrid screens and selected Sec5 as a candidate. Sec5 is a subunit of the exocyst, a protein complex that is involved in vesicle trafficking. AVR1-like (A-L), a close homolog of AVR1, also acts as a virulence factor, but unlike AVR1, A-L does not suppress CRINKLER2 (CRN2)-induced cell death or interact with Sec5. Compared with AVR1, A-L is shorter and lacks the carboxyl-terminal tail, the T-region that is crucial for CRN2-induced cell death suppression and Sec5 interaction. In planta analyses revealed that AVR1 and Sec5 are in close proximity, and coimmunoprecipitation confirmed the interaction. Sec5 is required for secretion of the pathogenesis-related protein PR-1 and callose deposition and also plays a role in CRN2-induced cell death. Our findings show that P. infestans manipulates an exocyst subunit and thereby potentially disturbs vesicle trafficking, a cellular process that is important for basal defense. This is a novel strategy that oomycete pathogens exploit to modulate host defense. </div>
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