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The C-terminal half of Phytophthora infestans RXLR effector AVR3a is sufficient to trigger R3a-mediated hypersensitivity and suppress INF1-induced cell death in Nicotiana benthamiana.

Identifieur interne : 001F58 ( Main/Exploration ); précédent : 001F57; suivant : 001F59

The C-terminal half of Phytophthora infestans RXLR effector AVR3a is sufficient to trigger R3a-mediated hypersensitivity and suppress INF1-induced cell death in Nicotiana benthamiana.

Auteurs : Jorunn I B. Bos [États-Unis] ; Thirumala-Devi Kanneganti ; Carolyn Young ; Cahid Cakir ; Edgar Huitema ; Joe Win ; Miles R. Armstrong ; Paul R J. Birch ; Sophien Kamoun

Source :

RBID : pubmed:16965554

Descripteurs français

English descriptors

Abstract

The RXLR cytoplasmic effector AVR3a of Phytophthora infestans confers avirulence on potato plants carrying the R3a gene. Two alleles of Avr3a encode secreted proteins that differ in only three amino acid residues, two of which are in the mature protein. Avirulent isolates carry the Avr3a allele, which encodes AVR3aKI (containing amino acids C19, K80 and I103), whereas virulent isolates express only the virulence allele avr3a, encoding AVR3aEM (S19, E80 and M103). Only the AVR3aKI protein is recognized inside the plant cytoplasm where it triggers R3a-mediated hypersensitivity. Similar to other oomycete avirulence proteins, AVR3aKI carries a signal peptide followed by a conserved motif centered on the consensus RXLR sequence that is functionally similar to a host cell-targeting signal of malaria parasites. The interaction between Avr3a and R3a can be reconstructed by their transient co-expression in Nicotiana benthamiana. We exploited the N. benthamiana experimental system to further characterize the Avr3a-R3a interaction. R3a activation by AVR3aKI is dependent on the ubiquitin ligase-associated protein SGT1 and heat-shock protein HSP90. The AVR3aKI and AVR3aEM proteins are equally stable in planta, suggesting that the difference in R3a-mediated death cannot be attributed to AVR3aEM protein instability. AVR3aKI is able to suppress cell death induced by the elicitin INF1 of P. infestans, suggesting a possible virulence function for this protein. Structure-function experiments indicated that the 75-amino acid C-terminal half of AVR3aKI, which excludes the RXLR region, is sufficient for avirulence and suppression functions, consistent with the view that the N-terminal region of AVR3aKI and other RXLR effectors is involved in secretion and targeting but is not required for effector activity. We also found that both polymorphic amino acids, K80 and I103, of mature AVR3a contribute to the effector functions.

DOI: 10.1111/j.1365-313X.2006.02866.x
PubMed: 16965554


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Le document en format XML

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<term>Algal Proteins (chemistry)</term>
<term>Algal Proteins (genetics)</term>
<term>Algal Proteins (physiology)</term>
<term>Alleles (MeSH)</term>
<term>Amino Acid Motifs (MeSH)</term>
<term>Apoptosis (MeSH)</term>
<term>Gene Silencing (MeSH)</term>
<term>HSP90 Heat-Shock Proteins (genetics)</term>
<term>HSP90 Heat-Shock Proteins (metabolism)</term>
<term>Phytophthora (genetics)</term>
<term>Phytophthora (metabolism)</term>
<term>Phytophthora (pathogenicity)</term>
<term>Plant Leaves (anatomy & histology)</term>
<term>Plant Leaves (metabolism)</term>
<term>Plant Leaves (physiology)</term>
<term>Plant Proteins (genetics)</term>
<term>Plant Proteins (metabolism)</term>
<term>Polymorphism, Genetic (MeSH)</term>
<term>Protein Structure, Tertiary (MeSH)</term>
<term>Proteins (MeSH)</term>
<term>Signal Transduction (MeSH)</term>
<term>Structure-Activity Relationship (MeSH)</term>
<term>Tobacco (anatomy & histology)</term>
<term>Tobacco (metabolism)</term>
<term>Tobacco (physiology)</term>
<term>Virulence Factors (genetics)</term>
<term>Virulence Factors (metabolism)</term>
<term>Virulence Factors (physiology)</term>
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<term>Apoptose (MeSH)</term>
<term>Extinction de l'expression des gènes (MeSH)</term>
<term>Facteurs de virulence (génétique)</term>
<term>Facteurs de virulence (métabolisme)</term>
<term>Facteurs de virulence (physiologie)</term>
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<term>Feuilles de plante (métabolisme)</term>
<term>Feuilles de plante (physiologie)</term>
<term>Motifs d'acides aminés (MeSH)</term>
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<term>Phytophthora (métabolisme)</term>
<term>Phytophthora (pathogénicité)</term>
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<term>Protéines d'algue (composition chimique)</term>
<term>Protéines d'algue (génétique)</term>
<term>Protéines d'algue (physiologie)</term>
<term>Protéines du choc thermique HSP90 (génétique)</term>
<term>Protéines du choc thermique HSP90 (métabolisme)</term>
<term>Protéines végétales (génétique)</term>
<term>Protéines végétales (métabolisme)</term>
<term>Relation structure-activité (MeSH)</term>
<term>Structure tertiaire des protéines (MeSH)</term>
<term>Tabac (anatomie et histologie)</term>
<term>Tabac (métabolisme)</term>
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<term>Tobacco</term>
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<term>Protéines d'algue</term>
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<term>Feuilles de plante</term>
<term>Phytophthora</term>
<term>Protéines du choc thermique HSP90</term>
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<term>Amino Acid Motifs</term>
<term>Apoptosis</term>
<term>Gene Silencing</term>
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<term>Apoptose</term>
<term>Extinction de l'expression des gènes</term>
<term>Motifs d'acides aminés</term>
<term>Polymorphisme génétique</term>
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<div type="abstract" xml:lang="en">The RXLR cytoplasmic effector AVR3a of Phytophthora infestans confers avirulence on potato plants carrying the R3a gene. Two alleles of Avr3a encode secreted proteins that differ in only three amino acid residues, two of which are in the mature protein. Avirulent isolates carry the Avr3a allele, which encodes AVR3aKI (containing amino acids C19, K80 and I103), whereas virulent isolates express only the virulence allele avr3a, encoding AVR3aEM (S19, E80 and M103). Only the AVR3aKI protein is recognized inside the plant cytoplasm where it triggers R3a-mediated hypersensitivity. Similar to other oomycete avirulence proteins, AVR3aKI carries a signal peptide followed by a conserved motif centered on the consensus RXLR sequence that is functionally similar to a host cell-targeting signal of malaria parasites. The interaction between Avr3a and R3a can be reconstructed by their transient co-expression in Nicotiana benthamiana. We exploited the N. benthamiana experimental system to further characterize the Avr3a-R3a interaction. R3a activation by AVR3aKI is dependent on the ubiquitin ligase-associated protein SGT1 and heat-shock protein HSP90. The AVR3aKI and AVR3aEM proteins are equally stable in planta, suggesting that the difference in R3a-mediated death cannot be attributed to AVR3aEM protein instability. AVR3aKI is able to suppress cell death induced by the elicitin INF1 of P. infestans, suggesting a possible virulence function for this protein. Structure-function experiments indicated that the 75-amino acid C-terminal half of AVR3aKI, which excludes the RXLR region, is sufficient for avirulence and suppression functions, consistent with the view that the N-terminal region of AVR3aKI and other RXLR effectors is involved in secretion and targeting but is not required for effector activity. We also found that both polymorphic amino acids, K80 and I103, of mature AVR3a contribute to the effector functions.</div>
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<AbstractText>The RXLR cytoplasmic effector AVR3a of Phytophthora infestans confers avirulence on potato plants carrying the R3a gene. Two alleles of Avr3a encode secreted proteins that differ in only three amino acid residues, two of which are in the mature protein. Avirulent isolates carry the Avr3a allele, which encodes AVR3aKI (containing amino acids C19, K80 and I103), whereas virulent isolates express only the virulence allele avr3a, encoding AVR3aEM (S19, E80 and M103). Only the AVR3aKI protein is recognized inside the plant cytoplasm where it triggers R3a-mediated hypersensitivity. Similar to other oomycete avirulence proteins, AVR3aKI carries a signal peptide followed by a conserved motif centered on the consensus RXLR sequence that is functionally similar to a host cell-targeting signal of malaria parasites. The interaction between Avr3a and R3a can be reconstructed by their transient co-expression in Nicotiana benthamiana. We exploited the N. benthamiana experimental system to further characterize the Avr3a-R3a interaction. R3a activation by AVR3aKI is dependent on the ubiquitin ligase-associated protein SGT1 and heat-shock protein HSP90. The AVR3aKI and AVR3aEM proteins are equally stable in planta, suggesting that the difference in R3a-mediated death cannot be attributed to AVR3aEM protein instability. AVR3aKI is able to suppress cell death induced by the elicitin INF1 of P. infestans, suggesting a possible virulence function for this protein. Structure-function experiments indicated that the 75-amino acid C-terminal half of AVR3aKI, which excludes the RXLR region, is sufficient for avirulence and suppression functions, consistent with the view that the N-terminal region of AVR3aKI and other RXLR effectors is involved in secretion and targeting but is not required for effector activity. We also found that both polymorphic amino acids, K80 and I103, of mature AVR3a contribute to the effector functions.</AbstractText>
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<DescriptorName UI="D020868" MajorTopicYN="N">Gene Silencing</DescriptorName>
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