The race‐specific elicitor AVR9 of the tomato pathogen <i>Cladosporium fulvum</i>: a cystine knot protein

Vervoort, Jacques; Hooven, Henno W. van den; Berg, Axel van den; Vossen, Paul; Vogelsang, R.; Joosten, M.H.A.J.; Wit, P.J.G.M. de

doi:10.1016/s0014-5793(97)00117-8

Cited by 76 publications

(40 citation statements)

References 51 publications

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“…1D-NMR spectra were recorded as described by Vervoort et al (1997). CD spectra were recorded on a Spectropolarimeter (model DP J-600, Jasco, Easton, MD) connected to an IBM personal computer.…”

Section: Nmr and CD Spectroscopymentioning

confidence: 99%

“…de Wit and P. Vossen, unpublished data). The global fold of the AVR9 peptide has been determined by 2D-NMR spectroscopy (Vervoort et al, 1997). The AVR9 elicitor contains a ␤-sheet of three antiparallel strands and three disulfide bonds arranged in a cystine knot (Isaacs, 1995).…”

mentioning

confidence: 99%

“…The AVR9 elicitor contains a ␤-sheet of three antiparallel strands and three disulfide bonds arranged in a cystine knot (Isaacs, 1995). The AVR9 elicitor is structurally related to small inhibitor peptides, such as protease inhibitors and ionchannel blockers (Vervoort et al, 1997).…”

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confidence: 99%

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Correlation between Binding Affinity and Necrosis-Inducing Activity of Mutant AVR9 Peptide Elicitors1

Kooman-Gersmann¹,

Vogelsang²,

Vossen³

et al. 1998

Plant Physiology

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The race-specific peptide elicitor AVR9 of the fungus Cladosporium fulvum induces a hypersensitive response only in tomato (Lycopersicon esculentum) plants carrying the complementary resistance gene Cf-9 (MoneyMaker-Cf9). A binding site for AVR9 is present on the plasma membranes of both resistant and susceptible tomato genotypes. We used mutant AVR9 peptides to determine the relationship between elicitor activity of these peptides and their affinity to the binding site in the membranes of tomato. Mutant AVR9 peptides were purified from tobacco (Nicotiana clevelandii) inoculated with recombinant potato virus X expressing the corresponding avirulence gene Avr9. In addition, several AVR9 peptides were synthesized chemically. Physicochemical techniques revealed that the peptides were correctly folded. Most mutant AVR9 peptides purified from potato virus X::Avr9-infected tobacco contain a single N-acetylglucosamine. These glycosylated AVR9 peptides showed a lower affinity to the binding site than the nonglycosylated AVR9 peptides, whereas their necrosis-inducing activity was hardly changed. For both the nonglycosylated and the glycosylated mutant AVR9 peptides, a positive correlation between their affinity to the membrane-localized binding site and their necrosis-inducing activity in MoneyMaker-Cf9 tomato was found. The perception of AVR9 in resistant and susceptible plants is discussed.

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Section: Nmr and CD Spectroscopymentioning

confidence: 99%

mentioning

confidence: 99%

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Correlation between Binding Affinity and Necrosis-Inducing Activity of Mutant AVR9 Peptide Elicitors1

Kooman-Gersmann¹,

Vogelsang²,

Vossen³

et al. 1998

Plant Physiology

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“…Although the tertiary structure of the protein has not yet been completely elucidated, the presence of a cystine knot motif could be established. Furthermore, the preliminary three-dimensional structure of AVR9 shows homology to that of the carboxypeptidase inhibitor, whose structure was determined by x-ray diffraction (36,37). The cystine knot motif was not found in NIP1.…”

Section: Discussionmentioning

confidence: 99%

“…The structure of NIP1 shows no homology to structures in the protein data bank, as was verified using the DALI server (www2.ebi.ac.uk/dali/) using a Zscore value of 2 as cut-off, nor with other elicitor proteins. For instance, the global fold of the AVR9 elicitor from the fungal tomato pathogen C. fulvum has been derived (36). Although the tertiary structure of the protein has not yet been completely elucidated, the presence of a cystine knot motif could be established.…”

Section: Discussionmentioning

confidence: 99%

Solution Structure of the Plant Disease Resistance-triggering Protein NIP1 from the Fungus Rhynchosporium secalis Shows a Novel β-Sheet Fold

Slot

Burg

Kloks

et al. 2003

Journal of Biological Chemistry

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Activation of the disease resistance response in a host plant frequently requires the interaction of a plant resistance gene product with a corresponding, pathogenderived signal encoded by an avirulence gene. The products of resistance genes from diverse plant species show remarkable structural similarity. However, due to the general paucity of information on pathogen avirulence genes the recognition process remains in most cases poorly understood. NIP1, a small protein secreted by the fungal barley pathogen Rhynchosporium secalis, is one of only a few fungal avirulence proteins identified and characterized to date. The defense-activating activity of NIP1 is mediated by barley resistance gene Rrs1. In addition, a role of the protein in fungal virulence is suggested by its nonspecific toxicity in leaf tissues of host and non-host cereals as well as its resistance geneindependent stimulatory effect on the plant plasma membrane H ؉ -ATPase. Four naturally occurring NIP1 isoforms are characterized by single amino acid alterations that affect the different activities in a similar way. As a step toward unraveling the signal perception/ transduction mechanism, the solution structure of NIP1 was determined. The protein structure is characterized by a novel fold. It consists of two parts containing ␤-sheets of two and three anti-parallel strands, respectively. Five intramolecular disulfide bonds, comprising a novel disulfide bond pattern, stabilize these parts and their position with respect to each other. A comparative analysis of the protein structure with the properties of the NIP1 isoforms suggests two loop regions to be crucial for the resistance-triggering activity of NIP1.

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Transmembrane Receptors in Plants: Receptor Kinases and Their Ligands

Torii

2018

Annual Plant Reviews Online

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Receptor‐like kinases (RLKs) represent by far the largest family of cell surface receptors in plants. They mediate cell–cell signals regulating self‐incompatibility, innate immunity, and a wide variety of developmental processes. The genetic dissection of paralogous RLKs illuminated their intricate redundancy, synergism, and antagonism. The nature of corresponding ligands for RLKs has been largely elusive. However, recent efforts using genetics, biochemistry, genome‐wide functional genomics, and bioinformatics led to the discovery of small, secreted peptides and cysteine‐rich secreted proteins as candidate ligands for RLKs. Studies of brassinosteroid signaling and innate immunity to bacterial flagellin peptide revealed a striking resemblance of the mechanism of plant RK activation to that of animal transforming growth factor β receptors.

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The race‐specific elicitor AVR9 of the tomato pathogen Cladosporium fulvum: a cystine knot protein

Cited by 76 publications

References 51 publications

Correlation between Binding Affinity and Necrosis-Inducing Activity of Mutant AVR9 Peptide Elicitors1

Correlation between Binding Affinity and Necrosis-Inducing Activity of Mutant AVR9 Peptide Elicitors1

Solution Structure of the Plant Disease Resistance-triggering Protein NIP1 from the Fungus Rhynchosporium secalis Shows a Novel β-Sheet Fold

Transmembrane Receptors in Plants: Receptor Kinases and Their Ligands

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