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Mayte Villalba - One of the best experts on this subject based on the ideXlab platform.
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a relevant ige reactive 28 kda protein identified from salsola kali pollen extract by proteomics is a natural degradation product of an integral 47 kda polygalaturonase
Biochimica et Biophysica Acta, 2017Co-Authors: Carmen Oeosantos, Vivian De Los Rios, Javier Cuestaherranz, Cédric Colas, Rodrigo Barderas, Javier Fernandez, Rosalia Rodriguez, Araceli Diazperales, D Barber, Mayte VillalbaAbstract:A highly prevalent IgE-binding protein band of 28 kDa is observed when Salsola kali pollen extract is incubated with individual sera from Amaranthaceae pollen sensitized patients. By an immunoproteomic analysis of S. kali pollen extract, we identified this protein band as an allergenic Polygalacturonase enzyme. The allergen, named Sal k 6, exhibits a pI of 7.14 and a molecular mass of 39,554.2 Da. It presents similarities to Platanaceae, Poaceae, and Cupressaceae allergenic Polygalacturonases. cDNA-encoding sequence was subcloned into the pET41b vector and produced in bacteria as a His-tag fusion recombinant protein. The far-UV CD spectrum determined that rSal k 6 was folded. Immunostaining of the S. kali pollen protein extract with a rSal k 6-specific pAb and LC-MS/MS proteomic analyses confirmed the co-existence of the 28 kDa band together with an allergenic band of about 47 kDa in the pollen extract. Therefore, the 28 kDa was assigned as a natural degradation product of the 47 kDa integral Polygalacturonase. The IgE-binding inhibition to S. kali pollen extract using rSal k 6 as inhibitor showed that signals directed to both protein bands of 28 and 47 kDa were completely abrogated. The average prevalence of rSal k 6 among the three populations analyzed was 30%, with values correlating well with the levels of grains/m3 of Amaranthaceae pollen. Sal k 6 shares IgE epitopes with Oleaceae members (Fraxinus excelsior, Olea europaea and Syringa vulgaris), with IgE-inhibition values ranging from 20% to 60%, respectively. No IgE-inhibition was observed with plant-derived food extracts.
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a relevant ige reactive 28kda protein identified from salsola kali pollen extract by proteomics is a natural degradation product of an integral 47kda polygalaturonase proteins and proteomics
Biochimica et Biophysica Acta, 2017Co-Authors: Carmen Oeosantos, Vivian De Los Rios, Javier Cuestaherranz, Cédric Colas, Rodrigo Barderas, Javier Fernandez, Rosalia Rodriguez, Araceli Diazperales, D Barber, Mayte VillalbaAbstract:A highly prevalent IgE-binding protein band of 28kDa is observed when Salsola kali pollen extract is incubated with individual sera from Amaranthaceae pollen sensitized patients. By an immunoproteomic analysis of S. kali pollen extract, we identified this protein band as an allergenic Polygalacturonase enzyme. The allergen, named Sal k 6, exhibits a pI of 7.14 and a molecular mass of 39,554.2Da. It presents similarities to Platanaceae, Poaceae, and Cupressaceae allergenic Polygalacturonases. cDNA-encoding sequence was subcloned into the pET41b vector and produced in bacteria as a His-tag fusion recombinant protein. The far-UV CD spectrum determined that rSal k 6 was folded. Immunostaining of the S. kali pollen protein extract with a rSal k 6-specific pAb and LC-MS/MS proteomic analyses confirmed the co-existence of the 28kDa band together with an allergenic band of about 47kDa in the pollen extract. Therefore, the 28kDa was assigned as a natural degradation product of the 47kDa integral Polygalacturonase. The IgE-binding inhibition to S. kali pollen extract using rSal k 6 as inhibitor showed that signals directed to both protein bands of 28 and 47kDa were completely abrogated. The average prevalence of rSal k 6 among the three populations analyzed was 30%, with values correlating well with the levels of grains/m³ of Amaranthaceae pollen. Sal k 6 shares IgE epitopes with Oleaceae members (Fraxinus excelsior, Olea europaea and Syringa vulgaris), with IgE-inhibition values ranging from 20% to 60%, respectively. No IgE-inhibition was observed with plant-derived food extracts.
Felice Cervone - One of the best experts on this subject based on the ideXlab platform.
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plant immunity triggered by engineered in vivo release of oligogalacturonides damage associated molecular patterns
Proceedings of the National Academy of Sciences of the United States of America, 2015Co-Authors: Manuel Benedetti, Daniela Pontiggia, Sara Raggi, Zhenyu Cheng, Flavio Scaloni, Simone Ferrari, Frederick M Ausubel, Felice Cervone, Giulia De LorenzoAbstract:Oligogalacturonides (OGs) are fragments of pectin that activate plant innate immunity by functioning as damage-associated molecular patterns (DAMPs). We set out to test the hypothesis that OGs are generated in planta by partial inhibition of pathogen-encoded Polygalacturonases (PGs). A gene encoding a fungal PG was fused with a gene encoding a plant Polygalacturonase-inhibiting protein (PGIP) and expressed in transgenic Arabidopsis plants. We show that expression of the PGIP–PG chimera results in the in vivo production of OGs that can be detected by mass spectrometric analysis. Transgenic plants expressing the chimera under control of a pathogen-inducible promoter are more resistant to the phytopathogens Botrytis cinerea, Pectobacterium carotovorum, and Pseudomonas syringae. These data provide strong evidence for the hypothesis that OGs released in vivo act as a DAMP signal to trigger plant immunity and suggest that controlled release of these molecules upon infection may be a valuable tool to protect plants against infectious diseases. On the other hand, elevated levels of expression of the chimera cause the accumulation of salicylic acid, reduced growth, and eventually lead to plant death, consistent with the current notion that trade-off occurs between growth and defense.
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an update on Polygalacturonase inhibiting protein pgip a leucine rich repeat protein that protects crop plants against pathogens
Frontiers in Plant Science, 2015Co-Authors: Raviraj M Kalunke, Manuel Benedetti, Felice Cervone, Giulia De Lorenzo, Silvio Tundo, Renato DovidioAbstract:Polygalacturonase inhibiting proteins (PGIPs) are cell wall proteins that inhibit the pectin-depolymerizing activity of Polygalacturonases secreted by microbial pathogens and insects. These ubiquitous inhibitors have a leucine-rich repeat structure that is strongly conserved in monocot and dicot plants. Previous reviews have summarized the importance of PGIP in plant defense and the structural basis of PG-PGIP interaction; here we update the current knowledge about PGIPs with the recent findings on the composition and evolution of pgip gene families, with a special emphasis on legume and cereal crops. We also update the information about the inhibition properties of single pgip gene products against microbial PGs and the results, including field tests, showing the capacity of PGIP to protect crop plants against fungal, oomycetes and bacterial pathogens.
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integration of evolutionary and desolvation energy analysis identifies functional sites in a plant immunity protein
Proceedings of the National Academy of Sciences of the United States of America, 2009Co-Authors: Manuela Casasoli, Flavio Scaloni, Felice Cervone, Adele Di Matteo, Luca Federici, Francesco Spinelli, Nicoletta Vella, Juan Fernandezrecio, Giulia De LorenzoAbstract:Plant immune responses often depend on leucine-rich repeat receptors that recognize microbe-associated molecular patterns or pathogen-specific virulence proteins, either directly or indirectly. When the recognition is direct, a molecular arms race takes place where plant receptors continually and rapidly evolve in response to virulence factor evolution. A useful model system to study ligand-receptor coevolution dynamics at the protein level is represented by the interaction between pathogen-derived Polygalacturonases (PGs) and plant Polygalacturonase-inhibiting proteins (PGIPs). We have applied codon substitution models to PGIP sequences of different eudicotyledonous families to identify putative positively selected sites and then compared these sites with the propensity of protein surface residues to interact with protein partners, based on desolvation energy calculations. The 2 approaches remarkably correlated in pinpointing several residues in the concave face of the leucine-rich repeat domain. These residues were mutated into alanine and their effect on the recognition of several PGs was tested, leading to the identification of unique hotspots for the PGIP-PG interaction. The combined approach used in this work can be of general utility in cases where structural information about a pattern-recognition receptor or resistance-gene product is available.
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Polygalacturonase inhibiting protein pgip in plant defence a structural view
Phytochemistry, 2006Co-Authors: Adele Di Matteo, Daniele Bonivento, Demetrius Tsernoglou, Luca Federici, Felice CervoneAbstract:Abstract Polygalacturonase-inhibiting proteins are plant extracellular leucine-rich repeat proteins that specifically bind and inhibit fungal Polygalacturonases. The interaction with PGIP limits the destructive potential of Polygalacturonases and might trigger the plant defence responses induced by oligogalacturonides. A high degree of polymorphism is found both in PGs and PGIPs, accounting for the specificity of different plant inhibitors for PGs from different fungi. Here, we review the structural features and our current understanding of the PG–PGIP interaction.
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Polygalacturonase inhibiting proteins: players in plant innate immunity?
Trends in plant science, 2006Co-Authors: Luca Federici, Demetrius Tsernoglou, Adele Di Matteo, Juan Fernández-recio, Felice CervoneAbstract:Polygalacturonase-inhibiting proteins (PGIPs) are extracellular leucine-rich repeat (LRR) proteins that recognize and inhibit fungal Polygalacturonases (PGs). The PG-PGIP interaction favours the accumulation of elicitor-active oligogalacturonides and causes the activation of defence responses. Small gene families encode PGIP isoforms that differ in affinity and specificity for PGs secreted by different pathogens. The consensus motif within the LRR structure of PGIPs is the same as that of the extracellular receptors of the plant innate immune system. Structural and functional evidence suggest that PGIPs are versatile proteins involved in innate immunity and that they are capable of recognizing different surface motifs of functionally related but structurally variable PGs.
Carmen Oeosantos - One of the best experts on this subject based on the ideXlab platform.
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a relevant ige reactive 28 kda protein identified from salsola kali pollen extract by proteomics is a natural degradation product of an integral 47 kda polygalaturonase
Biochimica et Biophysica Acta, 2017Co-Authors: Carmen Oeosantos, Vivian De Los Rios, Javier Cuestaherranz, Cédric Colas, Rodrigo Barderas, Javier Fernandez, Rosalia Rodriguez, Araceli Diazperales, D Barber, Mayte VillalbaAbstract:A highly prevalent IgE-binding protein band of 28 kDa is observed when Salsola kali pollen extract is incubated with individual sera from Amaranthaceae pollen sensitized patients. By an immunoproteomic analysis of S. kali pollen extract, we identified this protein band as an allergenic Polygalacturonase enzyme. The allergen, named Sal k 6, exhibits a pI of 7.14 and a molecular mass of 39,554.2 Da. It presents similarities to Platanaceae, Poaceae, and Cupressaceae allergenic Polygalacturonases. cDNA-encoding sequence was subcloned into the pET41b vector and produced in bacteria as a His-tag fusion recombinant protein. The far-UV CD spectrum determined that rSal k 6 was folded. Immunostaining of the S. kali pollen protein extract with a rSal k 6-specific pAb and LC-MS/MS proteomic analyses confirmed the co-existence of the 28 kDa band together with an allergenic band of about 47 kDa in the pollen extract. Therefore, the 28 kDa was assigned as a natural degradation product of the 47 kDa integral Polygalacturonase. The IgE-binding inhibition to S. kali pollen extract using rSal k 6 as inhibitor showed that signals directed to both protein bands of 28 and 47 kDa were completely abrogated. The average prevalence of rSal k 6 among the three populations analyzed was 30%, with values correlating well with the levels of grains/m3 of Amaranthaceae pollen. Sal k 6 shares IgE epitopes with Oleaceae members (Fraxinus excelsior, Olea europaea and Syringa vulgaris), with IgE-inhibition values ranging from 20% to 60%, respectively. No IgE-inhibition was observed with plant-derived food extracts.
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a relevant ige reactive 28kda protein identified from salsola kali pollen extract by proteomics is a natural degradation product of an integral 47kda polygalaturonase proteins and proteomics
Biochimica et Biophysica Acta, 2017Co-Authors: Carmen Oeosantos, Vivian De Los Rios, Javier Cuestaherranz, Cédric Colas, Rodrigo Barderas, Javier Fernandez, Rosalia Rodriguez, Araceli Diazperales, D Barber, Mayte VillalbaAbstract:A highly prevalent IgE-binding protein band of 28kDa is observed when Salsola kali pollen extract is incubated with individual sera from Amaranthaceae pollen sensitized patients. By an immunoproteomic analysis of S. kali pollen extract, we identified this protein band as an allergenic Polygalacturonase enzyme. The allergen, named Sal k 6, exhibits a pI of 7.14 and a molecular mass of 39,554.2Da. It presents similarities to Platanaceae, Poaceae, and Cupressaceae allergenic Polygalacturonases. cDNA-encoding sequence was subcloned into the pET41b vector and produced in bacteria as a His-tag fusion recombinant protein. The far-UV CD spectrum determined that rSal k 6 was folded. Immunostaining of the S. kali pollen protein extract with a rSal k 6-specific pAb and LC-MS/MS proteomic analyses confirmed the co-existence of the 28kDa band together with an allergenic band of about 47kDa in the pollen extract. Therefore, the 28kDa was assigned as a natural degradation product of the 47kDa integral Polygalacturonase. The IgE-binding inhibition to S. kali pollen extract using rSal k 6 as inhibitor showed that signals directed to both protein bands of 28 and 47kDa were completely abrogated. The average prevalence of rSal k 6 among the three populations analyzed was 30%, with values correlating well with the levels of grains/m³ of Amaranthaceae pollen. Sal k 6 shares IgE epitopes with Oleaceae members (Fraxinus excelsior, Olea europaea and Syringa vulgaris), with IgE-inhibition values ranging from 20% to 60%, respectively. No IgE-inhibition was observed with plant-derived food extracts.
Javier Fernandez - One of the best experts on this subject based on the ideXlab platform.
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a relevant ige reactive 28 kda protein identified from salsola kali pollen extract by proteomics is a natural degradation product of an integral 47 kda polygalaturonase
Biochimica et Biophysica Acta, 2017Co-Authors: Carmen Oeosantos, Vivian De Los Rios, Javier Cuestaherranz, Cédric Colas, Rodrigo Barderas, Javier Fernandez, Rosalia Rodriguez, Araceli Diazperales, D Barber, Mayte VillalbaAbstract:A highly prevalent IgE-binding protein band of 28 kDa is observed when Salsola kali pollen extract is incubated with individual sera from Amaranthaceae pollen sensitized patients. By an immunoproteomic analysis of S. kali pollen extract, we identified this protein band as an allergenic Polygalacturonase enzyme. The allergen, named Sal k 6, exhibits a pI of 7.14 and a molecular mass of 39,554.2 Da. It presents similarities to Platanaceae, Poaceae, and Cupressaceae allergenic Polygalacturonases. cDNA-encoding sequence was subcloned into the pET41b vector and produced in bacteria as a His-tag fusion recombinant protein. The far-UV CD spectrum determined that rSal k 6 was folded. Immunostaining of the S. kali pollen protein extract with a rSal k 6-specific pAb and LC-MS/MS proteomic analyses confirmed the co-existence of the 28 kDa band together with an allergenic band of about 47 kDa in the pollen extract. Therefore, the 28 kDa was assigned as a natural degradation product of the 47 kDa integral Polygalacturonase. The IgE-binding inhibition to S. kali pollen extract using rSal k 6 as inhibitor showed that signals directed to both protein bands of 28 and 47 kDa were completely abrogated. The average prevalence of rSal k 6 among the three populations analyzed was 30%, with values correlating well with the levels of grains/m3 of Amaranthaceae pollen. Sal k 6 shares IgE epitopes with Oleaceae members (Fraxinus excelsior, Olea europaea and Syringa vulgaris), with IgE-inhibition values ranging from 20% to 60%, respectively. No IgE-inhibition was observed with plant-derived food extracts.
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a relevant ige reactive 28kda protein identified from salsola kali pollen extract by proteomics is a natural degradation product of an integral 47kda polygalaturonase proteins and proteomics
Biochimica et Biophysica Acta, 2017Co-Authors: Carmen Oeosantos, Vivian De Los Rios, Javier Cuestaherranz, Cédric Colas, Rodrigo Barderas, Javier Fernandez, Rosalia Rodriguez, Araceli Diazperales, D Barber, Mayte VillalbaAbstract:A highly prevalent IgE-binding protein band of 28kDa is observed when Salsola kali pollen extract is incubated with individual sera from Amaranthaceae pollen sensitized patients. By an immunoproteomic analysis of S. kali pollen extract, we identified this protein band as an allergenic Polygalacturonase enzyme. The allergen, named Sal k 6, exhibits a pI of 7.14 and a molecular mass of 39,554.2Da. It presents similarities to Platanaceae, Poaceae, and Cupressaceae allergenic Polygalacturonases. cDNA-encoding sequence was subcloned into the pET41b vector and produced in bacteria as a His-tag fusion recombinant protein. The far-UV CD spectrum determined that rSal k 6 was folded. Immunostaining of the S. kali pollen protein extract with a rSal k 6-specific pAb and LC-MS/MS proteomic analyses confirmed the co-existence of the 28kDa band together with an allergenic band of about 47kDa in the pollen extract. Therefore, the 28kDa was assigned as a natural degradation product of the 47kDa integral Polygalacturonase. The IgE-binding inhibition to S. kali pollen extract using rSal k 6 as inhibitor showed that signals directed to both protein bands of 28 and 47kDa were completely abrogated. The average prevalence of rSal k 6 among the three populations analyzed was 30%, with values correlating well with the levels of grains/m³ of Amaranthaceae pollen. Sal k 6 shares IgE epitopes with Oleaceae members (Fraxinus excelsior, Olea europaea and Syringa vulgaris), with IgE-inhibition values ranging from 20% to 60%, respectively. No IgE-inhibition was observed with plant-derived food extracts.
Rodrigo Barderas - One of the best experts on this subject based on the ideXlab platform.
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a relevant ige reactive 28 kda protein identified from salsola kali pollen extract by proteomics is a natural degradation product of an integral 47 kda polygalaturonase
Biochimica et Biophysica Acta, 2017Co-Authors: Carmen Oeosantos, Vivian De Los Rios, Javier Cuestaherranz, Cédric Colas, Rodrigo Barderas, Javier Fernandez, Rosalia Rodriguez, Araceli Diazperales, D Barber, Mayte VillalbaAbstract:A highly prevalent IgE-binding protein band of 28 kDa is observed when Salsola kali pollen extract is incubated with individual sera from Amaranthaceae pollen sensitized patients. By an immunoproteomic analysis of S. kali pollen extract, we identified this protein band as an allergenic Polygalacturonase enzyme. The allergen, named Sal k 6, exhibits a pI of 7.14 and a molecular mass of 39,554.2 Da. It presents similarities to Platanaceae, Poaceae, and Cupressaceae allergenic Polygalacturonases. cDNA-encoding sequence was subcloned into the pET41b vector and produced in bacteria as a His-tag fusion recombinant protein. The far-UV CD spectrum determined that rSal k 6 was folded. Immunostaining of the S. kali pollen protein extract with a rSal k 6-specific pAb and LC-MS/MS proteomic analyses confirmed the co-existence of the 28 kDa band together with an allergenic band of about 47 kDa in the pollen extract. Therefore, the 28 kDa was assigned as a natural degradation product of the 47 kDa integral Polygalacturonase. The IgE-binding inhibition to S. kali pollen extract using rSal k 6 as inhibitor showed that signals directed to both protein bands of 28 and 47 kDa were completely abrogated. The average prevalence of rSal k 6 among the three populations analyzed was 30%, with values correlating well with the levels of grains/m3 of Amaranthaceae pollen. Sal k 6 shares IgE epitopes with Oleaceae members (Fraxinus excelsior, Olea europaea and Syringa vulgaris), with IgE-inhibition values ranging from 20% to 60%, respectively. No IgE-inhibition was observed with plant-derived food extracts.
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a relevant ige reactive 28kda protein identified from salsola kali pollen extract by proteomics is a natural degradation product of an integral 47kda polygalaturonase proteins and proteomics
Biochimica et Biophysica Acta, 2017Co-Authors: Carmen Oeosantos, Vivian De Los Rios, Javier Cuestaherranz, Cédric Colas, Rodrigo Barderas, Javier Fernandez, Rosalia Rodriguez, Araceli Diazperales, D Barber, Mayte VillalbaAbstract:A highly prevalent IgE-binding protein band of 28kDa is observed when Salsola kali pollen extract is incubated with individual sera from Amaranthaceae pollen sensitized patients. By an immunoproteomic analysis of S. kali pollen extract, we identified this protein band as an allergenic Polygalacturonase enzyme. The allergen, named Sal k 6, exhibits a pI of 7.14 and a molecular mass of 39,554.2Da. It presents similarities to Platanaceae, Poaceae, and Cupressaceae allergenic Polygalacturonases. cDNA-encoding sequence was subcloned into the pET41b vector and produced in bacteria as a His-tag fusion recombinant protein. The far-UV CD spectrum determined that rSal k 6 was folded. Immunostaining of the S. kali pollen protein extract with a rSal k 6-specific pAb and LC-MS/MS proteomic analyses confirmed the co-existence of the 28kDa band together with an allergenic band of about 47kDa in the pollen extract. Therefore, the 28kDa was assigned as a natural degradation product of the 47kDa integral Polygalacturonase. The IgE-binding inhibition to S. kali pollen extract using rSal k 6 as inhibitor showed that signals directed to both protein bands of 28 and 47kDa were completely abrogated. The average prevalence of rSal k 6 among the three populations analyzed was 30%, with values correlating well with the levels of grains/m³ of Amaranthaceae pollen. Sal k 6 shares IgE epitopes with Oleaceae members (Fraxinus excelsior, Olea europaea and Syringa vulgaris), with IgE-inhibition values ranging from 20% to 60%, respectively. No IgE-inhibition was observed with plant-derived food extracts.
