ABSTRACT
Research Interests:
Research Interests:
Research Interests:
The pulp of ripe bananas (Musa acuminata) contains an abundant thaumatin-like protein (TLP). Characterization of the protein and molecular cloning of the corresponding gene from banana demonstrated that the native protein consists of a... more
The pulp of ripe bananas (Musa acuminata) contains an abundant thaumatin-like protein (TLP). Characterization of the protein and molecular cloning of the corresponding gene from banana demonstrated that the native protein consists of a single polypeptide chain of 200 amino acid residues. Molecular modelling further revealed that the banana thaumatin-like protein (Ban-TLP) adopts an overall fold similar to that of thaumatin and thaumatin-like PR-5 proteins. Although the banana protein exhibits an electrostatically polarized surface, which is believed to be essential for the antifungal properties of TLPs, it is apparently devoid of antifungal activity towards pathogenic fungi. It exhibits a low but detectable in vitro endo-beta-1,3-glucanase (EC 3.2.1.x) activity. As well as being present in fruits, Ban-TLP also occurs in root tips where its accumulation is enhanced by methyl jasmonate treatment of plants. Pulp of plantains (Musa acuminata) also contains a very similar TLP, which is even more abundant than its banana homologue. Our results demonstrate for the first time that fruit-specific (abundant) TLPs are not confined to dicots but occur also in fruits of monocot species. The possible role of the apparent widespread accumulation of fruit-specific TLPs is discussed.
Research Interests:
Research Interests:
Page 1. Plant Molecular Biology 29: 579-598, 1995. © 1995 Kluwer Academic Publishers. Printed in Belgium. 579 A lectin and a lectin-related protein are the two most prominent proteins in the bark of yellow wood (Cladrastis lutea). ...
Research Interests:
Page 1. 511 AM Wu (ed.), The Molecular Immunology of Complex Carbohydrates-3, Advances in Experimental Medicine and Biology 705, DOI 10.1007/978-1-4419-7877-6_27, © Springer Science+Business Media, LLC 2011 ...
Research Interests:
... 789795. Article | PDF (381 K) | View Record in Scopus | Cited By in Scopus (79). [2] M. Fernández-Rivas, S. Bolhaar, E. González-Mancebo, R. Asero, A. van Leeuwen and B ... 627654. Full Text via CrossRef | View Record in Scopus |... more
... 789795. Article | PDF (381 K) | View Record in Scopus | Cited By in Scopus (79). [2] M. Fernández-Rivas, S. Bolhaar, E. González-Mancebo, R. Asero, A. van Leeuwen and B ... 627654. Full Text via CrossRef | View Record in Scopus | Cited By in Scopus (374). [6] JP Borges, A ...
Interactions between plant cell walls and plasma membranes are essential for cells to function properly, but the molecules that mediate the structural continuity between wall and membrane are unknown. Some of these interactions, which are... more
Interactions between plant cell walls and plasma membranes are essential for cells to function properly, but the molecules that mediate the structural continuity between wall and membrane are unknown. Some of these interactions, which are visualized upon tissue plasmolysis in Arabidopsis (Arabidopsis thaliana), are disrupted by the RGD (arginine-glycine-aspartic acid) tripeptide sequence, a characteristic cell adhesion motif in mammals. In planta induced-O (IPI-O) is an RGD-containing protein from the plant pathogen Phytophthora infestans that can disrupt cell wall-plasma membrane adhesions through its RGD motif. To identify peptide sequences that specifically bind the RGD motif of the IPI-O protein and potentially play a role in receptor recognition, we screened a heptamer peptide library displayed in a filamentous phage and selected two peptides acting as inhibitors of the plasma membrane RGD-binding activity of Arabidopsis. Moreover, the two peptides also disrupted cell wall-plas...
Research Interests: Cell Adhesion, Signal Transduction, Arabidopsis thaliana, Biological Sciences, Protein-Protein Interaction, and 16 morePlant Physiology, Plant, Lectins, Arabidopsis, Protein Sequence Analysis, Fabaceae, Phytophthora infestans, Amino Acid Profile, Plant Pathogen, Plant Cell Wall, Amino Acid Sequence, Cell Wall, Cell Surface Markers, Ligands, Receptor-Like Kinase, and Plasma Membrane
An Arabidopsis cDNA clone that defines a new class of plant serine/threonine receptor kinases was found to be a member of a family of four clustered genes (lecRK-a1-a4) which have been cloned, sequenced and mapped on chromosome 3. This... more
An Arabidopsis cDNA clone that defines a new class of plant serine/threonine receptor kinases was found to be a member of a family of four clustered genes (lecRK-a1-a4) which have been cloned, sequenced and mapped on chromosome 3. This family belongs to a large superfamily encoding putative receptors with an extracellular domain homologous to legume lectins and appears to be conserved at least among dicots. In the Columbia ecotype only the lecRK-a1 and perhaps the lecRK-a3 gene is functional, since lecRK-a2 is disrupted by a Ty-copia retroelement and lecRK-a4 contains a frameshift mutation. Structural analysis of the lecRK-al and lecRK-a3 deduced amino-acid sequences suggests that the lectin domain is unlikely to be involved in binding monosaccharides but could interact with complex glycans and/or with hydrophobic ligands. Immunodetection of lecRK gene products in plasma membranes purified by free-flow electrophoresis showed that the lecRK-a proteins are probably highly glycosylated...
Research Interests: Genetics, Molecular Evolution, Plant Biology, Medicinal Plants, Plant Molecular Biology, and 12 morePhylogeny, Sequence alignment, Lectins, Structure Analysis, Plant Lectins, Arabidopsis, Fabaceae, Protein Conformation, Amino Acid Sequence, PLANT PROTEINS, Plasma Membrane, and Biochemistry and cell biology
ABSTRACT The three-dimensional structures available for peanut and tree nut allergens are derived primarily from homology modeling and, less often, from crystallographic or 1H-NMR studies. They belong to different groups of proteins,... more
ABSTRACT The three-dimensional structures available for peanut and tree nut allergens are derived primarily from homology modeling and, less often, from crystallographic or 1H-NMR studies. They belong to different groups of proteins, including: (1): legumin and vicilin proteins with a cupin motif (Ara h 1, Ara h 3/4, tree nut legumins and vicilins); (2): 2S albumins (Ara h 2, Ara h 6, Ara h 7, 2S albumins from tree nuts); (3): profilins (Ara h 5); (4): PR-10 proteins (Ara h 8); (5): lipid transfer proteins (LTP) (Ara h 9); and (6): lectins (Ara h agglutinin or peanut agglutinin [PNA]). They consist essentially of seed storage proteins occurring in protein bodies, which usually resist heat denaturation while resistance to digestive proteolysis is variable but often elevated. In addition, oleosins, which occur in seed oil bodies (oleosomes), have been recently characterized as major allergens. Most of the sequential IgE-binding epitopes (B epitopes) on the molecular surface of the major peanut allergens (Ara h 1, Ara h 2, Ara h 3) have been mapped. The existence of common epitopes is the basis for cross-reactions between peanut and tree nut, the clinical significance of which is not always evident. To date, however, very few data are available on the T-cell epitopes of peanut allergens, with the exception of the T-cell epitopes of Ara h 2 which have been characterized. These advances on the localization of the B and T-cell epitopes on the molecular surface of these allergens pave the way for the production of recombinant hypoallergenic proteins to be used in specific immunotherapy.
Research Interests:
Plant lectins comprise a widespread group of carbohydrate-binding proteins that show a marked heterogeneity with respect to their molecular structure, sugar-binding specificity and temporal and spatial regulation. Until recently, the role... more
Plant lectins comprise a widespread group of carbohydrate-binding proteins that show a marked heterogeneity with respect to their molecular structure, sugar-binding specificity and temporal and spatial regulation. Until recently, the role of most lectins was associated with ...
Research Interests:
Research Interests: Plant Biology and Plant
Research Interests:
Research Interests:
Research Interests:
Research Interests:
Research Interests: Physiology, Molecular Evolution, Tobacco, Regulation of Gene Expression, Plant Growth Regulators, and 13 moreP-glycoprotein, Lectins, Plant growth hormone, Medical Physiology, Plant Lectins, Cell nucleus, Nicotiana Tabacum, Cytoplasm, Methyl Ester, Biochemistry and cell biology, Jasmonic Acid, Plant Leaves, and Cucurbitaceae
Heltuba, a tuber lectin from the Jerusalem artichoke Helianthus tuberosus, belongs to the mannose-binding subgroup of the family of jacalin-related plant lectins. Heltuba is highly specific for the disaccharides Man alpha 1-3Man or Man... more
Heltuba, a tuber lectin from the Jerusalem artichoke Helianthus tuberosus, belongs to the mannose-binding subgroup of the family of jacalin-related plant lectins. Heltuba is highly specific for the disaccharides Man alpha 1-3Man or Man alpha 1-2Man, two carbohydrates that are particularly abundant in the glycoconjugates exposed on the surface of viruses, bacteria and fungi, and on the epithelial cells along the gastrointestinal tract of lower animals. Heltuba is therefore a good candidate as a defense protein against plant pathogens or predators. The 2.0 A resolution structure of Heltuba exhibits a threefold symmetric beta-prism fold made up of three four-stranded beta sheets. The crystal structures of Heltuba in complex with Man alpha 1-3Man and Man alpha 1-2Man, solved at 2.35 A and 2.45 A resolution respectively, reveal the carbohydrate-binding site and the residues required for the specificity towards alpha 1-3 or alpha 1-2 mannose linkages. In addition, the crystal packing reveals a remarkable, donut-shaped, octahedral assembly of subunits with the mannose moieties at the periphery, suggesting possible cross-linking interactions with branched oligomannosides. The structure of Heltuba, which is the prototype for an extended family of mannose-binding agglutinins, shares the carbohydrate-binding site and beta-prism topology of its galactose-binding counterparts jacalin and Maclura pomifera lectin. However, the beta-prism elements recruited to form the octameric interface of Heltuba, and the strategy used to forge the mannose-binding site, are unique and markedly dissimilar to those described for jacalin. The present structure highlights a hitherto unrecognized adaptability of the beta-prism building block in the evolution of plant proteins.
Research Interests: Structure, Protein Folding, Crystallization, Biological Sciences, Crystal structure, and 13 moreSequence alignment, Lectins, Plant Lectins, CHEMICAL SCIENCES, Protein Secondary Structure Prediction, Gastrointestinal Tract, Plant Pathogen, Helianthus, Amino Acid Sequence, Disaccharides, Agglutinins, Mannose, and Binding Site
Research Interests: Catalysis, Proteomics, Polysaccharides, Macromolecular X-Ray Crystallography, Biological Sciences, and 21 moreCrystal structure, LaTeX, Glucose, Mathematical Sciences, Musa, Fruit, Allergens, Immunoglobulin E, Proteins, Protein Secondary Structure Prediction, Phenylalanine, Time Factors, Substrate Specificity, Molecular Conformation, Protein Conformation, Amino Acid Sequence, Protein Binding, Epitopes, Syndrome, Glutamic Acid, and Tyrosine
Research Interests: Structural Analysis, Allergy, Humans, Circular Dichroism, Escherichia coli, and 13 moreAnimals, Allergens, Structure Analysis, Pichia pastoris, Molecular cloning, Protein expression and purification, Malus, Rats, Gateway, Recombinant Protein, Recombinant Proteins, Site-directed Mutagenesis, and Biochemistry and cell biology
Research Interests:
The pulp of ripe bananas (Musa acuminata) contains an abundant thaumatin-like protein (TLP). Characterization of the protein and molecular cloning of the corresponding gene from banana demonstrated that the native protein consists of a... more
The pulp of ripe bananas (Musa acuminata) contains an abundant thaumatin-like protein (TLP). Characterization of the protein and molecular cloning of the corresponding gene from banana demonstrated that the native protein consists of a single polypeptide chain of 200 amino acid residues. Molecular modelling further revealed that the banana thaumatin-like protein (Ban-TLP) adopts an overall fold similar to that of thaumatin and thaumatin-like PR-5 proteins. Although the banana protein exhibits an electrostatically polarized surface, which is believed to be essential for the antifungal properties of TLPs, it is apparently devoid of antifungal activity towards pathogenic fungi. It exhibits a low but detectable in vitro endo-beta-1,3-glucanase (EC 3.2.1.x) activity. As well as being present in fruits, Ban-TLP also occurs in root tips where its accumulation is enhanced by methyl jasmonate treatment of plants. Pulp of plantains (Musa acuminata) also contains a very similar TLP, which is even more abundant than its banana homologue. Our results demonstrate for the first time that fruit-specific (abundant) TLPs are not confined to dicots but occur also in fruits of monocot species. The possible role of the apparent widespread accumulation of fruit-specific TLPs is discussed.
Research Interests:
The localization and distribution of non-specific lipid transfer proteins (nsLTP) allergens in the skin and pulp of Rosaceae fruits (apple, peach, apricot, plum) has been investigated. nsLTP essentially concentrate in the pericarp of the... more
The localization and distribution of non-specific lipid transfer proteins (nsLTP) allergens in the skin and pulp of Rosaceae fruits (apple, peach, apricot, plum) has been investigated. nsLTP essentially concentrate in the pericarp of the fruits whereas the pulp contains lower amounts of allergens. Immunolocalization showed they are primarily located in the cytosol but are subsequently excreted and finally accumulate at the plasmalemma-cell wall interface and in the cell wall. However, high discrepancies were observed in the content of allergens among, e.g. different cultivars of apple. As a consequence, the consumption of peeled-off fruits is recommended to reduce the risk of severe allergic reactions (anaphylactic shock) in individuals sensitized to Rosaceae fruits.
Research Interests:
Research Interests:
Research Interests:
Research Interests:
Research Interests: Genetics, Plant Biology, Plant Molecular Biology, Phylogeny, Structural equation models, and 14 moreMolecular Modelling, Plants, Lectins, RNA isolation, Plant Lectins, Plant Roots, Molecular cloning, Protein Secondary Structure Prediction, Molecular weight, Amino Acid Sequence, Base Sequence, Binding Site, cDNA library, and Biochemistry and cell biology
Many higher plants establish symbiotic relationships with arbuscular mycorrhizal (AM) fungi that improve their ability to acquire nutrients from the soil. In addition to establishing AM symbiosis, legumes also enter into a nitrogen-fixing... more
Many higher plants establish symbiotic relationships with arbuscular mycorrhizal (AM) fungi that improve their ability to acquire nutrients from the soil. In addition to establishing AM symbiosis, legumes also enter into a nitrogen-fixing symbiosis with bacteria known as rhizobia that results in the formation of root nodules. Several genes involved in the perception and transduction of bacterial symbiotic signals named "Nod factors" have been cloned recently in model legumes through forward genetic approaches. Among them, DMI3 (Doesn't Make Infections 3) is a calcium- and calmodulin-dependent kinase required for the establishment of both nodulation and AM symbiosis. We have identified, by a yeast two-hybrid system, a novel protein interacting with DMI3 named IPD3 (Interacting Protein of DMI3). IPD3 is predicted to interact with DMI3 through a C-terminal coiled-coil domain. Chimeric IPD3::GFP is localized to the nucleus of transformed Medicago truncatula root cells, in which split yellow fluorescent protein assays suggest that IPD3 and DMI3 physically interact in Nicotiana benthamiana. Like DMI3, IPD3 is extremely well conserved among the angiosperms and is absent from Arabidopsis. Despite this high level of conservation, none of the homologous proteins have a demonstrated biological or biochemical function. This work provides the first evidence of the involvement of IPD3 in a nuclear interaction with DMI3.
Research Interests:
Linear IgE-binding epitopes identified in legumin allergens of peanut (Ara h 3) and other allergenic tree nuts (Jug r 4 of walnut, Cor a 9 of hazelnut, Ana o 2 cashew nut) were mapped on three-dimensional models of the proteins built up... more
Linear IgE-binding epitopes identified in legumin allergens of peanut (Ara h 3) and other allergenic tree nuts (Jug r 4 of walnut, Cor a 9 of hazelnut, Ana o 2 cashew nut) were mapped on three-dimensional models of the proteins built up by homology modelling. A conformational analysis revealed that consensual surface-exposed IgE-binding epitopes exhibited some structural homology susceptible to account for the IgE-binding cross-reactivity observed among peanut and tree nut allergens. This structurally related cross-reactivity seems irrespective of the botanical origin of the allergens and thus demands that persons allergic to peanut avoid other three nuts to prevent possible allergic reactions. IgE-binding epitopes similar to those found in 11S globulin allergens do not apparently occur in other vicilin allergens with the cupin fold from peanut (Ara h 1) or tree nuts (Jug r 2 of walnut, Cor a 1 of hazel nut, Ana o 3 of cashew nut).
Research Interests:
Surface-exposed IgE-binding epitopes of close overall conformation were characterized on the molecular surface of three-dimensional models built for the vicilin allergens of peanut (Ara h 1), walnut (Jug r 2), hazelnut (Cor a 11) and... more
Surface-exposed IgE-binding epitopes of close overall conformation were characterized on the molecular surface of three-dimensional models built for the vicilin allergens of peanut (Ara h 1), walnut (Jug r 2), hazelnut (Cor a 11) and cashew nut (Ana o 1). They correspond to linear stretches of conserved amino acid sequences mainly located along the C-terminus of the polypeptide chains. A glyco-epitope corresponding to an exposed N-glycosylation site could also interfere with the IgE-binding epitopes. All these epitopic regions should participate in the IgE-binding cross-reactivity commonly reported between tree nuts or between peanut and some tree nuts in sensitized individuals. Owing to this epitopic community which constitutes a risk of cross-sensitization, the avoidance or a restricted consumption of other tree nuts should be recommended to peanut-sensitized individuals.
Research Interests: Immunology, Molecular, Molecular Immunology, NUTS, Epitope mapping, and 13 moreJuglans, Immunoglobulin E, Angiosperms, Three Dimensional, Amino Acid Profile, Conformational Analysis, Amino Acid Sequence, Corylus, Hypersensitivity, Arachis Hypogaea, Epitopes, PLANT PROTEINS, and Seed storage proteins
Eight distinct sequential IgE-binding epitopes were identified along the amino acid sequence of Ara h 3 using the Spot technology. They essentially correspond to preferencially electropositive regions exposed on the molecular surface of... more
Eight distinct sequential IgE-binding epitopes were identified along the amino acid sequence of Ara h 3 using the Spot technology. They essentially correspond to preferencially electropositive regions exposed on the molecular surface of the protein. A few IgE-binding epitopes are coalescent to create more extended IgE-binding regions exposed on the surface of the allergen. Ara h 3 contains a core region corresponding to the cupin motifs and predicted to be preserved upon the trypsin and chymotrypsin attack in the gastro-intestinal tract. Some of the identified IgE-binding epitopes should remain unaltered in the core region to subsequently interact with the local immune system. They most probably account for the strong allergenic potency of Ara h 3. Most of the identified IgE-binding epitopes of Ara h 3 readily differ from the corresponding regions of other legume and tree-nut legumin allergens except for epitope #1 and #7 which are rather conserved essentially in other allergens. These structurally related epitopes could account for some cross-reactions occurring between Ara h 3 and other legumin allergens.
Research Interests:
Research Interests:
Research Interests:
... Plant Physiol Bio-chem 2006;44:535-42. [10] Barre A, Brul C, Borges JP, Culerrier R, Jauneau A, Didier A, et al. Concentration des LTP dans la peau et la pulpe des fruits. Rev. Fr. Allergol. 2009;49:166-9. [11] Asero R, Mistrello G,... more
... Plant Physiol Bio-chem 2006;44:535-42. [10] Barre A, Brul C, Borges JP, Culerrier R, Jauneau A, Didier A, et al. Concentration des LTP dans la peau et la pulpe des fruits. Rev. Fr. Allergol. 2009;49:166-9. [11] Asero R, Mistrello G, Roncarolo D, Amato S, Falagiani P. Analysis of ...
Research Interests:
... Fax: +05 61 17 59 94, email: Pierre.Rouge@ipbs.fr ... CS-II, lectin from Cytisus scoparius; CSA-I, lectin from C. sessilifolius; EcorL, lectin from Erythrina corallodendron; LCA, lectin from Lens culinaris; LoLI, isolectin I from... more
... Fax: +05 61 17 59 94, email: Pierre.Rouge@ipbs.fr ... CS-II, lectin from Cytisus scoparius; CSA-I, lectin from C. sessilifolius; EcorL, lectin from Erythrina corallodendron; LCA, lectin from Lens culinaris; LoLI, isolectin I from Lathyrus ochrus; LTA, lectin from Lotus tetragonolobus; PHA ...
Research Interests:
... ASTERIDAE Dipsacales Caprifoliaceae Sambucus canadensis Bark [P(32 + 35»)4 NANA Sambucus ebu/us Bark [P(32 + 37»)4 NANA 401 Page 8. ... Sambucus nigra Seed Vs [P(26 + 32)12 GaINAc>Gal Bark I [P(32 + 35)] 4 NANA Nu... more
... ASTERIDAE Dipsacales Caprifoliaceae Sambucus canadensis Bark [P(32 + 35»)4 NANA Sambucus ebu/us Bark [P(32 + 37»)4 NANA 401 Page 8. ... Sambucus nigra Seed Vs [P(26 + 32)12 GaINAc>Gal Bark I [P(32 + 35)] 4 NANA Nu (SNAI) Bark I' [P(32 + 35)] 2 NANA Nu (SNAI') ...
Research Interests:
... lectins are not only the most famous lectin family but also played a determining role in the ... are carbohydrate-bind-ing proteins follows the observation that cane sugar inhibited the agglutinationactivity of ConA ... Legume lectins... more
... lectins are not only the most famous lectin family but also played a determining role in the ... are carbohydrate-bind-ing proteins follows the observation that cane sugar inhibited the agglutinationactivity of ConA ... Legume lectins have also been found in different vegetative tissues. ...
Research Interests:
Research Interests:
Research Interests:
ABSTRACT Around 40 species of Hylarana amphibians are distributed in tropical and subtropical Asia, and Chinese broad-folded frog, Hylarana latouchii (Boulenger, 1899) is one of them. In this study, six different cDNAs encoding four novel... more
ABSTRACT Around 40 species of Hylarana amphibians are distributed in tropical and subtropical Asia, and Chinese broad-folded frog, Hylarana latouchii (Boulenger, 1899) is one of them. In this study, six different cDNAs encoding four novel antimicrobial peptide precursors were cloned by screening the cDNA library of the Chinese broad-folded frog skin. The protein sequence analysis demonstrated that two deduced peptides belong to the brevinin-1 family, and the other two belong to temporin family of amphibian antimicrobial peptides. Thus, they were named as brevinin-1LT1 (FMGSALRIAAKVLPAALCQIFKKC), brevinin-1LT2 (FFGSVLKVAAKVLPAALCQIFKKC), temporin-LT1 (FLPGLIAGIAKML–NH2) and temporin-LT2 (FLPIALKALGSIFPKIL–NH2), respectively. Furthermore, brevinin-1LT1 and temporin-LT1 were purified by HPLC from the skin secretion of H. latouchii. In this work, all the peptides kill microbes by membrane-disturbing mechanisms, and this procedure was visualized via scanning electron microscopy (SEM).