Pierre Rouge - Academia.edu (original) (raw)

Papers by Pierre Rouge

Biochemical Journal, Feb 1, 1998

Arcelin-1 is a lectin-like protein found in the seeds of wild varieties of the kidney bean (Phase... more Arcelin-1 is a lectin-like protein found in the seeds of wild varieties of the kidney bean (Phaseolus ulgaris). This protein displays insecticidal properties, but the mechanism of action is as yet unknown. In the present study we investigated the biochemical and biophysical properties of arcelin-1 from Phaseolus ulgaris cv. RAZ-2. Native arcelin-1 is a dimeric glycoprotein of 60 kDa, built from the non-covalent association of two identical monomers. This dimer resists dissociation by chaotropic agents and is highly resistant to proteolytic enzymes. Each subunit contains

Plant Physiology, Feb 1, 2000

The most abundant protein of resting rhizomes of Calystegia sepium (L.) R.Br. (hedge bindweed) ha... more The most abundant protein of resting rhizomes of Calystegia sepium (L.) R.Br. (hedge bindweed) has been isolated and its corresponding cDNA cloned. The native protein consists of a single polypeptide of 212 amino acid residues and occurs as a mixture of glycosylated and unglycosylated isoforms. Both forms are derived from the same preproprotein containing a signal peptide and a C-terminal propeptide. Analysis of the deduced amino acid sequence indicated that the C. sepium protein shows high sequence identity and structural similarity with plant RNases. However, no RNase activity could be detected in highly purified preparations of the protein. This apparent lack of activity results most probably from the replacement of a conserved His residue, which is essential for the catalytic activity of plant RNases. Our findings not only demonstrate the occurrence of a catalytically inactive variant of an S-like RNase, but also provide further evidence that genes encoding storage proteins may have evolved from genes encoding enzymes or other biologically active proteins.

Frontiers in Cellular and Infection Microbiology, Jan 23, 2023

Editorial on the Research Topic Lectins from plants, algae, fungi, bacteria and animals as potent... more Editorial on the Research Topic Lectins from plants, algae, fungi, bacteria and animals as potential therapeutic tools for SARS-CoV-2 and other pathogenic enveloped viruses, in a "one-health" perspective Lectins or carbohydrate-binding agents (CBAs) from diverse sources including plants, algae, fungi, cyanobacteria and animals, can recognize the glycan chains decorating pathogenic enveloped viruses, and consequently offer an interesting alternative to antibodies and antiviral drugs for combating viral infections. Most of the pathogenic enveloped viruses are highly N-glycosylated and exhibit surface glycoproteins containing different types of N-glycans, including complex-type glycans, high-mannose-or oligomannoside-type glycans, and hybrid-type glycans, representing potential targets for lectins with different carbohydrate-binding specificities (Barre et al., 2022). In this regard, the perspective paper from Maier, demonstrated that natural cyanovirin-N (CV-N), the mannose-specific lectin from the cyanobacterium Nostoc ellipsosporum, specifically recognizes N-glycans of the high-mannose type occurring on the surface of hemagglutinin from influenza virus, gp120 from human immunodeficiency virus 1 (HIV-1) and spike protein S from SARS-CoV and SARS-CoV-2. In addition, an engineered recombinant cyanovirin-N (CV-N) domain-swapped dimer with enhanced binding capacities towards SARS-CoV-2 showed increased binding affinity to the highly Nglycosylated spike protein and hemagglutinin. These engineered CV-N dimers with enhanced binding capacities could be used to improve the neutralization ability of the lectin towards pathogenic enveloped viruses by reducing both the internalization and the spreading of the viruses. However, the antiviral activity of lectins is not limited to hampering or preventing the recognition and subsequent anchorage of the viral particles to the host cells. The Original Research article of Vanhulle et al., brings interesting insights into the antiviral activity of the stinging nettle (Urtica dioica) lectin UDA, a small monomeric lectin with a specificity for Frontiers in Cellular and Infection Microbiology frontiersin.org 01

Glycoconjugate Journal, Nov 24, 2022

the host cell receptor dipeptidyl peptidase-4 (DPP4) for MERS-CoV, and the angiotensin-converting... more the host cell receptor dipeptidyl peptidase-4 (DPP4) for MERS-CoV, and the angiotensin-converting enzyme 2 (ACE2) for SARS-CoV and SARS-CoV-2, are also glycosylated proteins exhibiting glycan free surfaces allowing the recognition of the RBDs from the pathogenic beta-coronaviruses [5, 6] (Fig. 1). Since the onset of beta-coronavirus-related respiratory syndromes, the glycans covering the MERS-CoV, SARS-CoV and SARS-CoV-2 spikes, have been investigated in detail [7-10]. Complex-, high mannose-and hybrid-type N-glycans occupy the S proteins forming the spikes from MERS-CoV, SARS-CoV and SARS-CoV-2, but the proportions of these three types of N-glycans occurring at the 23 N-glycosylation sites of MERS-CoV and the 22 N-glycosylation sites of SARS-CoV and SARS-CoV-2 are very different (Fig. 3) [7]. In this respect, high-mannose type N-glycans are most abundant in spikes of MERS-CoV, whereas complex-type glycans are predominantly distributed on the spikes of SARS-CoV and SARS-CoV-2, respectively. High-mannose type glycans occurring in the S proteins of beta-coronaviruses essentially correspond to

HAL (Le Centre pour la Communication Scientifique Directe), 2019

Allergic diseases have increased its incidence worldwide, increasing the significance of research... more Allergic diseases have increased its incidence worldwide, increasing the significance of research in diagnostics to offer more precise immunotherapy options. Most current lines of work revolve around single-protein detection, which relies mostly on faint fluorescence signals and large expensive detectors. In this context, we propose a procedure based on visible light absorption by polymeric microparticles. The beads acting as supports react with the serum of an allergic patient and perform a magnetically-assisted immunoassay, similar to indirect ELISA. Firstly, protein binding on surface and antibody recognition was evaluated by SEM imaging. Then, the procedure sensibility was determined, were the lowest detected IgE concentration is 24 ng/mL, and the response is linear within a working range comparable to commercial standards. Finally, the effects of cross-reactive allergen specimens were assessed, yielding difficulties in detection at antibody concentrations below 36 ng/mL. Consequently, we have provided a proof-of-concept of a microparticle-based immunoassay with affordable miniaturization capability for benchtop equipement.

Foods, Jan 30, 2021

This article is an open access article distributed under the terms and conditions of the Creative... more This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY

Proteins, Dec 1, 1997

Arcelin-1 and ␣-amylase inhibitor are two lectin-like glycoproteins expressed in the seeds of the... more Arcelin-1 and ␣-amylase inhibitor are two lectin-like glycoproteins expressed in the seeds of the kidney bean (Phaseolus vulgaris). They display insecticidal activities and protect the seeds from predation by larvae of various bruchids through different biological actions. Solution-state investigations by small-angle X-ray scattering (SAXS) show the dimeric structure of arcelin-1, a requirement for its hemagglutinating properties. Anions were found to have specific properties in their effectiveness to disrupt protein aggregates, affect solubility, and improve crystallizability. The SAXS results were used to improve crystallization conditions, and single crystals diffracting beyond 1.9 Å resolution were obtained. X-ray diffraction data analysis shows that noncrystallographic symmetryrelated arcelin-1 molecules form a lectin-like dimer and reveals the presence of a solventexposed anion binding site on the protein, at a crystal-packing interface. The solution state properties of arcelin-1 and crystal twinning may be explained by the anion specificity of this binding site. Proteins 29:433-442, 1997.

Cancers, Aug 28, 2021

Marine Drugs, Jul 26, 2019

To date, a number of mannose-specific lectins have been isolated and characterized from seaweeds,... more To date, a number of mannose-specific lectins have been isolated and characterized from seaweeds, especially from red algae. In fact, man-specific seaweed lectins consist of different structural scaffolds harboring a single or a few carbohydrate-binding sites which specifically recognize mannose-containing glycans. Depending on the structural scaffold, man-specific seaweed lectins belong to five distinct structurally-related lectin families, namely (1) the griffithsin lectin family (β-prism I scaffold); (2) the Oscillatoria agardhii agglutinin homolog (OAAH) lectin family (β-barrel scaffold); (3) the legume lectin-like lectin family (β-sandwich scaffold); (4) the Galanthus nivalis agglutinin (GNA)-like lectin family (β-prism II scaffold); and, (5) the MFP2-like lectin family (MFP2-like scaffold). Another algal lectin from Ulva pertusa, has been inferred to the methanol dehydrogenase related lectin family, because it displays a rather different GlcNAc-specificity. In spite of these structural discrepancies, all members from the five lectin families share a common ability to specifically recognize man-containing glycans and, especially, high-mannose type glycans. Because of their mannose-binding specificity, these lectins have been used as valuable tools for deciphering and characterizing the complex mannose-containing glycans from the glycocalyx covering both normal and transformed cells, and as diagnostic tools and therapeutic drugs that specifically recognize the altered high-mannose N-glycans occurring at the surface of various cancer cells. In addition to these anti-cancer properties, man-specific seaweed lectins have been widely used as potent human immunodeficiency virus (HIV-1)-inactivating proteins, due to their capacity to specifically interact with the envelope glycoprotein gp120 and prevent the virion infectivity of HIV-1 towards the host CD4+ T-lymphocyte cells in vitro.

Biochimica Et Biophysica Acta - Proteins And Proteomics, Nov 1, 1997

Ž. Ž. Alpha-amylase inhibitor a-AI from kidney bean Phaseolus Õulgaris L. cv Tendergreen seeds ha... more Ž. Ž. Alpha-amylase inhibitor a-AI from kidney bean Phaseolus Õulgaris L. cv Tendergreen seeds has been purified to homogeneity by heat treatment in acidic medium, ammonium sulphate fractionation, chromatofocusing and gel filtration. Two isoforms, a-AI1 and a-AI1 X , of 43 kDa have been isolated which differ from each other by their isoelectric points and Ž. neutral sugar contents. The major isoform a-AI1 inhibited human and porcine pancreatic a-amylases PPA but was devoid of activity on a-amylases of bacterial or fungal origins. As shown on the Lineweaver-Burk plots, the nature of the inhibition is explained by a mixed non-competitive inhibition mechanism. a-AI1 formed a 1:2 stoichiometric complex with PPA which showed an optimum pH of 4.5 at 308C. Owing to the low optimum pH found for a-AI activity, inhibitor-containing diets such as beans or transgenic plants expressing a-AI should be devoid of any harmful effect on human health. q 1997 Elsevier Science B.V.

HAL (Le Centre pour la Communication Scientifique Directe), 2013

HAL is a multidisciplinary open access archive for the deposit and dissemination of scientific re... more HAL is a multidisciplinary open access archive for the deposit and dissemination of scientific research documents, whether they are published or not. The documents may come from teaching and research institutions in France or abroad, or from public or private research centers. L'archive ouverte pluridisciplinaire HAL, est destinée au dépôt et à la diffusion de documents scientifiques de niveau recherche, publiés ou non, émanant des établissements d'enseignement et de recherche français ou étrangers, des laboratoires publics ou privés. Distributed under a Creative Commons Attribution-NonCommercial-ShareAlike| 4.0 International License AVIS en réponse à la saisine 130418-saisine HCBdossier 2012-1061 concernant le dossier EFSA-GMO-NL-2012-106

Foods, Nov 24, 2020

Lectins or carbohydrate-binding proteins are widely distributed in seeds and vegetative parts of ... more Lectins or carbohydrate-binding proteins are widely distributed in seeds and vegetative parts of edible plant species. A few lectins from different fruits and vegetables have been identified as potential food allergens, including wheat agglutinin, hevein (Hev b 6.02) from the rubber tree and chitinases containing a hevein domain from different fruits and vegetables. However, other well-known lectins from legumes have been demonstrated to behave as potential food allergens taking into account their ability to specifically bind IgE from allergic patients, trigger the degranulation of sensitized basophils, and to elicit interleukin secretion in sensitized people. These allergens include members from the different families of higher plant lectins, including legume lectins, type II ribosome-inactivating proteins (RIP-II), wheat germ agglutinin (WGA), jacalin-related lectins, GNA (Galanthus nivalis agglutinin)-like lectins, and Nictaba-related lectins. Most of these potentially active lectin allergens belong to the group of seed storage proteins (legume lectins), pathogenesis-related protein family PR-3 comprising hevein and class I, II, IV, V, VI, and VII chitinases containing a hevein domain, and type II ribosome-inactivating proteins containing a ricin B-chain domain (RIP-II). In the present review, we present an exhaustive survey of both the structural organization and structural features responsible for the allergenic potency of lectins, with special reference to lectins from dietary plant species/tissues consumed in Western countries.

Biomolecules, Jul 16, 2022

Allergies, Feb 3, 2023

Frontiers in Physiology, Nov 17, 2021

Trypsin is a serine protease that is synthesized by the gut epithelial cells of female mosquitoes... more Trypsin is a serine protease that is synthesized by the gut epithelial cells of female mosquitoes; it is the enzyme that digests the blood meal. To study its molecular regulation, Culex quinquefasciatus late trypsin was purified by diethylaminoethyl (DEAE), affinity, and C 18 reverse-phase high performance liquid chromatography (HPLC) steps, and the N-terminal amino acid sequence was determined for molecular cloning. Five overlapping segments of the late trypsin cDNA were amplified by PCR, cloned, and the full sequence (855 bp) was characterized. Three-dimensional models of the protrypsin and activated trypsin were built and compared with other trypsin models. Trypsin modulating oostatic factor (TMOF) concentrations in the hemolymph were determined by ELISA and compared with trypsin activity in the gut after the blood meal. The results showed that there was an increase in TMOF concentrations circulating in the hemolymph which has correlated to the reduction of trypsin activity in the mosquito gut. Northern blot analysis of the trypsin transcripts after the blood meal indicated that trypsin activity also followed the increase and decrease of the trypsin transcript. Injections of different amounts of TMOF (0.025 to 50 µg) decreased the amounts of trypsin in the gut. However, Northern blot analysis showed that TMOF injections did not cause a decrease in trypsin transcript abundance, indicating that TMOF probably affected trypsin translation.

Biochemical Journal, Jun 1, 2002

Sambucus nigra agglutinin I (SNA-I) is a type 2 ribosomeinactivating protein. Site-directed mutag... more Sambucus nigra agglutinin I (SNA-I) is a type 2 ribosomeinactivating protein. Site-directed mutagenesis was used to mimic the conversion of the highly active B-chain of fruit-specific SNA (SNA-If) into the completely inactive B-chain of the closely related and naturally occurring loss-of-activity mutant called S. nigra agglutinin lectin-related protein. In the first mutant SNA-If-M1 the high-affinity site 2 of SNA-If was disrupted by replacing the presumed critical residue Asp#$" with Glu#$". In the double mutant SNA-If-M2, site 1 of SNA-If-M1 was also disrupted by substituting the presumed critical residue Asn%) with Ser%). The parent type 2 ribosome-inactivating protein and both mutants were expressed in Nicotiana tabacum Samsun NN and

Biochemical Journal, May 10, 1999

Two lectins have been isolated from bluebell (Scilla campanulata) bulbs. From their isolation by ... more Two lectins have been isolated from bluebell (Scilla campanulata) bulbs. From their isolation by affinity chromatography, they are characterized as a mannose-binding lectin (SCAman) and a fetuin-binding lectin (SCAfet). SCAman preferentially binds oligosaccharides with α(1,3)and α(1,6)-linked mannopyranosides. It is a tetramer of four identical protomers of approx. 13 kDa containing 119 amino acid residues ; it is not glycosylated. The fetuin-binding lectin (SCAfet), which is not inhibited by any simple sugars, is also unglycosylated. It is a tetramer of four identical subunits of approx. 28 kDa containing Abbreviations used : AMA, tuber lectin from Arum maculatum ; DOM, domain ; GNA, Galanthus nivalis agglutinin ; HCA, hydrophobic cluster analysis ; LECSCA, cDNA encoding the lectin from Scilla campanulata ; RIPs, ribosome-inactivating proteins ; SCAman, mannose-binding Scilla campanulata lectin ; SCAfet, fetuin-binding Scilla campanulata lectin.

HAL (Le Centre pour la Communication Scientifique Directe), 2012

HAL (Le Centre pour la Communication Scientifique Directe), 2009

Le Comité scientifique du Haut conseil des biotechnologies à été saisi le 20 juillet 2009, par le... more Le Comité scientifique du Haut conseil des biotechnologies à été saisi le 20 juillet 2009, par les autorités compétentes françaises (Ministère de l'Alimentation, de l'Agriculture et de la Pêche) d'une demande d'avis relative à un dossier de demande d'autorisation aux fins de mise en culture, d'importation, de transformation, et d'alimentation humaine et animale, dans l'Union Européenne du maïs génétiquement modifié portant l'évènement NK603. Ce dossier est déposé par Monsanto Europe S.A., dans le cadre du règlement 1829/2003 et enregistré à l'AESA (Autorité européenne de sécurité des aliments) sous la référence EFSA/ GMO/NL/2005/22. Le Comité scientifique du Haut conseil des biotechnologies réuni le 29 septembre 2009, sous la présidence du Professeur Jean-Christophe Pagès, a procédé à l'examen de ce dossier EFSA/ GMO/NL/2005/22. Compte tenu du fait que ce dossier a déjà donné lieu à une opinion de 1/9 l'AESA et des délais impartis, le Comité scientifique a discuté l'analyse des risques pour l'environnement menée par l'AESA mais n'a pas examiné en détail les risques pour la santé. Outre l'analyse des risques pour l'environnement, le CS a examiné les implications qu'aurait la mise en culture du maïs NK603 en termes de coexistence des filières de production.