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Geert Angenon - One of the best experts on this subject based on the ideXlab platform.
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The Arcelin-5 Gene of Phaseolus vulgaris Directs High Seed-Specific Expression in Transgenic Phaseolus acutifolius and Arabidopsis Plants 1
2013Co-Authors: Alain Goossens, Geert Angenon, Willy Dillen, Janniek De Clercq, Marc Van Montagu, Laboratorium Voor GeneticaAbstract:The regulatory sequences of many genes encoding seed storage proteins have been used to drive seed-specific expression of a variety of proteins in transgenic plants. Because the levels at which these transgene-derived proteins accumulate are generally quite low, we investigated the utility of the Arcelin-5 regulatory sequences in obtaining high seed-specific expression in transgenic plants. Arcelin-5 is an abundant seed protein found in some wild common bean (Phaseolus vulgaris L.) genotypes. Seeds of Arabidopsis and Tepary bean (Phaseolus acutifolius A. Gray) plants transformed with Arcelin-5 gene constructs synthesized Arcelin-5 to levels of 15 % and 25 % of the total protein content, respectively. To our knowledge, such high expression levels directed by a transgene have not been reported before. The transgenic plants also showed low plant-to-plant variation in Arcelin expression. Complex transgene integration patterns, which often result in gene silencing effects
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Analysis of bruchid resistance in the wild common bean accession G02771: no evidence for insecticidal activity of Arcelin 5
Journal of Experimental Botany, 2000Co-Authors: Alain Goossens, Cesar Cardona, Constanza Quintero, Willy Dillen, Riet De Rycke, Jose Flower Valor, Janniek De Clercq, Marc Van Montagu, Geert AngenonAbstract:Arcelins are abundant seed storage proteins thought to be implicated in the resistance of wild Phaseolus vulgaris (L.) genotypes against Zabrotes subfasciatus (Boheman), an important storage insect pest of common bean. Here, the insecticidal activity of the Arcelin-5 variant that is present in the highly resistant P. vulgaris accession G02771 was investigated. No correlation could be established between the presence of Arcelin 5 and the insecticidal effects observed in G02771 seeds. Insect feeding assays with artificial seeds into which purified Arcelin-5 protein was incorporated and with transgenic P, acutifolius (A, Gray) seeds in which the Arcelin-5 genes were expressed, showed that the presence of Arcelin-5 proteins, even at elevated levels, was not sufficient to achieve adequate resistance against Z. subfasciatus, The same might apply to other Arcelin variants. Nevertheless, as resistance is clearly closely linked to the presence of the Arcelin-1 or Arcelin-5 locus, Arcelins remain useful markers in breeding programmes aimed at introgressing high levels of resistance to Z. subfasciatus in P. vulgaris cultivars.
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the Arcelin 5 gene of phaseolus vulgaris directs high seed specific expression in transgenic phaseolus acutifolius and arabidopsis plants
Plant Physiology, 1999Co-Authors: Alain Goossens, Willy Dillen, Janniek De Clercq, Marc Van Montagu, Geert AngenonAbstract:The regulatory sequences of many genes encoding seed storage proteins have been used to drive seed-specific expression of a variety of proteins in transgenic plants. Because the levels at which these transgene-derived proteins accumulate are generally quite low, we investigated the utility of the Arcelin-5 regulatory sequences in obtaining high seed-specific expression in transgenic plants. Arcelin-5 is an abundant seed protein found in some wild common bean (Phaseolus vulgaris L.) genotypes. Seeds of Arabidopsis and Tepary bean (Phaseolus acutifolius A. Gray) plants transformed with Arcelin-5 gene constructs synthesized Arcelin-5 to levels of 15% and 25% of the total protein content, respectively. To our knowledge, such high expression levels directed by a transgene have not been reported before. The transgenic plants also showed low plant-to-plant variation in Arcelin expression. Complex transgene integration patterns, which often result in gene silencing effects, were not associated with reduced Arcelin-5 expression. High transgene expression was the result of high mRNA steady-state levels and was restricted to seeds. This indicates that all requirements for high seed-specific expression are cis elements present in the cloned genomic Arcelin-5 sequence and trans-acting factors that are available in Arabidopsis and Phaseolus spp., and thus probably in most dicotyledonous plants.
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Crystal structure of Arcelin-5, a lectin-like defense protein from Phaseolus vulgaris
Journal of Biological Chemistry, 1996Co-Authors: Thomas Hamelryck, Lode Wyns, F. Poortmans, Geert Angenon, Alain Goossens, Marc Van Montagu, Remy LorisAbstract:Abstract In the seeds of the legume plants, a class of sugar-binding proteins with high structural and sequential identity is found, generally called the legume lectins. The seeds of the common bean (Phaseolus vulgaris) contain, besides two such lectins, a lectin-like defense protein called Arcelin, in which one sugar binding loop is absent. Here we report the crystal structure of Arcelin-5 (Arc5), one of the electrophoretic variants of Arcelin, solved at a resolution of 2.7 A. The R factor of the refined structure is 20.6%, and the free R factor is 27.1%. The main difference between Arc5 and the legume lectins is the absence of the metal binding loop. The bound metals are necessary for the sugar binding capabilities of the legume lectins and stabilize an Ala-Asp cis-peptide bond. Surprisingly, despite the absence of the metal binding site in Arc5, this cis-peptide bond found in all legume lectin structures is still present, although the Asp residue has been replaced by a Tyr residue. Despite the high identity between the different legume lectin sequences, they show a broad range of quaternary structures. The structures of three different dimers and three different tetramers have been solved. Arc5 crystallized as a monomer, bringing the number of known quaternary structures to seven.
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isolation and characterisation of Arcelin 5 proteins and cdnas
FEBS Journal, 1994Co-Authors: Alain Goossens, Marc Van Montagu, Roberto A Geremia, Guy Bauw, Geert AngenonAbstract:Arcelins are seed storage proteins present in some wild bean accessions (Phaseolus vulgaris). They are implicated in the resistance phenotype of these wild beans towards the Mexican bean weevil. Arcelin 5, one of six Arcelin electrophoretic variants, has been characterised in detail. The purified Arcelin-5 protein fraction contained two major polypeptides of 32.2 and 31.5 kDa, designated Arcelin 5a and Arcelin 5b, respectively, and one minor polypeptide of 30.8 kDa, designated Arcelin 5c. The three polypeptides have an identical isoelectric point and are identical for their first nine N-terminal amino acids. Arcelin 5a and Arcelin 5b are glycoproteins whereas Arcelin 5c is not glycosylated. Native Arcelin 5 has a molecular mass corresponding to a dimer form. Using amino acid sequence analysis and PCR techniques, two different Arcelin-5 cDNA sequences were obtained, designated arc5-I and arc5-II. Both encode proteins of 261 amino acids with a signal peptide of 21 amino acids. The identity between the two is 99% at the DNA level and 97% at the level of the deduced amino acid sequences. The arc5-I and arc5-II cDNAs encode Arcelin 5a and Arcelin 5b, respectively. Sequence comparisons and protein characteristics show clearly that Arcelin 5 is related to, but distinct from, other Arcelin variants and lectins of P. vulgaris.
Alain Goossens - One of the best experts on this subject based on the ideXlab platform.
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The Arcelin-5 Gene of Phaseolus vulgaris Directs High Seed-Specific Expression in Transgenic Phaseolus acutifolius and Arabidopsis Plants 1
2013Co-Authors: Alain Goossens, Geert Angenon, Willy Dillen, Janniek De Clercq, Marc Van Montagu, Laboratorium Voor GeneticaAbstract:The regulatory sequences of many genes encoding seed storage proteins have been used to drive seed-specific expression of a variety of proteins in transgenic plants. Because the levels at which these transgene-derived proteins accumulate are generally quite low, we investigated the utility of the Arcelin-5 regulatory sequences in obtaining high seed-specific expression in transgenic plants. Arcelin-5 is an abundant seed protein found in some wild common bean (Phaseolus vulgaris L.) genotypes. Seeds of Arabidopsis and Tepary bean (Phaseolus acutifolius A. Gray) plants transformed with Arcelin-5 gene constructs synthesized Arcelin-5 to levels of 15 % and 25 % of the total protein content, respectively. To our knowledge, such high expression levels directed by a transgene have not been reported before. The transgenic plants also showed low plant-to-plant variation in Arcelin expression. Complex transgene integration patterns, which often result in gene silencing effects
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Analysis of bruchid resistance in the wild common bean accession G02771: no evidence for insecticidal activity of Arcelin 5
Journal of Experimental Botany, 2000Co-Authors: Alain Goossens, Cesar Cardona, Constanza Quintero, Willy Dillen, Riet De Rycke, Jose Flower Valor, Janniek De Clercq, Marc Van Montagu, Geert AngenonAbstract:Arcelins are abundant seed storage proteins thought to be implicated in the resistance of wild Phaseolus vulgaris (L.) genotypes against Zabrotes subfasciatus (Boheman), an important storage insect pest of common bean. Here, the insecticidal activity of the Arcelin-5 variant that is present in the highly resistant P. vulgaris accession G02771 was investigated. No correlation could be established between the presence of Arcelin 5 and the insecticidal effects observed in G02771 seeds. Insect feeding assays with artificial seeds into which purified Arcelin-5 protein was incorporated and with transgenic P, acutifolius (A, Gray) seeds in which the Arcelin-5 genes were expressed, showed that the presence of Arcelin-5 proteins, even at elevated levels, was not sufficient to achieve adequate resistance against Z. subfasciatus, The same might apply to other Arcelin variants. Nevertheless, as resistance is clearly closely linked to the presence of the Arcelin-1 or Arcelin-5 locus, Arcelins remain useful markers in breeding programmes aimed at introgressing high levels of resistance to Z. subfasciatus in P. vulgaris cultivars.
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the Arcelin 5 gene of phaseolus vulgaris directs high seed specific expression in transgenic phaseolus acutifolius and arabidopsis plants
Plant Physiology, 1999Co-Authors: Alain Goossens, Willy Dillen, Janniek De Clercq, Marc Van Montagu, Geert AngenonAbstract:The regulatory sequences of many genes encoding seed storage proteins have been used to drive seed-specific expression of a variety of proteins in transgenic plants. Because the levels at which these transgene-derived proteins accumulate are generally quite low, we investigated the utility of the Arcelin-5 regulatory sequences in obtaining high seed-specific expression in transgenic plants. Arcelin-5 is an abundant seed protein found in some wild common bean (Phaseolus vulgaris L.) genotypes. Seeds of Arabidopsis and Tepary bean (Phaseolus acutifolius A. Gray) plants transformed with Arcelin-5 gene constructs synthesized Arcelin-5 to levels of 15% and 25% of the total protein content, respectively. To our knowledge, such high expression levels directed by a transgene have not been reported before. The transgenic plants also showed low plant-to-plant variation in Arcelin expression. Complex transgene integration patterns, which often result in gene silencing effects, were not associated with reduced Arcelin-5 expression. High transgene expression was the result of high mRNA steady-state levels and was restricted to seeds. This indicates that all requirements for high seed-specific expression are cis elements present in the cloned genomic Arcelin-5 sequence and trans-acting factors that are available in Arabidopsis and Phaseolus spp., and thus probably in most dicotyledonous plants.
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Crystal structure of Arcelin-5, a lectin-like defense protein from Phaseolus vulgaris
Journal of Biological Chemistry, 1996Co-Authors: Thomas Hamelryck, Lode Wyns, F. Poortmans, Geert Angenon, Alain Goossens, Marc Van Montagu, Remy LorisAbstract:Abstract In the seeds of the legume plants, a class of sugar-binding proteins with high structural and sequential identity is found, generally called the legume lectins. The seeds of the common bean (Phaseolus vulgaris) contain, besides two such lectins, a lectin-like defense protein called Arcelin, in which one sugar binding loop is absent. Here we report the crystal structure of Arcelin-5 (Arc5), one of the electrophoretic variants of Arcelin, solved at a resolution of 2.7 A. The R factor of the refined structure is 20.6%, and the free R factor is 27.1%. The main difference between Arc5 and the legume lectins is the absence of the metal binding loop. The bound metals are necessary for the sugar binding capabilities of the legume lectins and stabilize an Ala-Asp cis-peptide bond. Surprisingly, despite the absence of the metal binding site in Arc5, this cis-peptide bond found in all legume lectin structures is still present, although the Asp residue has been replaced by a Tyr residue. Despite the high identity between the different legume lectin sequences, they show a broad range of quaternary structures. The structures of three different dimers and three different tetramers have been solved. Arc5 crystallized as a monomer, bringing the number of known quaternary structures to seven.
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isolation and characterisation of Arcelin 5 proteins and cdnas
FEBS Journal, 1994Co-Authors: Alain Goossens, Marc Van Montagu, Roberto A Geremia, Guy Bauw, Geert AngenonAbstract:Arcelins are seed storage proteins present in some wild bean accessions (Phaseolus vulgaris). They are implicated in the resistance phenotype of these wild beans towards the Mexican bean weevil. Arcelin 5, one of six Arcelin electrophoretic variants, has been characterised in detail. The purified Arcelin-5 protein fraction contained two major polypeptides of 32.2 and 31.5 kDa, designated Arcelin 5a and Arcelin 5b, respectively, and one minor polypeptide of 30.8 kDa, designated Arcelin 5c. The three polypeptides have an identical isoelectric point and are identical for their first nine N-terminal amino acids. Arcelin 5a and Arcelin 5b are glycoproteins whereas Arcelin 5c is not glycosylated. Native Arcelin 5 has a molecular mass corresponding to a dimer form. Using amino acid sequence analysis and PCR techniques, two different Arcelin-5 cDNA sequences were obtained, designated arc5-I and arc5-II. Both encode proteins of 261 amino acids with a signal peptide of 21 amino acids. The identity between the two is 99% at the DNA level and 97% at the level of the deduced amino acid sequences. The arc5-I and arc5-II cDNAs encode Arcelin 5a and Arcelin 5b, respectively. Sequence comparisons and protein characteristics show clearly that Arcelin 5 is related to, but distinct from, other Arcelin variants and lectins of P. vulgaris.
Oriani, Maria A. De G. - One of the best experts on this subject based on the ideXlab platform.
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Preferência para oviposição de Bemisia tabaci (Genn.) biótipo B (Homoptera: Aleyrodidae) por genótipos de feijoeiros portadores de Arcelina nas sementes
Sociedade Entomológica do Brasil, 2000Co-Authors: Oriani, Maria A. De G., Lara, Fernando M.Abstract:The oviposition preference of Bemisia tabaci biotype B (Homoptera: Aleyrodidae) for bean (Phaseolus vulgaris L.) genotypes containing Arcelin in the seeds was evaluated. The tests were carried out under greenhouse conditions, in the dry and wet seasons, with the following genotypes: ARC 3s, ARC 5s (wild genotypes containing Arcelin in the seeds); ARC 1, ARC 2, ARC 3, ARC 4 (near isogenic lines containing Arcelin in the seeds - EMBRAPA) and Porrillo 70, Bolinha, IAPAR MD 808 (commercial genotypes without Arcelin). In the free choice and no-choice oviposition tests, Bolinha and Porrillo 70 genotypes were preferred for oviposition by that insect. The Bolinha susceptibility could be related to the great number of acicular trichomes presents on its leaves surface. The wild genotypes, ARC 5s and ARC 3s, showed oviposition nonpreference resistance type. This resistance is not related to the Arcelin variants, since the bred genotypes also contain Arcelin in its seeds and did not show resistance to B. tabaci, biotype B.Genótipos de feijoeiro (P. vulgaris) que contêm Arcelina em suas sementes foram avaliados quanto à preferência para oviposição de Bemisia tabaci biótipo B (Homoptera: Aleyrodidae). Os testes foram conduzidos em condições de estufa, nas épocas "das águas" e "da seca", em dois anos consecutivos, com os seguintes genótipos: ARC 3s, ARC 5s (genótipos selvagens portadores de Arcelina); ARC 1, ARC 2, ARC 3, ARC 4 (linhagens quase-isogênicas portadoras de Arcelina - EMBRAPA), Porrillo 70, Bolinha e IAPAR MD 808 (cultivares sem Arcelina). Nos ensaios de preferência para oviposição, em teste com e sem chance de escolha, observou-se que os genótipos Bolinha e Porrillo 70 foram os mais preferidos para oviposição pelo inseto. A suscetibilidade do genótipo Bolinha pode estar relacionada com o grande número de tricomas aciculares presentes em suas folhas. Os genótipos selvagens, ARC 5s e ARC 3s, apresentaram resistência do tipo não-preferência para oviposição. Esta resistência não está relacionada com a Arcelina, uma vez que os genótipos melhorados também contêm Arcelina em suas sementes e não mostraram-se resistentes a esse biótipo de B. tabaci
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Preferência para oviposição de Bemisia tabaci (Genn.) biótipo B (Homoptera: Aleyrodidae) por genótipos de feijoeiros portadores de Arcelina nas sementes
Sociedade Entomológica do Brasil, 2000Co-Authors: Oriani, Maria A. De G., Lara, Fernando Mesquita [unesp]Abstract:Genótipos de feijoeiro (P. vulgaris) que contêm Arcelina em suas sementes foram avaliados quanto à preferência para oviposição de Bemisia tabaci biótipo B (Homoptera: Aleyrodidae). Os testes foram conduzidos em condições de estufa, nas épocas das águas e da seca, em dois anos consecutivos, com os seguintes genótipos: ARC 3s, ARC 5s (genótipos selvagens portadores de Arcelina); ARC 1, ARC 2, ARC 3, ARC 4 (linhagens quase-isogênicas portadoras de Arcelina - Empresa Brasileira de Pesquisa Agropecuária (EMBRAPA)), Porrillo 70, Bolinha e IAPAR MD 808 (cultivares sem Arcelina). Nos ensaios de preferência para oviposição, em teste com e sem chance de escolha, observou-se que os genótipos Bolinha e Porrillo 70 foram os mais preferidos para oviposição pelo inseto. A suscetibilidade do genótipo Bolinha pode estar relacionada com o grande número de tricomas aciculares presentes em suas folhas. Os genótipos selvagens, ARC 5s e ARC 3s, apresentaram resistência do tipo não-preferência para oviposição. Esta resistência não está relacionada com a Arcelina, uma vez que os genótipos melhorados também contêm Arcelina em suas sementes e não mostraram-se resistentes a esse biótipo de B. tabaci.The oviposition preference of Bemisia tabaci biotype B (Homoptera: Aleyrodidae) for bean (Phaseolus vulgaris L.) genotypes containing Arcelin in the seeds was evaluated. The tests were carried out under greenhouse conditions, in the dry and wet seasons, with the following genotypes: ARC 3s, ARC 5s (wild genotypes containing Arcelin in the seeds); ARC 1, ARC 2, ARC 3, ARC 4 (near isogenic lines containing Arcelin in the seeds - Empresa Brasileira de Pesquisa Agropecuária (EMBRAPA)) and Porrillo 70, Bolinha, IAPAR MD 808 (commercial genotypes without Arcelin). In the free choice and no-choice oviposition tests, Bolinha and Porrillo 70 genotypes were preferred for oviposition by that insect. The Bolinha susceptibility could be related to the great number of acicular trichomes presents on its leaves surface. The wild genotypes, ARC 5s and ARC 3s, showed oviposition nonpreference resistance type. This resistance is not related to the Arcelin variants, since the bred genotypes also contain Arcelin in its seeds and did not show resistance to B. tabaci, biotype B
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Oviposition preference of Bemisia tabaci (Genn.) biotype B (Homoptera: Aleyrodidae) for bean genotypes containing Arcelin in the seeds
Sociedade Entomológica do Brasil, 2000Co-Authors: Oriani, Maria A. De G., Lara, Fernando MesquitaAbstract:Genótipos de feijoeiro (P. vulgaris) que contêm Arcelina em suas sementes foram avaliados quanto à preferência para oviposição de Bemisia tabaci biótipo B (Homoptera: Aleyrodidae). Os testes foram conduzidos em condições de estufa, nas épocas das águas e da seca, em dois anos consecutivos, com os seguintes genótipos: ARC 3s, ARC 5s (genótipos selvagens portadores de Arcelina); ARC 1, ARC 2, ARC 3, ARC 4 (linhagens quase-isogênicas portadoras de Arcelina - Empresa Brasileira de Pesquisa Agropecuária (EMBRAPA)), Porrillo 70, Bolinha e IAPAR MD 808 (cultivares sem Arcelina). Nos ensaios de preferência para oviposição, em teste com e sem chance de escolha, observou-se que os genótipos Bolinha e Porrillo 70 foram os mais preferidos para oviposição pelo inseto. A suscetibilidade do genótipo Bolinha pode estar relacionada com o grande número de tricomas aciculares presentes em suas folhas. Os genótipos selvagens, ARC 5s e ARC 3s, apresentaram resistência do tipo não-preferência para oviposição. Esta resistência não está relacionada com a Arcelina, uma vez que os genótipos melhorados também contêm Arcelina em suas sementes e não mostraram-se resistentes a esse biótipo de B. tabaci.The oviposition preference of Bemisia tabaci biotype B (Homoptera: Aleyrodidae) for bean (Phaseolus vulgaris L.) genotypes containing Arcelin in the seeds was evaluated. The tests were carried out under greenhouse conditions, in the dry and wet seasons, with the following genotypes: ARC 3s, ARC 5s (wild genotypes containing Arcelin in the seeds); ARC 1, ARC 2, ARC 3, ARC 4 (near isogenic lines containing Arcelin in the seeds - Empresa Brasileira de Pesquisa Agropecuária (EMBRAPA)) and Porrillo 70, Bolinha, IAPAR MD 808 (commercial genotypes without Arcelin). In the free choice and no-choice oviposition tests, Bolinha and Porrillo 70 genotypes were preferred for oviposition by that insect. The Bolinha susceptibility could be related to the great number of acicular trichomes presents on its leaves surface. The wild genotypes, ARC 5s and ARC 3s, showed oviposition nonpreference resistance type. This resistance is not related to the Arcelin variants, since the bred genotypes also contain Arcelin in its seeds and did not show resistance to B. tabaci, biotype B.Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq
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Efeitos antibióticos de genótipos de feijoeiros portadores de Arcelina nas sementes sobre Bemisia tabaci (Genn.) biótipo B (Homoptera: Aleyrodidae)
Sociedade Entomológica do Brasil, 2000Co-Authors: Oriani, Maria A. De G., Lara, Fernando M.Abstract:The biology of Bemisia tabaci biotype B (Genn.) on bean (Phaseolus vulgaris L.) genotypes containing Arcelin in the seeds was evaluated. Also, biochemical screening of seeds and leaves material of these genotypes were carried out in order to verify if traces of Arcelin could be found in its leaves. The tests were conducted under greenhouse conditions, in the dry and wet seasons, with the following genotypes: ARC 3s, ARC 5s (wild genotypes containing Arcelin in the seeds); ARC 1, ARC 2, ARC 3, ARC 4 (near isogenic lines containing Arcelin in the seeds - EMBRAPA) and Porrillo 70, Bolinha, IAPAR MD 808 (commercial genotypes without Arcelin). The wild genotypes, ARC 3s and ARC 5s, showed high levels of antibiosis resistance type, mainly for ARC 5s which presented the highest nymphs mortality rates, approximately 90%. Also, the longest development time for nymphs fed on ARC 5s genotype suggest antibiosis and/or feeding nonpreference resistance type. The wild genotype resistance is not related with Arcelin presence in the seeds, since no trace of this protein was found in its leaves.A biologia de Bemisia tabaci biótipo B (Genn.) foi avaliada em genótipos de feijoeiro (Phaseolus vulgaris L.) que contêm Arcelina em suas sementes. Foi também realizada análise bioquímica de proteínas, em sementes e em folhas dos genótipos de feijoeiro, a fim de verificar se haveria traços de Arcelina nas folhas dos materiais a serem avaliados. Os testes foram conduzidos em condições de casa de vegetação, nas épocas "das águas" e "da seca", em dois anos consecutivos, com os seguintes genótipos: ARC 3s, ARC 5s (genótipos selvagens portadores de Arcelina); ARC 1, ARC 2, ARC 3, ARC 4 (linhagens quase-isogênicas portadoras de Arcelina - EMBRAPA), Porrillo 70, Bolinha e IAPAR MD 808 (genótipos sem Arcelina). Os genótipos selvagens, ARC 3s e ARC 5s, apresentaram altos níveis de antibiose, com ênfase para o ARC 5s (as ninfas tiveram alta mortalidade, em torno de 90%). O prolongamento do ciclo de desenvolvimento dos insetos provenientes do genótipo ARC 5s podem sugerir uma resistência do tipo antibiose e/ou não-preferência para alimentação. A resistência dos genótipos selvagens não está relacionada com a presença de Arcelina nas sementes, já que nenhum traço dessa proteína foi encontrado nas folhas destes
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Efeitos antibióticos de genótipos de feijoeiros portadores de Arcelina nas sementes sobre Bemisia tabaci (Genn.) biótipo B (Homoptera: Aleyrodidae)
Sociedade Entomológica do Brasil, 2000Co-Authors: Oriani, Maria A. De G., Lara, Fernando Mesquita [unesp]Abstract:A biologia de Bemisia tabaci biótipo B (Genn.) foi avaliada em genótipos de feijoeiro (Phaseolus vulgaris L.) que contêm Arcelina em suas sementes. Foi também realizada análise bioquímica de proteínas, em sementes e em folhas dos genótipos de feijoeiro, a fim de verificar se haveria traços de Arcelina nas folhas dos materiais a serem avaliados. Os testes foram conduzidos em condições de casa de vegetação, nas épocas das águas e da seca, em dois anos consecutivos, com os seguintes genótipos: ARC 3s, ARC 5s (genótipos selvagens portadores de Arcelina); ARC 1, ARC 2, ARC 3, ARC 4 (linhagens quase-isogênicas portadoras de Arcelina - Empresa Brasileira de Pesquisa Agropecuária (EMBRAPA)), Porrillo 70, Bolinha e IAPAR MD 808 (genótipos sem Arcelina). Os genótipos selvagens, ARC 3s e ARC 5s, apresentaram altos níveis de antibiose, com ênfase para o ARC 5s (as ninfas tiveram alta mortalidade, em torno de 90%). O prolongamento do ciclo de desenvolvimento dos insetos provenientes do genótipo ARC 5s podem sugerir uma resistência do tipo antibiose e/ou não-preferência para alimentação. A resistência dos genótipos selvagens não está relacionada com a presença de Arcelina nas sementes, já que nenhum traço dessa proteína foi encontrado nas folhas destes.The biology of Bemisia tabaci biotype B (Genn.) on bean (Phaseolus vulgaris L.) genotypes containing Arcelin in the seeds was evaluated. Also, biochemical screening of seeds and leaves material of these genotypes were carried out in order to verify if traces of Arcelin could be found in its leaves. The tests were conducted under greenhouse conditions, in the dry and wet seasons, with the following genotypes: ARC 3s, ARC 5s (wild genotypes containing Arcelin in the seeds); ARC 1, ARC 2, ARC 3, ARC 4 (near isogenic lines containing Arcelin in the seeds - Empresa Brasileira de Pesquisa Agropecuária (EMBRAPA)) and Porrillo 70, Bolinha, IAPAR MD 808 (commercial genotypes without Arcelin). The wild genotypes, ARC 3s and ARC 5s, showed high levels of antibiosis resistance type, mainly for ARC 5s which presented the highest nymphs mortality rates, approximately 90%. Also, the longest development time for nymphs fed on ARC 5s genotype suggest antibiosis and/or feeding nonpreference resistance type. The wild genotype resistance is not related with Arcelin presence in the seeds, since no trace of this protein was found in its leaves
S Janarthanan - One of the best experts on this subject based on the ideXlab platform.
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analysis on the Arcelin expression in bruchid pest resistant wild pulses using real time rt qpcr
Indian Journal of Experimental Biology, 2014Co-Authors: Shanmugavel Sakthivelkumar, Velayutham Veeramani, Karuppiah Hilda, Munusamy Arumugam, S JanarthananAbstract:Arcelin, the antimetabolic protein from wild pulses is a known natural insecticidal molecule. Wild pulses with high Arcelin content could serve as potential source to. increase the levels of insect resistance in cultivated pulse crops. In this study, Arcelin (Arl) gene expression was screened in seven stored product insect pest resistant wild pulse varieties using real time RT-qPCR. Arcelin gene specific real time PCR primers were synthesized from Arcelin mRNA sequence of the wild pulse variety, Lablab purpureus. The results revealed different levels of Arcelin gene expression in the tested varieties. Canavalia virosa registered significantly high content indicating its suitability for utilization of Arcelin gene in developing stored product insect pest resistance with other cultivated pulses.
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diversity and analysis of sequences encoded by Arcelin genes from indian wild pulses resistant to bruchids
Process Biochemistry, 2013Co-Authors: Shanmugavel Sakthivelkumar, Velayutham Veeramani, Munusamy Arumugam, Michael Immanuel Jesse, Paulchamy Ramaraj, Krishnan Kathiravan, S JanarthananAbstract:Abstract Wild pulse accessions are considered a vital source of genes for insect resistance for crop improvement programmes. Wild pulses resistant to infestation towards the bruchid insect pest, Callosobruchus maculatus from South India were chosen to screen the existence of potent insecticidal protein, Arcelin from APA locus (Arcelin/Phytohemagglutinin/α-Amylase inhibitor) to ascertain their nature and functional diversity without any specific indication for insect resistant factors. The DNA sequence coding for Arcelin from various species of wild pulses were amplified, sequenced and deduced to their protein sequences. These protein sequences were examined physico-chemically using several bioinformatics tools and docked with various sugars to resolve the nature of Arcelin molecules. Results indicated the presence of significant differences in the properties of Arcelin molecules from various species of Indian wild pulses with their amino acid sequences, several physico-chemical properties and binding ability with sugars. The differences observed on these Arcelin molecules from diverse wild pulses are predicted to provide a prospective insect pest control factors.
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a new variant of antimetabolic protein Arcelin from an indian bean lablab purpureus linn and its effect on the stored product pest callosobruchus maculatus
Food Chemistry, 2012Co-Authors: S Janarthanan, Shanmugavel Sakthivelkumar, Velayutham Veeramani, Dixit Radhika, Subbaratnam MuthukrishananAbstract:The anti-metabolic or insecticidal gene, Arcelin (Arl) was isolated, cloned and sequenced using sequence specific degenerate primers from the seeds of Lablab purpureus collected from the Western Ghats, Tamil Nadu, India. The L. purpureus Arcelin nucleotide sequence was homologous to Arl-3 and Arl-4 alleles from Phaseolus spp. The protein it encodes has 70% amino acid identity with the amino acid sequences of Arl-3I, Arl-3III, Arl-4 precursor, Arl-4 and Arl-4I. The partially purified Arcelin from the seeds of L. purpureus using an artificial diet confirmed the complete retardation of development of the stored product pest Callosobruchus maculatus at 0.2% w/w Arcelin-incorporated artificial seeds.
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Prediction of putative binding pocket for carbohydrates docking in computed model of an insecticidal lectin-like protein, Arcelin from Indian wild pulse Lablab purpureus
2011Co-Authors: Nagarajan Arumugam, Velayutham Veeramani, Shanmugavel Sakthivelkumar, S JanarthananAbstract:Protein-carbohydrate recognition is a most important form of inter-cell communication that performs key role in many biologically significant processes. The legume lectin family has served as a model system for proteincarbohydrate interactions for several decades. Although there were extensive studies in the protein-carbohydrate recognition using legume lectin molecules, specific studies are not available for legume lectin-like proteins called Arcelin. In this study, an attempt was made to reveal the identification of potential carbohydrate binding pocket using different carbohydrates in refined computed model of Arcelin isolated from wild legume seed, Lablab purpureus. The four methods viz., LIGSITEcs, PASS, Q-SiteFinder and SURFNET through Meta Pocket Server was used to identify the potential carbohydrate binding pocket for suitable ligand docking. The docking studies revealed that chitotriose (-11.37Kcal/Mol) produced more affinity towards the computed model of L. purpureus Arcelin. The identified ligand-chitotriose would thus act as inducer for the molecular action of Arcelin. This prediction provides development of potential transgenic L.purpureus plant with Arcelin and Chitotriose synthesizing gene for Integrated Pest Management Programme (IPM) against bruchid larvae.
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toxicity assessment of wild bean seed protein Arcelin on asian armyworm spodoptera litura fabricius
Indian Journal of Experimental Biology, 2003Co-Authors: B Malaikozhundan, P Suresh, S Seshadri, S JanarthananAbstract:Arcelin, an anti-metabolic protein was purified from the seeds of wild bean, Lablab purpureus. The feeding assay containing Arcelin at 5, 10 and 15 microg concentrations revealed no antifeedant effect against fifth instar larvae of S. litura. However, the enhanced activity of alpha- and beta-naphthyl esterases in the mid-gut samples of S. litura treated with Arcelin suggests countermeasure against the toxic effect of Arcelin.
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The Arcelin-5 Gene of Phaseolus vulgaris Directs High Seed-Specific Expression in Transgenic Phaseolus acutifolius and Arabidopsis Plants 1
2013Co-Authors: Alain Goossens, Geert Angenon, Willy Dillen, Janniek De Clercq, Marc Van Montagu, Laboratorium Voor GeneticaAbstract:The regulatory sequences of many genes encoding seed storage proteins have been used to drive seed-specific expression of a variety of proteins in transgenic plants. Because the levels at which these transgene-derived proteins accumulate are generally quite low, we investigated the utility of the Arcelin-5 regulatory sequences in obtaining high seed-specific expression in transgenic plants. Arcelin-5 is an abundant seed protein found in some wild common bean (Phaseolus vulgaris L.) genotypes. Seeds of Arabidopsis and Tepary bean (Phaseolus acutifolius A. Gray) plants transformed with Arcelin-5 gene constructs synthesized Arcelin-5 to levels of 15 % and 25 % of the total protein content, respectively. To our knowledge, such high expression levels directed by a transgene have not been reported before. The transgenic plants also showed low plant-to-plant variation in Arcelin expression. Complex transgene integration patterns, which often result in gene silencing effects
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Analysis of bruchid resistance in the wild common bean accession G02771: no evidence for insecticidal activity of Arcelin 5
Journal of Experimental Botany, 2000Co-Authors: Alain Goossens, Cesar Cardona, Constanza Quintero, Willy Dillen, Riet De Rycke, Jose Flower Valor, Janniek De Clercq, Marc Van Montagu, Geert AngenonAbstract:Arcelins are abundant seed storage proteins thought to be implicated in the resistance of wild Phaseolus vulgaris (L.) genotypes against Zabrotes subfasciatus (Boheman), an important storage insect pest of common bean. Here, the insecticidal activity of the Arcelin-5 variant that is present in the highly resistant P. vulgaris accession G02771 was investigated. No correlation could be established between the presence of Arcelin 5 and the insecticidal effects observed in G02771 seeds. Insect feeding assays with artificial seeds into which purified Arcelin-5 protein was incorporated and with transgenic P, acutifolius (A, Gray) seeds in which the Arcelin-5 genes were expressed, showed that the presence of Arcelin-5 proteins, even at elevated levels, was not sufficient to achieve adequate resistance against Z. subfasciatus, The same might apply to other Arcelin variants. Nevertheless, as resistance is clearly closely linked to the presence of the Arcelin-1 or Arcelin-5 locus, Arcelins remain useful markers in breeding programmes aimed at introgressing high levels of resistance to Z. subfasciatus in P. vulgaris cultivars.
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the Arcelin 5 gene of phaseolus vulgaris directs high seed specific expression in transgenic phaseolus acutifolius and arabidopsis plants
Plant Physiology, 1999Co-Authors: Alain Goossens, Willy Dillen, Janniek De Clercq, Marc Van Montagu, Geert AngenonAbstract:The regulatory sequences of many genes encoding seed storage proteins have been used to drive seed-specific expression of a variety of proteins in transgenic plants. Because the levels at which these transgene-derived proteins accumulate are generally quite low, we investigated the utility of the Arcelin-5 regulatory sequences in obtaining high seed-specific expression in transgenic plants. Arcelin-5 is an abundant seed protein found in some wild common bean (Phaseolus vulgaris L.) genotypes. Seeds of Arabidopsis and Tepary bean (Phaseolus acutifolius A. Gray) plants transformed with Arcelin-5 gene constructs synthesized Arcelin-5 to levels of 15% and 25% of the total protein content, respectively. To our knowledge, such high expression levels directed by a transgene have not been reported before. The transgenic plants also showed low plant-to-plant variation in Arcelin expression. Complex transgene integration patterns, which often result in gene silencing effects, were not associated with reduced Arcelin-5 expression. High transgene expression was the result of high mRNA steady-state levels and was restricted to seeds. This indicates that all requirements for high seed-specific expression are cis elements present in the cloned genomic Arcelin-5 sequence and trans-acting factors that are available in Arabidopsis and Phaseolus spp., and thus probably in most dicotyledonous plants.
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isolation and characterisation of Arcelin 5 proteins and cdnas
FEBS Journal, 1994Co-Authors: Alain Goossens, Marc Van Montagu, Roberto A Geremia, Guy Bauw, Geert AngenonAbstract:Arcelins are seed storage proteins present in some wild bean accessions (Phaseolus vulgaris). They are implicated in the resistance phenotype of these wild beans towards the Mexican bean weevil. Arcelin 5, one of six Arcelin electrophoretic variants, has been characterised in detail. The purified Arcelin-5 protein fraction contained two major polypeptides of 32.2 and 31.5 kDa, designated Arcelin 5a and Arcelin 5b, respectively, and one minor polypeptide of 30.8 kDa, designated Arcelin 5c. The three polypeptides have an identical isoelectric point and are identical for their first nine N-terminal amino acids. Arcelin 5a and Arcelin 5b are glycoproteins whereas Arcelin 5c is not glycosylated. Native Arcelin 5 has a molecular mass corresponding to a dimer form. Using amino acid sequence analysis and PCR techniques, two different Arcelin-5 cDNA sequences were obtained, designated arc5-I and arc5-II. Both encode proteins of 261 amino acids with a signal peptide of 21 amino acids. The identity between the two is 99% at the DNA level and 97% at the level of the deduced amino acid sequences. The arc5-I and arc5-II cDNAs encode Arcelin 5a and Arcelin 5b, respectively. Sequence comparisons and protein characteristics show clearly that Arcelin 5 is related to, but distinct from, other Arcelin variants and lectins of P. vulgaris.