Comparative value of four arcelin variants in the development of dry bean lines resistant to the Mexican bean weevil

Cardona, César; Kornegay, Julia L.; Posso, Carmen Elisa; Morales, Francisco J.; Ramírez, Hernando

doi:10.1111/j.1570-7458.1990.tb01397.x

Cited by 104 publications

(88 citation statements)

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“…Each arcelin variant is composed of several polypeptides presumably encoded by a family of different genes (Hartweck, Vogelzang, & Osborn, 1991). The importance of arcelin in the present perspective is its insecticidal property and in particular their inhibitory activity on larval development in stored product pests (Cardona, Kornegay, Posso, Morales, & Ramirez, 1990;Janarthanan & Suresh, 2003;Janarthanan et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

A new variant of antimetabolic protein, arcelin from an Indian bean, Lablab purpureus (Linn.) and its effect on the stored product pest, Callosobruchus maculatus

Janarthanan¹,

Sakthivelkumar²,

Veeramani³

et al. 2012

Food Chemistry

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Section: Introductionmentioning

confidence: 99%

A new variant of antimetabolic protein, arcelin from an Indian bean, Lablab purpureus (Linn.) and its effect on the stored product pest, Callosobruchus maculatus

Janarthanan¹,

Sakthivelkumar²,

Veeramani³

et al. 2012

Food Chemistry

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“…Certain wild accessions of common beans are resistant to Z. subfasciatus and several groups have introgressed this resistance into cultivars by selecting for arcelin (Schoonhoven et al, 1983;Osborn et al, 1988;Cardona et al, 1990). Arcelin is not a single protein, but is classified as six electrophoretic variants (Osborn et al, 1986;Suzuki et al, 1995).…”

Section: Why Does Aai Not Play a Role In The Resistance Of Introgressmentioning

confidence: 99%

“…of this protein family, arcelin, is found only in wild accessions of the common bean, and the introgression of the arcelin gene(s) yields varieties that are resistant to Z. subfasciatus (Andreas et al, 1986;Osborn et al, 1986;Cardona et al, 1990). It appears that the larvae of A. obfectus and Z .…”

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Protective Mechanism of the Mexican Bean Weevil against High Levels of α--Amylase Inhibitor in the Common Bean

1996

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~The seeds of starchy grain legumes are an important staple in many countries, but as with other crops, insect pests can cause considerable crop losses. The postharvest damage done by larvae of bruchids (Co1eoptera:Bruchidae) can be quite extensive. Crops of the common bean (Pkaseolus vulgaris), the scarlet runner bean (Phaseoltis coccineus), and the tepary bean (Phaseolus acutifolius) can be severely damaged by the bean weevil (Acanthoscelides obtectus) and the Mexican bean weevil (Zabrotes subfasciatus) . This damage occurs ín spite of the presence in the seeds of a family of plant defense proteins that comprises PHA and aAI (see Chrispeels and Raikhel, 1991). The three Phaseolus species are not equally sensitive to the bruchids. For example, tepary bean is more resistant than common bean to the bean weevil (Shade et al., 1987).

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“…Although phytohemagglutinins from P. vulgaris did not provide protection to P. vulgaris predators, they did provide protection against seed-feeding pests of other Phaseolus species. Osborn et al (18) showed that arcelin-1 protected seeds against P. vulgaris pests and recently the four arcelin variants were found to be associated with different levels and types of resistance to the Mexican bean weevil or the common bean weevil (3,8). Characterization of arcelin variants and comparisons to each other as well as to PHA may aid in understanding specific host-pest interactions, thereby enabling plant breeders to plan an effective strategy to control bruchid pests.…”

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Characterization and Comparison of Arcelin Seed Protein Variants from Common Bean

Hartweck¹,

Vogelzang²,

Osborn³

1991

Plant Physiol.

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Four variants of arcelin, an insecticidal seed storage protein of bean, Phaseolus vulgaris L., were investigated. Each variant (arcelin-1, -2, -3, and -4) was purified, and solubilities and Mrs were determined. For arcelins-1, -2, and -4, the isoelectric points, hemagglutinating activities, immunological cross-reactivities, and N-terminal amino acid sequences were determined. On the basis of native and denatured M,s, the variants were classified as being composed of dimer protein (arcelin-2), tetramer protein (arcelins-3 and -4), or both dimer and tetramer proteins (arcelin-1). Although the dimer proteins (arcelins-ld and -2) could be distinguished by M,s and isoelectric points, they were identical for their first 37 N-terminal amino acids and had similar immunological cross-reactions, and bean lines containing these variants had a DNA restriction fragment in common. The tetramer proteins arcelin-It and arcelin-4 also could be distinguished from each other based on Mrs and isoelectric points; however, they had similar immunological cross-reactions and they were 77 to 93% identical for N-terminal amino acid composition. The similarities among arcelin variants, phytohemagglutinin, and a bean a-amylase inhibitor suggest that they are all encoded by related members of a lectin gene family.In screening 210 wild accessions from the common bean (Phaseolus vulgaris L.) germplasm collection, Schoonhoven and Cardona (22) found several accessions that had natural resistance to two important bruchid pests, the Mexican bean weevil (Zabrotes subfasciatus Boheman.) and the common bean weevil (Acanthoscelides obtectus Say.). It was later shown that most of these resistant wild accessions contained arcelin seed proteins that had never been observed in cultivated beans (19,21 Arcelin-1 is the most thoroughly characterized of the protein variants. Using artificial seeds reconstituted from bean flour with the addition of purified arcelin protein, arcelin-1 was shown to be the component of the wild lines that confers resistance to Z. subfasciatus (18). Arcelin and PHA isolated from an arcelin-1-containing line had similar solubility properties, subunit Mrs, deglycosylated Mrs, and amino acid compositions; however, they had very different isoelectric points, and PHA agglutinated native erythrocytes but arcelin agglutinated only Pronase-treated cells (20). These similarities and differences might be explained by the observation that the cDNA nucleotide-derived amino acid sequence of arcelin-1 is approximately 60% identical to PHA-E and PHA-L (18). Arcelin has one methionine (PHA-E and PHA-L have no methionine) and additional attached oligosaccharide residues (18, 20) that may affect the chemistry and conformation of the mature protein.Another difference between arcelin-1 and PHA concerns their effects on seed-feeding insects. Janzen et al. (11) proposed that phytohemagglutinins are involved in the specificity of host-insect interactions between Phaseolus species and seed-feeding predators. Although phytohemagglutinins from ...

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Comparative value of four arcelin variants in the development of dry bean lines resistant to the Mexican bean weevil

Cited by 104 publications

References 9 publications

A new variant of antimetabolic protein, arcelin from an Indian bean, Lablab purpureus (Linn.) and its effect on the stored product pest, Callosobruchus maculatus

A new variant of antimetabolic protein, arcelin from an Indian bean, Lablab purpureus (Linn.) and its effect on the stored product pest, Callosobruchus maculatus

Protective Mechanism of the Mexican Bean Weevil against High Levels of α--Amylase Inhibitor in the Common Bean

Characterization and Comparison of Arcelin Seed Protein Variants from Common Bean

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