[Identification of the common bean mosaic virus in the Ukraine].
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Microscopy, Electron↗
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[Biological behavior of protein fractions isolated from the common bean (Phaseolus vulgaris)].
The purpose of this study was to determine the factors responsible for the low digestibility of bean proteins. To this effect, protein fractions were isolated from black beans through sequential extraction with distilled water, 70% ethanol and 0.01 M sodium hydroxide. Since the amount of protein extracted with the solvents was very low, it was practically impossible to carry out its biological evaluation in rats. Therefore, the protein fractions were added to casein diets in order to determine the decrease in casein digestibility due to the particular protein fraction added. The extracts and residues were heated and dehydrated prior to their incorporation in the rations. Nine rations were prepared. The first one was the control with casein only; 20% of whole bean flour was added to the 2nd; rations 3, 4 and 5 contained the water extraction residue, the water extract, and both, respectively; rations 6, 7 and 8 contained the ethanolic residue, the ethanol extract, and both, respectively. Finally, ration 9 was prepared with the NaOH residue. All the materials used as well as the rations were analyzed for their proximate composition and amino acid pattern. The results of the biological evaluation were as follows: casein and dry matter digestibility decreased significantly with the 2nd ration which contained 20% whole bean flour, effect which was significant also in rations containing either the water or the ethanol extract. This effect is attributed to the antiphysiological factors present in the beans which are resistant to heat treatment. The protein efficiency ratio was lower for the rations prepared with the residues from water and ethanol extractions (3 and 6) than for casein; these results are attributed to the lysine and methionine deficiency in the protein fractions, complicated by a lower protein intake. The lowest nutritive value was found in group 7, which was fed the ration containing the ethanol extract, but when the latter was added together with its residue (ration 8), the PER was superior than for ration 7, possibly due to a higher content of methionine and lysine in ration 8. Finally, it is suggested that better results could be obtained by using higher amounts of beans and their protein fractions in the ration.
Amino Acids↗
[Significance of various antiphysiological and nutritional factors on the biological evaluation of various cultures of the common bean (Phaseolus sp.)].
Raw and cooked samples of beans supplemented with methionine were used to prepare 35 rat diets containing different amounts of methionine, tannins, and trypsin inhibitors. The effect of these diets on weight gain, mortality and protein utilization was measured. The weight gain/protein consumption ratio increased while mortality decreased as the proportion of raw beans decreased in the diet. The effects of diet, beans and their interaction were significant. Supplementation with methionine had no effect in diets with high proportions of raw beans, but it had a significant effect on the biological response to diets with high proportions of cooked beans. The high and early mortality that occurred with diets with a high content of raw beans did not permit the adequate determination of apparent digestibility. In diets with a high concentration of cooked beans, digestibility was higher for white than for black or red beans. Since methionine supplementation had no effect on digestibility, it is suggested that heat-induced changes in the protein could be of great importance in the improvement of bean protein. At the same time, heat destroys the antiphysiological factors, since no definite detrimental effect was observed in the cooked samples due to these factors. It is concluded that the low nutritive value of cooked beans is due to a deficiency of sulfur-containing amino acids, and that the structure of the protein is a factor of the utmost importance in determining its digestibility.
Animals↗
[Possible relationship of physical, chemical and nutritional measurements of the common bean (Phaseolus vulgaris)].
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Amino Acids↗
Genetic and molecular characterization of the I locus of Phaseolus vulgaris.
The I locus of the common bean, Phaseolus vulgaris, controls the development of four different phenotypes in response to inoculation with Bean common mosaic virus, Bean common mosaic necrosis virus, several other related potyviruses, and one comovirus. We have generated a high-resolution linkage map around this locus and have aligned it with a physical map constructed with BAC clones. These clones were obtained from a library of the cultivar "Sprite," which carries the dominant allele at the I locus. We have identified a large cluster of TIR-NBS-LRR sequences associated within this locus, which extends over a distance >425 kb. Bean cultivars from the Andean or Mesoamerican gene pool that contain the dominant allele share the same haplotypes as revealed by gel blot hybridizations with a TIR probe. In contrast, beans with a recessive allele display simpler and variable haplotypes. A survey of wild accessions from Argentina to Mexico showed that this multigene family has expanded significantly during evolution and domestication. RNA gel blot analysis indicated that the TIR family of genes plays a role in the response to inoculations with BCMV or BCMNV.
Amino Acid Sequence↗
A genetic linkage map of Phaseolus vulgaris L. and localization of genes for specific resistance to six races of anthracnose (Colletotrichum lindemuthianum).
A genetic map of common bean was constructed using 197 markers including 152 RAPDs, 32 RFLPs, 12 SCARs, and 1 morphological marker. The map was established by using a F(2) population of 85 individuals from the cross between a line derived from the Spanish landrace Andecha (Andean origin) and the Mesoamerican genotype A252. The resulting map covers about 1,401.9 cM, with an average marker distance of 7.1 cM and includes molecular markers linked to disease resistance genes for anthracnose, bean common mosaic virus, bean golden yellow mosaic virus, common bacterial blight, and rust. Resistance to races 6, 31, 38, 39, 65, and 357 of the pathogenic fungus Colletotrichum lindemuthianum (anthracnose) was evaluated in F(3) families derived from the corresponding F(2) individuals. The intermediate resistance to race 65 proceeding from Andecha can be explained by a single dominant gene located on linkage group B1, corresponding to the Co-1 gene. The recombination between the resistance specificities proceeding from A252 agrees with the assumption that total resistance to races 6, 31, 38, 39, 65, and 357, is organized in two clusters. One cluster, located on B4 linkage group, includes individual genes for specific resistance to races 6, 38, 39, and 357. The second cluster is located on linkage group B11 and includes individual genes for specific resistance to races 6, 31, 38, 39, and 65. These two clusters correspond to genes Co-3/Co-9 and Co-2, respectively. It is concluded that most anthracnose resistance Co- genes, previously described as single major genes conferring resistance to several races, could be organized as clusters of different genes conferring race-specific resistance.
Chromosome Mapping↗
Specific expression in reproductive tissues and fate of a mitochondrial sterility-associated protein in cytoplasmic male-sterile bean.
In common bean, cytoplasmic male sterility has been associated with a unique sequence found in the mitochondrial genome, designated pvs (for Phaseolus vulgaris sterility sequence). Within the pvs sequence, two open reading frames are encoded, ORF98 and ORF239. We have raised rabbit polyclonal antibodies against Pvs-ORF239 to evaluate the role of this putative male sterility-associated protein. Histological investigation of pollen development revealed that in the male-sterile bean line, callose deposition was abnormal and microspores remained as tetrads as previously reported. Pvs-ORF239 was found to be localized within the reproductive tissues of the male-sterile bean line, in contrast to all other cytoplasmic male sterility systems studied to date. This protein was associated with mitochondria, the callose layer, and developing primary cell walls during microsporogenesis. Expression of pvs-orf239 was not detected in fertile plants containing restorer gene Fr2. These observations, together with previous reports, suggest that nuclear restorer gene Fr2 interferes with expression of the pvs region post-transcriptionally.
Animals↗
Diversity in the rhizobia associated with Phaseolus vulgaris L. in Ecuador, and comparisons with Mexican bean rhizobia.
Common beans (Phaseolus vulgaris L.) have centers of origin in both Mesoamerica and Andean South America, and have been domesticated in each region for perhaps 5000 years. A third major gene pool may exist in Ecuador and Northern Peru. The diversity of the rhizobia associated with beans has also been studied, but to date with an emphasis on the Mesoamerican center of origin. In this study we compared bean rhizobia from Mexico and Andean South America using both phenotypic and phylogenetic approaches. When differences between the rhizobia of these two regions were shown, we then examined the influence of bean cultivar on the most probable number (MPN) count and biodiversity of rhizobia recovered from different soils. Three clusters of bean rhizobia were distinguished using phenotypic analysis and principal-component analysis of Box AIR-PCR banding patterns. They corresponded principally to isolates from Mexico, and the northern and southern Andean regions, with isolates from southern Ecuador exhibiting significant genetic diversity. Rhizobia from Dalea spp., which are infective and effective on beans, may have contributed to the apparent diversity of rhizobia recovered from the Mesoamerican region, while the rhizobia of wild Phaseolus aborigineus from Argentina showed only limited similarity to the other bean rhizobia tested. Use of P. vulgaris cultivars from the Mesoamerican and Andean Phaseolus gene pools as trap hosts did not significantly affect MPN counts of bean rhizobia from the soils of each region, but did influence the diversity of the rhizobia recovered. Such differences in compatibility of host and Rhizobium could be a factor in the poor reputation for nodulation and N2 fixation in this crop.
Colony Count, Microbial↗
The use of nitrogen-15 labeling for the assessment of leguminous protein digestibility.
This study evaluated the digestibility of leguminous protein labeled with 15N, by using nitrogen balance and quantitation of fecal endogenous nitrogen (FEN), determined by isotopic dilution, in order to correct apparent values. Seeds of common beans, cowpea and common pea labeled with 1.000 atoms% of 15N-excess were used as protein sources in diets for 60 male Wistar rats, during a 6-day assay. The real digestibility values obtained with FEN were 77.6, 84.4, and 86.3% for common beans, cowpea and common pea, respectively. They were higher and statistically different (p < 0.05) than true digestibility values, corrected by non-protein diet. FEN showed a direct, moderate and positive relation with weight of dry matter eaten, initial body weight, weight gain and weight of dry matter of feces, the latter showing the highest correlation, with a coefficient r = 0.8930 at 1% level.
Absorption↗
The diversity of rhizobia nodulating beans in Northwest Argentina as a source of more efficient inoculant strains.
The common bean (Phaseolus vulgaris L.) is cultivated widely in Central and South America and particularly in the Northwest of Argentina. In order to describe the diversity of the common bean nodulating rhizobial population from the bean producing area in Northwest Argentina (NWA), a collection of about 400 isolates of common beans recovered from nodules and soil samples from NWA were characterized by using nifH-PCR, analysis of genes coding for 16S rRNA and nodC, and REP-fingerprinting, respectively. It was found that species Rhizobium etli is predominant in common bean nodules although a high degree of diversity was found within the species. Other bean nodulating genotypes recovered from soils by using Leucaena sp. as the trapping host was found to have the 16S rDNA alleles of species such as Sinorhizobium fredii, Sinorhizobium saheli, Sinorhizobium teranga, Mesorhizobium loti, and Rhizobium tropici. Some of the bean genotypes that were found to be more efficient in green house experiments were selected and assayed in two successive bean-cropping seasons in the field environment in NWA, and an increase in yields with inoculation was found. The performance of strains isolated from the region indicates potential for exploiting the diversity.
Argentina↗
Impact of microwave heating on hemagglutinins, trypsin inhibitors and protein quality of selected legume seeds.
Selected legume seeds (dry and soaked) including faba beans, peas, chickpeas, soybeans, lentils and common beans containing 8 and 25% moisture, respectively, were subjected to microwave heating, and to a conventional cooking method to determine the heating effect on toxic compounds and protein quality. Trypsin inhibitors, hemagglutinins and available lysine were analyzed, and laboratory rats were used to determine digestibility and protein efficiency ratio (PER). Results indicated that microwaving destroyed trypsin inhibitors to a similar degree to that observed in beans cooked using the conventional method without affecting PER for raw seeds with low antinutrients content (faba beans, peas, chickpeas and lentils). Microwave-heated soaked soybeans had a higher amount of destroyed trypsin inhibitors, along with a higher PER, compared with microwave-heated dry soybeans. Microwave heating of common beans failed to destroy hemagglutinins and trypsin inhibitors, and consequently their digestibility and PER values were poor. Finally it was concluded that microwave heating constitutes an adequate method for destroying hemagglutinins and trypsin inhibitors without affecting protein quality of most legume seeds, except for common beans that despite of this process retained the antinutritional substances.
Animals↗
Inhibitors of animal cell-free protein synthesis from grains.
We described earlier the purification and properties of a protein (tritin) from wheat that enzymatically inhibits translation in cell-free systems from animals but not plants. In this report, we have examined 11 additional grains (Family Gramineae) and three other seeds for the presence of tritin-like proteins. In addition to wheat species, barley, oats, rye, triticale and corn were found to be sources of inhibitor; no inhibitor could be detected in rice, millet, sesame, alfalfa, mung bean or common bean seeds. The inhibitors from barley and rye were purified and found to differ from tritin with respect to heat inactivation, although they are similar to tritin with respect to molecular weight, behavior during purification and specific activity. The inhibitor from corn was purified and found to differ from tritin with respect to heat inactivation and molecular weight, although it is similar to tritin in behavior during purification and specific activity. These inhibitors constitute 2-17% of the total extractable protein in these grains. Thus, wheat, barley, rye and corn can serve as convenient sources of a family of closely related inhibitors of protein synthesis which, when conjugated with lectins, antibodies, or hormones, could prove useful as chimeric toxins.
Animals↗
Perspectives into factors limiting in vivo digestion of legume proteins: antinutritional compounds or storage proteins?
The in vivo protein digestibility of raw and cooked common bean (Phaseolus vulgaris L.) and faba bean (Vicia faba L.) and of protein fractions extracted from them was determined with growing rats. Overnight-fasted rats were intubated with a protein suspension or fed the same amount of protein added to a basal diet. The rats were killed 1 h later, the contents of stomach and small intestine were washed out, and their protein contents were measured. The in vivo digestibility of proteins of raw common bean flour was 72.4% and not significantly improved after cooking. In contrast, the digestibility of faba bean proteins was decreased from 86.5 to 60.6% by the thermal treatment. Globulins from either species had similar digestibilities (approximately 70%). Proteins in the soluble fraction of cooked beans were more digestible than those in the insoluble fraction, which contained the bulk of the proteins. Hemagglutination assay and trypsin inhibitor determination indicated that after the thermal treatment only very low, nonharmful, levels of both lectin and inhibitor remained. Faba bean contained more polyphenols than common bean samples, with most of the polyphenols being bound to globulins. However, protein-bound polyphenols were markedly decreased after cooking. SDS-PAGE characterization of the gastrointestinal digesta of globulins and amino acid analysis of undigested proteins of whole cooked common bean and faba bean suggested that it is mainly the structural properties of the storage proteins and not their binding of polyphenols, which determines the extent of protein aggregation on autoclaving and may therefore be responsible for their low digestibility.
Animals↗
Salt-tolerant rhizobia isolated from a Tunisian oasis that are highly effective for symbiotic N2-fixation with Phaseolus vulgaris constitute a novel biovar (bv. mediterranense) of Sinorhizobium meliloti.
Nodulation of common bean was explored in six oases in the south of Tunisia. Nineteen isolates were characterized by PCR-RFLP of 16S rDNA. Three species of rhizobia were identified, Rhizobium etli, Rhizobium gallicum and Sinorhizobium meliloti. The diversity of the symbiotic genes was then assessed by PCR-RFLP of nodC and nifH genes. The majority of the symbiotic genotypes were conserved between oases and other soils of the north of the country. Sinorhizobia isolated from bean were then compared with isolates from Medicago truncatula plants grown in the oases soils. All the nodC types except for nodC type p that was specific to common bean isolates were shared by both hosts. The four isolates with nodC type p induced N(2)-fixing effective nodules on common bean but did not nodulate M. truncatula and Medicago sativa. The phylogenetic analysis of nifH and nodC genes showed that these isolates carry symbiotic genes different from those previously characterized among Medicago and bean symbionts, but closely related to those of S. fredii Spanish and Tunisian isolates effective in symbiosis with common bean but unable to nodulate soybean. The creation of a novel biovar shared by S. meliloti and S. fredii, bv. mediterranense, was proposed.
DNA, Bacterial↗
Fractionation of phosphorus and trace elements species in soybean flour and common white bean seeds by size exclusion chromatography-inductively coupled plasma mass spectrometry.
Soluble species of phosphorus, sulfur, selenium and eight metals (Mn, Fe, Co, Ni, Cu, Zn, Mo and Cd) in soybean flour and common white bean seeds were investigated by size exclusion chromatography (SEC) and inductively coupled plasma mass spectrometry (ICP-MS). Samples were extracted by 0.02 mol l(-1) Tris-HCI buffer solution (pH 7.5). Fractionation of sample extracts by preparative scale SEC was accomplished using a Fractogel EMD BioSEC column (600 x 16 mm) and 0.02 mol l(-1) Tris-HCl buffer solution (pH 7.5) as mobile phase (flow rate: 2 ml min(-1)). A 2-ml sample was injected. Contents of elements in chromatographic fractions were determined by AAS, ICP-AES and ICP-MS. The elution profiles of P, Fe, Co, Ni, Cu, Zn and Mo in both samples were similar. Main species of Co, Ni, Cu, Zn and Mo were found in the low molecular weight region (2-5 kDa), whereas Fe is predominantly bound to high molecular weight compounds (180 kDa). The dominant phosphorus fraction was detected in the medium molecular weight region (10-30 kDa) and the other fraction in the low molecular weight region. Isotachophoretic analysis of chromatographic fractions revealed that the main phosphorus compound in the medium molecular weight region is phytic acid. SEC on Superdex 75 and Superdex Peptide columns (300 x 10 mm) was performed in on-line hyphenation with ICP-MS. The same mobile phase was used with a flow rate of 0.5 ml min(-1); volume of injected sample was 200 microl. Element specific chromatograms were obtained by continuous nebulization of effluent into ICP-mass spectrometer measuring intensities of 47(PO)+ and 48(SO)+ oxide ions and 55Mn, 57Fe, 59Co, 62Ni, 65Cu, 66Zn, 82Se, 95Mo and 114Cd nuclides. Chromatographic profiles of elements are generally analogous to those obtained with a Fractogel column, but better chromatographic resolution of separated species was achieved so that slight differences between samples were revealed. Estimated molecular weights of major phosphorus species in soybean flour and common white bean seed extracts are 6 and 3.6 kDa, respectively, whereas those of minor phosphorus species in both samples are 0.7 kDa. Traces of phosphorus were also detected in the high molecular weight region (130 kDa). Chromatograms of P, Ni, Cu, Zn and Mo compounds in both extracts are similar but not identical. Molecular weights of major Cu and Zn species are approximately 1 and 0.4 kDa for soybean flour and white bean seeds, respectively. In cases of Mn, Fe, Co and Se, the element profiles of soybean flour and white bean seed extracts are significantly different.
Chromatography, Gel↗
Molecular characterization of a bean alpha-amylase inhibitor that inhibits the alpha-amylase of the mexican bean weevil Zabrotes subfasciatus.
Cultivated varieties of the common bean (Phaseolus vulgaris L.) contain an alpha-amylase inhibitor (alpha AI-1) that inhibits porcine pancreatic alpha-amylase (PPA; EC 3.2.1.1) and the amylases of certain seed weevils, but not that of the Mexican bean weevil, Zabrotes subfasciatus. A variant of alpha AI-1, called alpha AI-2, is found in certain arcelin-containing wild accessions of the common bean. The variant alpha AI-2 inhibits Z. subfasciatus alpha-amylase (ZSA), but not PPA. We purified alpha AI-2 and studied its interaction with ZSA. The formation of the alpha AI-2-ZSA complex is time-dependent and occurs maximally at pH 5.0 or below. When a previously isolated cDNA assumed to encode alpha AI-2 was expressed in transgenic tobacco seeds, the seeds contained inhibitory activity toward ZSA but not toward PPA, confirming that the cDNA encodes alpha AI-2. The inhibitors alpha AI-1 and alpha AI-2 share 78% sequence identity at the amino acid level and they differ in an important region that is part of the site where the enzyme binds the inhibitor. The swap of a tripeptide in this region was not sufficient to change the specificity of the two inhibitors towards their respective enzymes. The three-dimensional structure of the alpha AI-1/PPA complex has just been solved and we recently obtained the derived amino acid sequence of ZSA. This additional information allows us to discuss the results described here in the framework of the amino acid residues of both proteins involved in the formation of the enzyme-inhibitor complex and to pinpoint the amino acids responsible for the specificity of the interaction.
Amino Acid Sequence↗
Identification of the protein storage vacuole and protein targeting to the vacuole in leaf cells of three plant species.
Protein storage vacuoles (PSVs) are specialized vacuoles devoted to the accumulation of large amounts of protein in the storage tissues of plants. In this study, we investigated the presence of the storage vacuole and protein trafficking to the compartment in cells of tobacco (Nicotiana tabacum), common bean (Phaseolus vulgaris), and Arabidopsis leaf tissue. When we expressed phaseolin, the major storage protein of common bean, or an epitope-tagged version of alpha-tonoplast intrinsic protein (alpha-TIP, a tonoplast aquaporin of PSV), in protoplasts derived from leaf tissues, these proteins were targeted to a compartment ranging in size from 2 to 5 microm in all three plant species. Most Arabidopsis leaf cells have one of these organelles. In contrast, from one to five these organelles occurred in bean and tobacco leaf cells. Also, endogenous alpha-TIP is localized in a similar compartment in untransformed leaf cells of common bean and is colocalized with transiently expressed epitope-tagged alpha-TIP. In Arabidopsis, phaseolin contained N-glycans modified by Golgi enzymes and its traffic was sensitive to brefeldin A. However, trafficking of alpha-TIP was insensitive to brefeldin A treatment and was not affected by the dominant-negative mutant of AtRab1. In addition, a modified alpha-TIP with an insertion of an N-glycosylation site has the endoplasmic reticulum-type glycans. Finally, the early step of phaseolin traffic, from the endoplasmic reticulum to the Golgi complex, required the activity of the small GTPase Sar1p, a key component of coat protein complex II-coated vesicles, independent of the presence of the vacuolar sorting signal in phaseolin. Based on these results, we propose that the proteins we analyzed are targeted to the PSV or equivalent organelle in leaf cells and that proteins can be transported to the PSV by two different pathways, the Golgi-dependent and Golgi-independent pathways, depending on the individual cargo proteins.
Arabidopsis↗
Digestion of legume starch granules by larvae of Zabrotes subfasciatus (Coleoptera: bruchidae) and the induction of alpha-amylases in response to different diets.
Zabrotes subfasciatus larvae possess three alpha-amylase isoforms as determined by in gel assays following SDS-PAGE. The two minor isoforms present lower electrophoretic mobility than the major form, and seem to occur as a heterodimer. When developed inside Vigna unguiculata (cowpea) seeds, fourth instar larvae have minor quantities of the slow-migrating forms, but when reared on seeds of Phaseolus vulgaris (common bean) or Phaseolus lunatus, the two slow-migrating forms are expressed in higher amounts, while activity of the major form was independent of the host seed. Larvae developing inside cowpea seeds at the beginning of the fourth instar were fed on flour from cotyledons of cowpea or common bean. Larvae fed on the common bean flour started to express the dimer in higher amounts when compared with the control larvae fed on cowpea flour. In an attempt to correlate differences between starch granules and the induction of alpha-amylases, a detailed study on the digestive process of the granules was conducted. Incorporation of purified starch granules into artificial diets did not induce the two minor alpha-amylases. The in vitro hydrolysis rates of purified granules and the pattern of dextrins liberated by the different alpha-amylases were similar for the two legume species. The starch granules enter the midgut extensively damaged, which may facilitate the access to the more susceptible parts of the granules to enzymatic attack.
Animals↗