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PubMed1999

Cloning and molecular characterization of three members of the NBS-LRR subfamily located in the vicinity of the Co-2 locus for anthracnose resistance in Phaseolus vulgaris.

Co-2 is one of the R-genes against anthracnose identified in common bean. A RAPD marker, cloned as PvH20, was previously shown to contain 6 imperfect leucine-rich-repeats and to reveal a family of related sequences in the vicinity of the Co-2 locus. Using PvH20 as probe, a genomic clone and 2 partial cDNAs were isolated. DNA sequencing revealed that the 6.1 kb genomic fragment contains sequences encoding both NBS-LRR (ORF1) and kinase-like (ORF2) products. The 2 partial cDNAs (cD7 and cD8) belong to the NBS-LRR subfamily as do most of the resistance genes cloned to date. The LRR domain of ORF1 is interrupted by 2 stop codons suggesting that it corresponds to a non-functional member of the multigene family and ORF2 appears to be a kinase pseudogene. The 3 NBS-LRR polypeptides share a high level of amino acid identity and represent different members of a related family. By genetic mapping ORF1, cD7, and cD8 were found to span a genetic distance of 3 cM: cD8 maps at 2 cM from Co-2 and 3 cM from ORF1, cD7 maps at 1 cM from ORF1 and co-segregates with Co-2, thus cD7 might be a putative candidate for the Co-2 R-gene.

Amino Acid Sequence↗
PubMed2005

Colonization of Phaseolus vulgaris nodules by Agrobacterium-like strains.

Non-nodulating Agrobacterium-like strains identified among root nodule isolates of common bean were labeled with gusA, a reporter gene encoding beta-glucuronidase (GUS). Bean plants were then co-inoculated with an infective Rhizobium strain and labeled transconjugants of Agrobacterium-like strains. Blue staining of nodules showed that Agrobacterium-like strains were able to colonize these symbiotic organs. Isolation and characterization by restriction fragment length polymorphism analysis of PCR-amplified 16S rRNA genes revealed a mixed population of Rhizobium and Agrobacterium-like strains in all nodules showing GUS activity. PCR amplification of the nifH gene and nodulation tests did not show any evidence of acquisition of symbiotic gene by lateral transfer from Rhizobium to Agrobacterium-like strains. Moreover, these strains were able to invade mature nodules. Based on sequencing of the 16S rRNA gene, one of these Agrobacterium-like strains showed 99.4% sequence similarity with Agrobacterium bv. 1 reference strains and 99% similarity with an Agrobacterium bv. 1 strain isolated from Acacia mollisima in Senegal. Agrobacterium tumefaciens C58 and the disarmed variant AT123 did not show any ability to colonize nodules. Co-inoculation of bean seeds with Agrobacterium and Rhizobium strains did not enhance nodulation and plant yield under controlled conditions.

Glucuronidase↗
PubMed2006

Mechanistic analysis of experimental food allergen-induced cutaneous reactions.

Individuals with food allergy often present with uritcaria and atopic dermatitis. Indeed, susceptibility to food allergy may predispose to the development of these cutaneous allergic disorders. Recently, we developed a model of food allergy, whereby oral consumption of food [pea Pisum sativum L.; expressing alpha-amylase inhibitor-1 (alphaAI) from the common bean Phaseolus vulgaris L. cv Tendergreen (pea-alphaAI)] promotes a T helper cell type 2 (Th2) inflammatory response and predisposes to cutaneous allergic reactions following subsequent food allergen (alphaAI) exposure. To delineate the kinetics of food allergen-induced cutaneous reactions and examine the inflammatory mechanisms involved in this allergic reaction, we used interleukin (IL)-13-, IL-4 receptor alpha-, and eotaxin-1-deficient mice and performed serum transfer and CD4+ T cell depletion studies. We demonstrate that consumption of pea-alphaAI promotes an alphaAI-specific immunoglobulin G1 (IgG1) and IgE antibody response. Furthermore, we show that subsequent food allergen (alphaAI) challenge in the skin induced an early (3 h)- and late-phase (24 h) cutaneous allergic reaction. The early-phase response was associated with mast cell degranulation and the presence of Ig, whereas the late-phase response was characterized by a lymphoid and eosinophilic infiltrate, which was critically regulated by CD4+ T cells, IL-13, and eotaxin-1. Collectively, these studies demonstrate that food allergy can predispose to cutaneous inflammatory reactions, and these processes are critically regulated by Th2 immune factors.

Allergens↗
PubMed2006

7S globulins from Phaseolus vulgaris L.: Impact of structural aspects on the nutritional quality.

7S globulins were extracted from common bean (Phaseolus vulgaris L.) seeds and characterized. SDS-PAGE showed major bands corresponding to the phaseolin subunits (43-53 kDa). An amino acid analysis indicated that, in spite of the limited amounts of sulphur amino acids and tryptophan, the globulins contained very high levels of essential amino acids. The protein solubility profiles of native and denatured (120 degrees C for 20 min) 7S globulins in water and in 0.5 M NaCl showed that NaCl had a limited effect on increasing the solubility of either the native or denatured proteins. The in vivo small intestinal digestibility of the 7S globulins was 90%, this being decreased to 86% after a thermal treatment. Fourier transform infrared spectroscopy revealed a high content of beta-sheet and beta-turn structures, together with a contribution at 1687 cm(-1) that was assigned to intramolecular beta-sheets. These features are diagnostic of a high propensity to irreversible aggregation that may be related to an adverse effect on the protein quality.

Amides↗
PubMed2001

Investigation of the mechanisms affecting Cu and Fe bioavailability from legumes: role of seed protein and antinutritional (nonprotein) factors.

Chemical composition and content in polyphenols, phytic acid, and dietary fiber of whole cooked common bean (Phaseolus vulgaris L.) and faba bean (Vicia faba L.) and of soluble and insoluble fractions separated from them were determined. Simultaneous determination of Cu, Fe, and protein bioavailability in the small intestine of rat was carried out in single-dose, short-term (1 h) experiments. After cooking, about 80% of seed components (on a weight basis) of either legume was recovered in the precipitate (insoluble fraction) after extraction with water. Protein, lipid, starch, dietary fiber, and polyphenols underwent the most severe insolubilization, together with more than 70% of total Cu and Fe. Cu, Fe, and protein bioavailability showed a similar trend (i.e., the lower the protein, the lower the Cu and Fe availability). Availability of proteins, Cu, and Fe in the insoluble fractions were the lowest, but Cu bioavailability was higher than that of Fe in all fractions. The results provide evidence that the heat-induced insolubilization process adversely affects not only protein but also Cu and Fe bioavailability from legumes and that polyphenols are likely to be a major inhibitor on absorption.

Absorption↗
PubMed2004

The seed coat of Phaseolus vulgaris interferes with the development of the cowpea weevil [Callosobruchus maculatus (F.) (Coleoptera: Bruchidae)].

We have confirmed here that the seeds of the common bean (Phaseolus vulgaris, L.) do not support development of the bruchid Callosobruchus maculatus (F.), a pest of cowpea [Vigna unguiculata (L.) Walp] seeds. Analysis of the testa (seed coat) of the bean suggested that neither thickness nor the levels of compounds such as tannic acid, tannins, or HCN are important for the resistance. On the other hand, we have found that phaseolin (vicilin-like 7S storage globulin), detected in the testa by Western blotting and N-terminal amino acid sequencing, is detrimental to the development of C. maculatus. As for the case of other previously studied legume seeds (Canavalia ensiformis and Phaseolus lunatus) we suggest that the presence of vicilin-like proteins in the testa of P. vulgaris may have had a significant role in the evolutionary adaptation of bruchids to the seeds of leguminous plants.

Animals↗
PubMed2000

Method for cloning restriction fragments containing the termini of BAC inserts.

We have developed a method to isolate the termini of BAC clones. The method is based on the two unique NotI sites located approximately 300 bp on either side of the EcoRI cloning site of the BAC vector pECS-BAC4. Our strategy includes the following steps: (i) generation of Southern blots with BAC clones digested with NotI and a second restriction enzyme; (ii) identification of the termini attached to the NotI/EcoRI fragment of the BAC vector via hybridization with a probe derived from sequences located between one NotI site (left or right arm) and the cloning site; (iii) ligation of the doubly digested BAC clone (NotI and the selected second restriction enzyme) with an equally doubly digested cloning plasmid vector; and (iv) confirmation of the clone as a terminus. This strategy has allowed us to begin the construction of a contig near a common bean gene that controls resistance to a group of potyviruses.

Blotting, Southern↗
PubMed1999

Purification of multiple functional leaf-actin isoforms from Phaseolus vulgaris L.

Plant actins show diversity in their gene sequences, protein isovariants and tissue distribution in eukaryotes. Besides general difficulties with the isolation of proteins from plant material (i.e. the presence of a cell wall and high proteolytic activity), the actin concentration in any vegetative plant tissue is much lower than in cytoplasmic animal tissues. In this study, we adapted a deoxyribonuclease I-Sepharose affinity purification scheme and we were able to enrich and isolate multiple functional plant actin isovariants from common bean leaves (Phaseolus vulgaris). Urea (4 M) elution proved that the DNase I column was able to bind at least eight actin isoforms with pI values ranging from 5.5 to 5.9, as observed by two-dimensional Western blots. Three of the most acidic actin isoforms, with pI values of approximately 5.6-5.7, were eluted partially with 0.75 M urea. The purified actin was also able to bind leaf and rabbit muscle profilin, phalloidin and DNase I. Moreover, the protein could polymerize into filaments that contained the main isoforms eluted from the column. The average actin recovery using this procedure was approximately 4-8 microg from 20 g of fresh tissue, of which at least 80% was able to form filaments. This is the first report of the purification of multiple plant-actin isoforms that are functional by the criteria of both binding to other ligands and polymerization.

Actins↗
PubMed2001

A mosaic disease of Senna hirsuta induced by a potyvirus in Nigeria.

A virus inducing mosaic and severe leaf malformation, isolated from Senna hirsuta in Nigeria, was studied. The virus had a rather narrow host range, infecting a few species in Caesalpinaceae, Chenopodiaceae and Fabaceae families. The virus was widespread in southern Nigeria with prevalence ranging from 74% to 86.4% in some locations. It was transmitted mechanically and in a non-persistent manner by Myzuspersicae, Aphis craccivora and A. spiraecola. There was no evidence of transmission by seeds. Electron microscopy of leaf dip preparations revealed flexuous rod-shaped particles. The viral coat protein had Mr of 32.5 K. The virus reacted positively with a monoclonal antibody (MAb) to peanut stripe virus specific for potyviruses (members of the Potvvirus genus) and with antisera to turnip mosaic virus (TuMV), potato virus Y (PVY), TuMV, potato virus A (PVA), potato virus V (PVV) and bean yellow mosaic virus (BYMV), but it failed to react with antisera to celery mosaic virrus (CeMV), bean common mosaic virus (BCMV), soybean mosaic virus (SMV), and clover yellow mosaic virus (ClYMV) in plate-trapped ELISA (PTA-ELISA). No positive reaction was obtained when the virus was tested against any of the antisera in double-antibody sandwich ELISA (DAS-ELISA). This is the first report of natural infection of Senna species in Nigeria. The virus, tentatively designated as Senna mosaic virus (SeMV), seems to differ from other viruses previously described from Senna species in the literature and indeed other legume potyviruses in Nigeria.

Capsid↗
PubMed2001

Genetics of thermotolerance in ciprofloxacin resistant mutant of Rhizobium leguminosarum bv phaseoli.

A ciprofloxacin resistant mutant (Cf(R)) of Rhizobium leguminossarum bv phaseoli USDA 2695 which nodulates common bean plants (Phaseolus vulgaris L) was isolated after nitrous acid mutagenesis. Another mutant resistant to nalidixic acid (Nal(R)) was isolated spontaneously. Both mutants showed thermotolerance as evident by their ability to grow at elevated (40 degrees C) temperature, although the wild type (USDA 2695) failed to grow at this temperature. Transformation and plasmid curing experiments suggested the gene(s) controlling thermotolerance (TrR) and resistance to nalidixic acid or ciprofloxacin were located on the main chromosome and not on the plasmids. High frequency of co-transfer of TrR-Cr(R) and Tr(R)-Nal(R) during transformation experiments indicated a close association of these gene(s). Role of DNA gyrase and supercoiling in these thermotolerant mutants has been discussed.

Adaptation, Physiological↗
PubMed1977

Lectin purification on affinity columns containing reductively aminated disaccharides.

A method is described for isolating lectins in pure form and quantitative yield in a single step by affinity chromatography on aminoethyl polyacrylamide gels containing reductively aminated disaccharide residues. The affinity columns were prepared in two steps: (a) direct reductive amination of the disaccharide and aminoethyl gel with sodium cyanoborohydride in aqueous solution at pH 9; (b) N-acetylation of excess amino groups. Affinity columns prepared by reductive amination of lactose, melibiose, maltose, and di-N-acetylchitobiose were used to purify the following lectins: lactose, peanut, castor bean; melibiose, Bandeiraea simplicifolia; maltose, jack bean, common lentil; di-N-acetylchitobiose, wheat germ. These columns are extremely stable, have good flow rates, and high binding capacities.

Chromatography, Affinity↗
PubMed2004

Properties of a virus isolated from Vernonia amygdalina Del. in Lagos, Nigeria.

A previously uncharacterized virus tentatively named Vernonia green vein-banding virus (VGVBV) was isolated from Vernonia amygdalina Del. ("bitterleaf") from Lagos, Nigeria. The virus was mechanically transmissible but had a narrow host range restricted to Nicotiana benthamiana, Chenopodium quinoa and C. amaranticolor. It was also transmissible in a non-persistent manner by Myzus persicae. The virus was purified from N. benthamiana and about 750 nm long flexuous rod-shaped particles were observed in purified preparations as well as in leaf-dips of Vernonia sp. Inclusion bodies in the form of pinwheels and scrolls were observed in ultrathin sections of Vernonia leaves by electron microscopy. M(r), of the viral coat protein was estimated to be about 34 K. In indirect ELISA, all 20 samples from naturally infected Vernonia sp. reacted positively with a potyvirus-specific monoclonal antibody (MAb) as well as with an antiserum raised against VGVBV. Apart from the homologous antigen, the VGVBV antiserum reacted only with Plum poxvirus (PPV). The VGVBV reacted strongly with the antisera to Bean yellow mosaic virus (BYMV), Bean common mosaic virus (BCMV) and Amaranthus leaf mottle virus (AmLMV) but weakly with antisera to PPV and Cowpea aphid-borne mosaic virus (CABMV) (all members of the family Potyviridae, the genus Potyvirus) in at least one of the assays used (indirect ELISA, dot-blot immunoassay and Western blot analysis). The results of our host range, cytopathological and serological studies and the available literature indicate that a hitherto difficult to transmit VGVBV has only been reported from Nigeria. We consider VGVBV a candidate for a new potyvirus. This virus should be further investigated to collect sufficient data for a qualified proposal of VGVBV as a new potyvirus.

Animals↗
PubMed2005

Allelopathic effects of weeds extracts against seed germination of some plants.

This study investigated the allelopathic effects of various weeds extracts on seed germination of 11 crop species. Most of the weed extracts tested had inhibitory effects on seed germination of common bean, tomato, pepper, squash, onion, barley, wheat, and corn at different application rates as compared with the 10% acetone control. Chickpea seed germination was inhibited by extracts of Solanum nigrum L., Chenopodium album L., and Matricaria chamomilla L. (10%, 20% and 22.5%, respectively) at the end of 21 day incubation period. However, Glycyrrhiza glabra L., Sorghum halepense (L.) Pers., and Reseda lutea L. extracts stimulated chickpea seed germination at the rates of 95%, 94%, and 93%, respectively, compared to control. It was concluded that some of the weed extracts tested in this study could be used as inhibitor while others could be used as stimulator for the crops.

Crops, Agricultural↗
PubMed1986

Secretion of phytohemagglutinin by monkey COS cells.

The entire coding region of a gene, which encodes a polypeptide of phytohemagglutinin (PHA-L), obtained from a library of genomic DNA of the common bean Phaseolus vulgaris cv. Greensleeves, was introduced into the SV40 expression vector pJC119. Monkey COS1 cells were transfected with the recombinant clone and the synthesis, glycosylation, and transport of PHA-L studied and compared with the normal processes in bean cotyledons. In the bean, phytohemagglutinin is synthesized on the rough endoplasmic reticulum and transported via the Golgi complex to protein bodies, vacuole-like organelles. Phytohemagglutinin was synthesized and glycosylated at the ER and processed in the Golgi apparatus of the transfected COS1 cells. After passing the Golgi apparatus, PHA-L was slowly secreted into the culture medium (half-time of 3-6 h), a result indicating that the signals for targeting proteins beyond the Golgi apparatus in plant cells are different from those in animal cells. PHA, which is stored in protein bodies in the plant cells, is secreted by animal cells. Tunicamycin inhibited both glycosylation and secretion of PHA by the COS1 cells, a finding indicating an essential role of the oligosaccharides for transport of PHA in these cells in contrast to the situation found in bean cotyledons. PHA, secreted into the culture medium, was partially sensitive to endo H, a result indicating the presence of one high-mannose and one complex oligosaccharide chain, a situation identical to that in beans.

Animals↗
PubMed1985

Cooking procedures for direct consumption of whole soybeans.

The purpose of this research was to determine adequate conditions for the preparation of soybeans at home level. In accordance with the results, soaking the soybeans for eight hours in a 0.25% bicarbonate solution, gives the appropriate hydration to the soybeans, which can then be easily cooked. Boiling them at atmospheric pressure during 20 minutes was required to destroy 80% of the soybeans antitrypsin activity, and a high PER was also obtained. Nevertheless, the soybeans texture was not satisfactory; therefore, longer boiling periods were tested so as to establish the most suitable time needed to achieve a softness similar to that of common beans as usually consumed. Softness was measured instrumentally, and the optimal conditions found were: 40 min boiling after 8 hr soaking in a 0.25% bicarbonate solution. Under these conditions, the PER and NPU values increased 18% and 33%, respectively, with respect to those of the casein PER and NPU. It is concluded that with this procedure, large amounts of protein can become available at an equivalent price to US$0.40/kg ($80.00/kg).

Cooking↗
PubMed1984

Expression of lectin genes during seed development in normal and phytohemagglutinin-deficient cultivars of Phaseolus vulgaris.

Phytohemagglutinin (PHA), the major lectin of the common bean Phaseolus vulgaris, is synthesized during the development of the seeds. In most cultivars PHA makes up 5-10% of the total seed protein, but certain cultivars do not contain PHA. In vivo labeling of a normal cultivar (Greensleeves) and a PHA-minus cultivar (Pinto 111) showed that PHA was not synthesized in the PHA-minus cultivar. To find out whether the lack of synthesis was due to the absence of mRNA for PHA, recombinant cDNA clones for PHA were obtained. Total poly(A)+ RNA was isolated from cotyledons of developing seeds of Greensleeves and used to direct cDNA synthesis. The double stranded cDNA was cloned in pUC8 and transformants of Escherichia coli screened with pPVL134, a recombinant plasmid which contains the complete coding sequence for a PHA-like protein. Two weakly hybridizing clones (pSC1 and pSC2) were selected. Hybrid selection experiments showed that these two clones selected mRNAs which could be translated into polypeptides identical in size to PHA and recognized by antibodies to PHA. The recombinant pPVL134 selected mRNA which translated into polypeptides which were slightly smaller than those of PHA, and poorly recognized by antibodies to PHA. The recombinant clones were used to demonstrate that the genes for PHA and for the PHA-like protein are under temporal control during seed development. The cultivar Pinto 111, which has no detectable PHA, also has greatly reduced levels of mRNA for PHA. However, the gene for the PHA-like protein encoded by pPVL134 is expressed to the same degree in the cultivars Greensleeves and Pinto 111.

Fabaceae↗
PubMed1996

Chitin-binding proteins from cowpea (Vigna unguiculata) seeds.

Vicilins (7S storage proteins) from cowpea (Vigna unguiculata) and other legume seeds were shown to bind to chitin, to regenerated chitin (fully acetylated chitin) and to chitosan (deacetylated chitin). Adsorbed vicilins were desorbed from these matrices by acetic and hydrochloric acids and by highly polymerized soluble chitosan. Proteins such as the lectin of common bean (PHA), soybean trypsin inhibitor (Kunitz), a beta-1,3-glucanase from cowpea seeds, bovine pancreatic alpha-chymotrypsin, chicken ovalbumin, serum albumin and rabbit gamma-globulin did not bind. The present result is the first description of vicilin binding to chitin but other proteins, such as wheat germ agglutinin (WGA), a lectin that contains the so called "chitin-binding domain", and a chitinase isolated from cowpea seeds, which are involved in the defense mechanisms of plants against insects and fungi, were also shown to bind to chitin as previously reported. The binding of vicilins to chitin is probably effected not through a "chitin-binding domain" because they do not share this sequence with the defense-related proteins cited above. We propose that this association of vicilins with chitin may be related to the effect of variant vicilins on the development of Callosobruchus maculatus (bruchid) in resistant cowpea seeds.

Chemical Fractionation↗
PubMed1996

Bioavailability of carbohydrates in legumes: digestible and indigestible fractions.

Despite their important contribution to seed weight, carbohydrates in pulses have received limited attention. However, experimental evidence accumulated during the last two decades indicate that legumes are rich sources of slowly digestible starch promoting moderate postprandial glycernic and insulinemic responses. Although the reasons for this phenomenon are not completely understood, some intrinsic properties of the starch itself and the microstructure of cotyledon cells appear to determine much of the slow release character. This beneficial feature is rather sensitive to thermal and mechanical processing. A minimum of 10% of the starch occurring in common beans and lentils escapes digestion and absorption in the normal small intestine, and is therefore referred to as "resistant starch". This material consists mainly of retrograded amylose fractions generated upon cooling of wet-heated pulses. Physically inaccessible starch fractions resulting from cotyledon microstructural properties may also contribute to incomplete digestibility, accounting for up to 40% of the indigestible starch. These indigestible starch fractions are fermented in the large intestine generating gases and volatile fatty acids, compounds that have important influence on the physiology of the colonic mucosa and peripheral metabolism.

Biological Availability↗