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PubMed1996

Frequent occurrence of recombinant potyvirus isolates.

We have performed a systematic search for recombination in the region encoding coat protein and the 3' non-translated region in natural isolates of potyviruses, the largest group of plant RNA viruses. The presence of recombination, and the localization of the cross-over points, were confirmed statistically, by three different methods. Recombination was detected or suspected in 18 out of 109 potyvirus isolates tested, belonging to four out of eight virus species, and was most prevalent in potato virus Y, clear in bean common mosaic virus, and possible in bean yellow mosaic and zucchini yellow mosaic viruses. Recombination was not detected in the four other potyvirus species tested, including plum pox virus, despite the availability of numerous sequences for this last species. Though it was not specifically researched, no evidence for inter-specific recombination was found. For several reasons, including the fact that only a minor portion of the genome was analysed, the above figures certainly represent an underestimate of the extent of recombination among isolates of potyviruses, which might thus be a common phenomenon.

Amino Acid Sequence↗
PubMed1998

Novel lectin-related proteins are major components in lima bean (Phaseolus lunatus L.) seeds.

The only component of the lectin-related protein family so far reported in Lima bean (Phaseolus lunatus L.) seeds is the minor seed lectin (LBL). In the morphotype Big Lima, we have isolated and characterised two abundant lectin-related seed proteins and the corresponding cDNA clones. The clones show 93.7% nucleotide identity and encode an arcelin-like (ARL) and an alpha-amylase inhibitor-like (AIL) protein. Not considering the signal peptides, ARL and AIL polypeptides contain 239 and 233 amino acids, respectively. Each polypeptide is present in the mature protein as two glycoforms. ARL subunits (43 and 46 kDa) make up oligomers of about 125 to 130 kDa whereas AIL subunits (40 and 42 kDa) oligomerise in dimers of about 88 to 100 kDa. cDNA clones encoding two isoforms of the less abundant Lima bean lectin were also isolated. In common bean (P. vulgaris) the lectin locus encodes the lectin and the lectin-related proteins alpha-amylase inhibitor and arcelin, all plant defence proteins. Our data indicate extensive evolution of the locus also in Lima bean.

Amino Acid Sequence↗
PubMed2003

Iron and zinc absorption from two bean (Phaseolus vulgaris L.) genotypes in young women.

Extrinsic and intrinsic iron and zinc labels were used to test iron and zinc absorption from two bean (Phaseolus vulgaris) genotypes, containing normal (common beans, CB) or higher (HFeZnB) iron and zinc concentrations, fed in single meals to young women with low iron reserves. The women were divided into two groups, with one receiving a CB test meal (n = 12) and the other, an HFeZnB test meal (n = 11). The beans were intrinsically labeled hydroponically with (55)Fe (CB and HFeZnB) and with (70)Zn (HFeZnB). Concentrations of zinc and iron were 98 and 65% higher, respectively, in HFeZnB as compared to CB, but phytic acid contents were similar. Extrinsic labels were (59)Fe (CB and HFeZnB), (67)Zn (CB), and (68)Zn (HFeZnB). Iron and zinc percent absorption levels were calculated from radio-iron activity in red blood cells and from urinary excretion of zinc isotopes. Intrinsic and extrinsic iron absorption measures were highly correlated (R (2) = 0.986) (average extrinsic/intrinsic ratio was 1.00). Iron absorption was low (geometric mean < 2%) in both bean types, and total iron absorbed was not different between types. Intrinsic zinc absorption from the HFeZn beans was higher than extrinsic absorption (15.2% vs 13.4%, p < 0.05) (average extrinsic/intrinsic was 0.90). The correlation between intrinsic and extrinsic zinc measures was not as high as that for iron (R (2) = 0.719). Percent zinc absorption levels were similar in both bean types, but total extrinsic zinc absorbed was 90% higher (p < 0.05) from the HFeZnB meal. Thus, the less expensive and time-consuming extrinsic labeling may be used to screen various varieties of beans for iron bioavailability in humans, but it underestimates zinc absorption by approximately 10%. Selective breeding for high-zinc bean genotypes may improve zinc status. However, high-iron genotypes appear to have little effect on iron status when fed alone in single meals to women with low iron reserves.

Adult↗
PubMed1994

Capsid protein properties of cowpea aphid-borne mosaic virus and blackeye cowpea mosaic virus confirm the existence of two major subgroups of aphid-transmitted, legume-infecting potyviruses.

A study of the capsid proteins of different legume-infecting potyviruses using specific monoclonal antibodies on immunoblots of crude extracts from infected plants revealed that cowpea aphid-borne mosaic virus (CAMV) and blackeye cowpea mosaic virus (BICMV) have coat protein M(r) values of 32K and 35K, respectively. Immunoblot comparisons of BICMV, peanut stripe mosaic virus (PStV), bean common mosaic virus (BCMV) and azuki bean mosaic virus (AzMV) revealed equal reactivity of their 35K coat proteins. Similar comparisons between CAMV and the necrotic strain of BCMV (isolate NL3) showed a serological relationship between their 32K coat proteins, results providing the first evidence of a possible similarity between CAMV and BCMV NL3. Peptides from trypsin digests of the coat proteins of several of these legume-infecting potyviruses were analysed by HPLC. Comparison of the peptide profiles confirmed the serological results in distinguishing the two subgroups. Peptide profiles of coat protein from BICMV, PStV, AzMV and BCMV were almost identical, results suggesting that they could be considered as strains of one virus. In contrast, peptide profiles of various CAMV serotypes and BCMV NL3 were distinct from the first group and exhibited limited similarities to each other.

Animals↗
PubMed2000

Complementation of the host range restriction of southern cowpea mosaic virus in bean by southern bean mosaic virus.

Vigna unguiculata (cowpea) and Phaseolus vulgaris (common bean) are permissive hosts for southern cowpea mosaic virus (SCPMV) and southern bean mosaic virus (SBMV), respectively. Neither of these two sobemoviruses systemically infects the permissive host of the other. Although bean cells are permissive for SCPMV RNA synthesis, they do not support the assembly of this virus. Thus, the host range restriction of SCPMV in bean may occur at the level of movement and may involve the inability of SCPMV to assemble in this host. In this study, it was demonstrated that SCPMV accumulates in an encapsidated form in the inoculated and systemic leaves of bean plants following coinoculation with SBMV. No evidence was observed that the SCPMV that accumulated in coinoculated bean plants had an altered host range relative to wild-type SCPMV. These results suggested that SBMV complemented the host range restriction of SCPMV in bean. Additional experiments demonstrated that cowpea protoplasts are permissive for SBMV RNA synthesis and assembly. It was concluded from these results that the host range restriction of SBMV in cowpea occurs at the level of movement. In mixed infections of cowpea with SCPMV and SBMV, the latter was recovered from the inoculated but not the systemic leaves. Its recovery from the inoculated leaves, however, was not dependent on the presence of SCPMV in the inoculum. From these results, it was concluded that SCPMV did not complement the host range restriction of SBMV in cowpea.

Comovirus↗
PubMed2006

Structure and enzyme properties of Zabrotes subfasciatus alpha-amylase.

Digestive alpha-amylases play an essential role in insect carbohydrate metabolism. These enzymes belong to an endo-type group. They catalyse starch hydrolysis, and are involved in energy production. Larvae of Zabrotes subfasciatus, the Mexican bean weevil, are able to infest stored common beans Phaseolus vulgaris, causing severe crop losses in Latin America and Africa. Their alpha-amylase (ZSA) is a well-studied but not completely understood enzyme, having specific characteristics when compared to other insect alpha-amylases. This report provides more knowledge about its chemical nature, including a description of its optimum pH (6.0 to 7.0) and temperature (20-30 degrees C). Furthermore, ion effects on ZSA activity were also determined, showing that three divalent ions (Mn2+, Ca2+, and Ba2+) were able to enhance starch hydrolysis. Fe2+ appeared to decrease alpha-amylase activity by half. ZSA kinetic parameters were also determined and compared to other insect alpha-amylases. A three-dimensional model is proposed in order to indicate probable residues involved in catalysis (Asp204, Glu240, and Asp305) as well other important residues related to starch binding (His118, Ala206, Lys207, and His304).

Amino Acid Sequence↗
PubMed1988

Denaturation by heat, sodium dodecyl sulphate and dithiothreitol of globulins and phaseolin from dry bean (Phaseolus vulgaris L.).

The electrophoretic pattern of the untreated common bean globulin cv. Flor de Mayo had 7 protein fractions ranging from 620 to 120 kilodaltons (kd). The last molecular weight corresponds to the monomeric form. One of the objectives of the present work was to establish a comparison among denaturation by heat, sodium dodecyl sulphate (SDS) and dithiothreitol (DTT). At pH 6.0, two bands were resistant to heat treatment, after SDS treatment of the untreated globulin several bands disappeared and two new bands with 26 and 15 kd appeared. DTT did not change the electrophoretic pattern, due to the small quantity of free SH groups in the globulin. At pH 6.0, phaseolin is partly resistant to heat denaturation due to aggregation in an acidic environment. Isoelectrofocusing (IEF) and SDS polyacrylamide gel electrophoresis (SDS-PAGE) separated phaseolin into 10 protein fractions. The hypothesis is that phaseolin or globulin aggregation is due to the charge difference of fractions.

Dithiothreitol↗
PubMed1991

[Bioavailability of amino acids in beans (Phaseolus vulgaris)].

Biological availability of amino acids of three common bean (Phaseolus vulgaris) varieties was evaluated in four, healthy adult subjects, consuming bean-based diets by the amino acid absorption technique and the short-term nitrogen balance method. The amino acid composition was determined according to the ionic interchange method, and tryptophan was estimated by a colorimetric procedure. The essential amino acid (EAA) and non-essential amino acid (NEAA) pattern suggests that no significant differences in content exists in the three bean varieties. When the EAA patterns were compared with those of FAO/WHO, the limiting AA in decreasing order were found to be: tryptophan, valine and threonine (sulfur AA are not considered because the hydrolysis used in this study destroys them); and the AA surpassing the reference pattern were the aromatic AA and isoleucine. Apparent (AD) and true (TD) digestibilities of the EAA fluctuated between 33 and 59% and 60 and 85%, respectively, for black beans. With red beans, these results diminished: 29 and 55% AD and 64 and 81% TD, while for white beans the limits extended: 18 and 57% AD and 36 and 86% TD. Valine proved to be the EAA of lower biological availability, and lysine and phenylalanine the most available. It is suggested that the low digestibility of valine could be due to the amino acid imbalance existing in the bean protein, since this contains an excess of isoleucine and leucine in relation to valine. The AD and TD of the AAE with respect to the NEAA were of 0.89 and 0.98 for black bean, 0.89 and 0.96 for the red and 0.77 and 0.90 for the white, which indicates that biological availability of the NEAA is higher than that of the EAA. Findings thus confirm that biological determination of the TD of protein permits prediction of the TD of the AA, since a positive correlation (r = 0.93) statistically significant was found (p less than 0.05) among them. Utilization of the TD parameter instead of that of AD to estimate the protein quality is therefore recommended.

Adult↗
PubMed1997

Classification of Austrian rhizobia and the Mexican isolate FL27 obtained from Phaseolus vulgaris L. as Rhizobium gallicum.

The phylogenetic positions of four rhizobial strains obtained from nodules of common bean plants (Phaseolus vulgaris L.) grown in an Austrian soil and of the Mexican bean isolate FL27 are described. Analysis of the 16S rRNA genes revealed sequences almost identical to that of the Rhizobium gallicum type strain, R602sp, with a maximum of two nucleotide substitutions. Comparison of the 16S rRNA gene sequences with those from other bacteria indicated highest similarity to Rhizobium sp. strain OK-50, Rhizobium leguminosarum IAM 12609, and Rhizobium etli. DNA homology determined by DNA-DNA hybridization was high among the Austrian isolates and R602spT (45 to 90%) and ranged from 21 to 65% with FL27, but hybridization analysis revealed very low homology to the recognized common bean-nodulating species, R. leguminosarum bv. phaseoli, R. etli, and Rhizobium tropici. Ribosomal gene organization was studied by Southern hybridization with the 16S rRNA gene and temperature gradient gel electrophoresis, indicating identical organizations and the presence of three identical 16S rRNA copies in the genome of this species. The six strains investigated showed different plasmid profiles based on their geographical origins. We propose that the Austrian isolates and the Mexican strain FL27 are members of the species R. gallicum.

Austria↗
PubMed2003

Effect of different soaking solutions on nutritive utilization of minerals (calcium, phosphorus, and magnesium) from cooked beans (Phaseolus vulgaris L.) in growing rats.

The effects of the commonly used processing techniques of soaking (at different pH values) and cooking on the digestive and nutritive utilization of calcium, phosphorus, and magnesium from common beans (Phaseolus vulgaris L.) were studied. Before the cooking step, the beans were soaked in solutions of acid (2.6 and 5.3) or basic (8.4) pH. Chemical and biological methods were used to determine nutritional parameters in growing rats, and the fiber content of the beans was established. As the pH of the soaking solution increased, so did mineral absorption and the apparent digestibility coefficient, which reached suitable values for growing rats, due to the reduced losses of soluble minerals and the increased food intake. Metabolic utilization also improved with increased pH of the soaking solution, although the values were, in general, low as a result of urinary losses under the experimental conditions. For the experimental period of 10 days, the femur and the muscle seem to be good metabolic indicators for calcium, but not for phosphorus or magnesium. The increased amount of cellulose in the soaked seed did not have a negative effect on the digestive utilization of minerals.

Animals↗
PubMed1995

Targeting and release of phytohemagglutinin from the roots of bean seedlings.

Phytohemagglutinin (PHA), an abundant vacuolar seed protein of the common bean (Phaseolus vulgaris), is a tetramer of two homologous polypeptides, PHA-E and PHA-L. The roots of bean seedlings release into the culture medium a cross-reacting lectin that is most closely related to PHA-E. Reverse-transcriptase polymerase chain reaction with root mRNA as template was used to identify PHA transcripts in the roots of bean seedlings. Roots were found to contain mRNA for PHA-E but not for PHA-L. Indirect immunocytochemical detection with colloidal gold and antibodies to deglycosylated PHA showed that in the meristem of the primary root, PHA accumulates in vacuoles. However, in elongated root cells PHA was found only in the cell walls, indicating targeting to an alternate location. These results are discussed in relation to the various mechanisms that may account for the release of a normally vacuolar protein by roots.

Amino Acid Sequence↗
PubMed1987

Structure, position, and biosynthesis of the high mannose and the complex oligosaccharide side chains of the bean storage protein phaseolin.

Phaseolin, the major storage protein of the common bean (Phaseolus vulgaris), is a glycoprotein which is synthesized during seed development and accumulates in protein storage vacuoles or protein bodies. The protein has three different N-linked oligosaccharide side chains: Man9(GlcNAc)2, Man7(GlcNAc)2, and Xyl-Man3(GlcNAc)2 (where Xyl represents xylose). The structures of these glycans were determined by 1H NMR spectroscopy. The Man9(GlcNAc)2 glycan has the typical structure found in plant and animal glycoproteins. The structures of the two other glycans are shown below. (Formula; see text) Phaseolin was separated by electrophoresis on denaturing gels into four size classes of polypeptides. The two abundant ones have two oligosaccharides each, whereas the less abundant ones have only one oligosaccharide each. Polypeptides with two glycans have Man7(GlcNAc)2 attached to Asn252 and Man9(GlcNAc)2 attached to Asn341. Polypeptides with only one glycan have Xyl-Man3(GlcNAc)2 attached to Asn252. Both these asparagine residues are in canonical glycosylation sites; the numbering starts with the N-terminal methionine of the signal peptide of phaseolin. The presence of the Man7(GlcNAc)2 and of Xyl-Man3(GlcNAc)2 at the same asparagine residue (position 252) of different polypeptides seems to be controlled by the glycosylation status of Asn341. When Asp341 is unoccupied, the glycan at Asn252 is complex. When Asn341 is occupied, the glycan at Asn252 is only modified to the extent that 2 mannosyl residues are removed. The processing of the glycans, after the removal of the glucose residues, involves enzymes in the Golgi apparatus as well as in the protein bodies. Formation of the Xyl-Man3(GlcNAc)2 glycan is a multistep process that involves the Golgi apparatus-mediated removal of 6 mannose residues and the addition of 2 N-acetylglucosamine residues and 1 xylose. The terminal N-acetylglucosamine residues are later removed in the protein bodies. The conversion of Man9(GlcNAc)2 to Man7(GlcNAc)2 is a late processing event which occurs in the protein bodies. Experiments in which [3H]glucosamine-labeled phaseolin obtained from the endoplasmic reticulum (i.e. precursor phaseolin) is incubated with jack bean alpha-mannosidase show that the high mannose glycan on Asn252, but not the one on Asn341, is susceptible to enzyme degradation. Incubation of [3H] glucosamine-labeled phaseolin obtained from the Golgi apparatus with jack bean beta-N-acetylglucosaminidase results in the removal of the terminal N-acetylglucosamine residues from the complex chain.(ABSTRACT TRUNCATED AT 400 WORDS)

Carbohydrate Conformation↗
PubMed2000

The chloroplast genomes of azuki bean and its close relatives: a deletion mutation found in weed azuki bean.

A physical map of the azuki bean (Vigna angularis cv. Erimo-shozu) chloroplast DNA (cpDNA) was constructed by localising the cleavage sites of PstI, SalI, SmaI, SacI, KpnI, PvuII and XhoI. The resulting map is more similar to the cpDNA-maps of two Vigna species (mung bean, V. radiata, and V. nakashimae) than to common bean (Phaseolus vulgaris) cpDNA map. Azuki bean was originally classified in the genus Phaseolus, and the inclusion of this taxon in the genus Vigna is a recent taxonomic decision. Our result is thus in favour of the taxonomic placement of azuki bean in the same genus as V. nakashimae and mung bean. We also found that a weed-form accession of azuki bean has a 96-bp deletion relative to the cultivar Erimo-shozu. The 96-bp deletion is located between the trnS-UGA and psbC genes in the large single-copy region of the chloroplast genome. This deletion is flanked by imperfect 9-bp direct repeats, suggesting that the deletion was a result of intra-molecular recombination mediated by these direct repeats.

Base Sequence↗
PubMed2003

Natural resistance to Clover yellow vein virus in beans controlled by a single recessive locus.

We characterized the resistance of the common bean cv. Jolanda to Clover yellow vein virus no. 30 (ClYVV). After inoculation, the virus was detected in neither inoculated nor upper leaves, suggesting that the resistance operates at either the viral replication or cell-to-cell movement level. To analyze the mechanism of resistance, we developed a green fluorescent protein (GFP)-tagged ClYVV, and monitored GFP fluorescence at sites of infection on ClYVV-inoculated leaves. No GFP fluorescence was detected in Jolanda, whereas its expression in single cells and spread on inoculated leaves were observed clearly in susceptible cultivars. ClYVV-introduced Jolanda cells were found to be still viable; therefore, it is unlikely that the restriction of multiplication was due to rapid cell death. Genetic analysis indicated that a single recessive locus controlled the resistant phenotype of Jolanda. We designated this locus desc (determinant of susceptibility to ClYVV). Meanwhile, a spontaneous mutant virus that overcomes the resistance (ClYVV-Br) was isolated. Inoculation assays using chimeric viruses suggested that a viral genome-linked protein (VPg) might be the avirulence determinant. The resistance mechanism may be associated with the role of VPg in the viral infection cycle.

Amino Acid Sequence↗
PubMed1993

Failure of long-distance movement of southern bean mosaic virus in a resistant host is correlated with lack of normal virion formation.

Sunn-hemp mosaic tobamovirus (SHMV) facilitated the spread of the cowpea strain of southern bean sobemovirus (SBMV-C) only in inoculated leaves of common bean (Phaseolus vulgaris L. cv. Bountiful), a resistant host for SBMV-C. Tissue prints of bean primary leaves doubly inoculated with SHMV and SBMV-C, developed by Western blotting, showed the presence of the SBMV-C capsid antigen in the mesophyll and epidermis, but no antigen was detected in the conducting bundles. Typical SBMV-C virions were not seen in electron micrographs of immunogold-labelled mesophyll cells; instead, specifically labelled, amorphous protein clumps were found in the vacuole. Particles of smaller diameter than that of typical SBMV-C virions were specifically trapped by SBMV antibodies following immunosorbent electron microscopy of extracts from doubly infected leaves. SBMV-C coat protein from infected Vigna unguiculata L. (cowpea) and bean plants showed no difference in its mobility following electrophoresis in denaturing SDS-polyacrylamide gels. Lack of efficient assembly of SBMV-C virions does not impede cell-to-cell movement of the virus in doubly infected leaves of bean, yet it is probably an important factor in determining the inability of SBMV-C to move into and/or through the vascular system of this host.

Antigens, Viral↗
PubMed1995

Wild type Rhizobium etli, a bean symbiont, produces acetyl-fucosylated, N-methylated, and carbamoylated nodulation factors.

Phaseolus vulgaris (common bean) can be nodulated by different Rhizobium species. A new species has been recently proposed: Rhizobium etli. Following transcriptional activation of the bacterial nodulation genes using naringenin or bean seed exudate, we have isolated, purified, and characterized R. etli extracellular nodulation factors. They are chitopentameric compounds that are N-methyl-N-vaccenoylated at their non-reducing end. At position 6 of the reducing N-acetyl-D-glucosamine, they are 4-O-acetyl-L-fucosylated. Minor compounds bear a carbamate group on the terminal non-reducing saccharidic residue.

Acetylglucosamine↗
PubMed1986

[Chemical composition and evaluation of the protein quality of beans in adult humans by the short-term nitrogen balance method].

Three varieties of common beans were chemically analyzed and their protein quality was evaluated in 12 human male adult subjects by the short-term nitrogen balance method. Chemical analyses were performed for both raw and cooked grains. Cooking reduced the trypsin inhibitors in 28 to 73%, hemagglutinins, 100%, tannins as acid tannic equivalents, 9 to 72%, and 55 to 75% as catequin equivalents, and alkali-soluble nitrogen in 65%. Red and black beans contained more residual trypsin inhibitors and tannins than white beans, while the latter contained more alkali-soluble nitrogen. Although cooked colored beans had more antinutritional factors that affect protein digestibility, their protein quality was similar to that of white beans. This could be explained by the fact that the amino acid composition and/or balance of red and black beans absorbed nitrogen is better than that of white beans, so that the final nutritional value will be determined by the sum of interactions between all factors. In this study, each of the three varieties presented at least one protein quality depressor in higher concentration than the other two varieties. Therefore, the overall differences found between treatments and residual effect, were small or non existent, while significant differences (p greater than 0.05) were found between subjects and nitrogen balance periods. A level of 0.65 g of bean protein/kg/day was not enough to maintain nitrogen balance in subjects fed a diet where beans were the only protein source. According to calculations, 0.9-1.0 g of bean protein/kg/day are necessary for nitrogen balance in male adults, and 1.2-1.3 g of protein bean would be the recommendation for a normal population.

Adult↗
PubMed1987

Advances in the molecular biology of plant seed storage proteins.

Plant seed storage proteins were among the first proteins to be isolated (20); however, only recently, as a result of using molecular biology techniques, have the amino acid sequences of many of these proteins been determined. With the accumulation of amino acid sequence data for many vicilin-type storage proteins much has been learned concerning the location of conserved amino acid regions and other regions which can tolerate amino acid sequence variation. Combining this knowledge with recent advances in plant gene transfer technologies will allow molecular biologists to correct (by using amino acid replacement mutations) the sulfur amino acid deficiency inherent to bean seed storage proteins. The development of more nutritious soybean and common bean seeds will be of benefit to programs involving human and animal nutrition.

Journal Article↗