Disease relevance of Lupinus

• Nodulation of Lupinus albus by strains of Ochrobactrum lupini sp. nov [1].
• We isolated over 300 phytate (Na-inositol hexa-phosphate; Na-IHP)-utilizing bacterial strains from the rhizosheath and the rhizoplane of Lupinus albus (L.). Almost all of the isolates were classified as Burkholderia based on 16S rDNA sequence analysis [2].
• Dissimilatory nitrate reductase from Bradyrhizobium sp. (Lupinus): subcellular location, catalytic properties, and characterization of the active enzyme forms [3].
• 4. The utilization of lysine fro weight gain compared with free lysine was 0.86-0.88 for meat meals, 0.95-0.99 for soya-bean meal, 0.69-0.75 for cotton-seed meal, 0.90 for lupins (Lupinus augustifolius) and 0.99 for milk [4].
• Mice that were given oral peanut showed only increase in peanut-specific IgG2a, but no IgE or IgG1 Abs and failed to develop anaphylactic reactions following injection of either peanut or lupine protein [5].

High impact information on Lupinus

• After surface-sterilized lupine seeds were successfully inoculated with the recombinant strain, the engineered endophytic bacteria strongly degraded toluene, resulting in a marked decrease in its phytotoxicity, and a 50-70% reduction of its evapotranspiration through the leaves [6].
• We identified two soybean genes encoding isoflavone synthase, and used them to isolate homologous genes from other leguminous species including red clover, white clover, hairy vetch, mung bean, alfalfa, lentil, snow pea, and lupine, as well as from the nonleguminous sugarbeet [7].
• Beta-cyano-L-alanine synthase [L-cysteine hydrogen-sulfide-lyase (adding HCN), EC 4.4.1.9] was purified about 4000-fold from blue lupine seedlings [8].
• These include the Cladrastis clade, the genistoids (including Lupinus), the mirbelioids, the dalbergioids (including Arachis), the millettioids (including Glycine and Phaseolus), and the hologalegina (galegoid) legumes, which comprise the robinioids (including Lotus) and the inverted repeat loss (IRL) clade (including Medicago and Pisum) [9].
• In this investigation, we have for the first time used a genetically modified (GM) plant, narrow leaf lupin (Lupinus angustifolius L.), expressing a gene for a potential allergen (sunflower seed albumin) (SSA-lupin) to examine whether a GM plant/food-based vaccine strategy can be used to suppress the development of experimental asthma [10].

Chemical compound and disease context of Lupinus

• Aerobic and anaerobic nitrate and nitrite reduction in free-living cells of Bradyrhizobium sp. (Lupinus) [11].

Biological context of Lupinus

• The nucleotide sequences of two Lupinus luteus asparagine tRNAs [12].
• The inclusion of 10% lupine flour in wheat flour without mandatory labeling makes lupine a hidden allergen, presenting a major risk of cross-reaction in subjects already allergic to peanut products [13].
• Distinction between genotypes of Lupinus species by sodium dodecyl sulphate-gel electrophoresis and by capillary electrophoresis [14].
• Comparison of protein coding regions, as well as 5'-untranslated regions derived from LlNGS1 and a Lupinus angustifolius pGS5 GS cDNA clone [Grant et al., Plant Mol. Biol. 13 (1989) 481-490], revealed a high degree of shared identity between both genes, indicating that they are orthologous [15].
• The deduced amino acid sequence of lupin farnesyl pyrophosphate synthase pFPS2 shares 90 and 79% identity with those from Lupinus albus (pFPS1) and Arabidopsis thaliana, respectively, 51% with the yeast enzyme, and 44% identity with those from rat and human [16].

Anatomical context of Lupinus

• A methionine tRNA gene from lupine mitochondria [17].
• Application of cytokinin to etiolated lupine seedlings induces polyribosome association of their mRNAs [18].
• We have previously found that glucose and insulin concentrations are elevated in the cerebrospinal fluid (CSF) of rams in which the secretion of gonadotrophins has been stimulated by a nutritional supplement of lupin grain (Lupinus angustifolius) [19].
• Plastid biogenesis in etiolated lupine (Lupinus luteus L.) cotyledons is highly sensitive to cytokinins and abscisic acid [20].
• BACKGROUND AND AIMS: The cotyledons of Lupinus angustifolius contain large amounts of cell wall storage polysaccharide (CWSP) composed mainly of (1-->4)-beta-linked D-galactose residues in the form of branches attached to a rhamnogalacturonan core molecule [21].

Associations of Lupinus with chemical compounds

• Enzymes hydrolyzing ApppA and/or AppppA in higher plants. Purification and some properties of diadenosine triphosphatase, diadenosine tetraphosphatase, and phosphodiesterase from yellow lupin (Lupinus luteus) seeds [22].
• A novel acyltransferase for alkaloid metabolism, tigloyl-CoA: (-)-13 alpha-hydroxymultiflorine/(+)-13 alpha-hydroxylupanine O-tigloyltransferase (HMT/HLTase), a monomeric 50-kDa protein, was purified to homogeneity from 10-day-old Lupinus termis seedlings [23].
• The NIT4 homologs of N. tabacum were found to catalyze the same reactions and protein extracts of A. thaliana, N. tabacum and Lupinus angustifolius also converted Ala(CN) to Asp and Asn in vitro [24].
• The reaction of Lupinus luteus tRNAPhe with 1 M chloroacetaldehyde in the pH range of 4 - 6 at 25 degrees C was studied [25].
• Cloning and characterization of a cDNA encoding aspartate aminotransferase-P1 from Lupinus angustifolius root tips [26].

Gene context of Lupinus

• The mitochondrial nad9 and nad6 genes were analyzed in four lupin species: Lupinus luteus, Lupinus angustifolius, Lupinus albus and Lupinus mutabilis [27].
• The development of clustered tertiary lateral roots (proteoid roots) and the expression of phosphoenolpyruvate carboxylase (PEPC, EC 4.1.1.31) in roots were studied in white lupin (Lupinus albus L.) grown with either 1 mM P (+P-treated) or without P (-P-treated) [28].
• Specificity and kinetic studies were performed with two aspartate aminotransferase isoenzymes (AAT-1 and AAT-2) from leaves of Lupinus albus L. cv Estoril using different amino donors and acceptors [29].
• For the first time in plants, we have established the sequence of four yellow lupine mitotic cyclin B1 genes [30].
• Specific IgEs were assayed for peanut, lupine flour, and pollen in 6 sera [13].

Analytical, diagnostic and therapeutic context of Lupinus

• Immunoblotting studies of electrophoretically separated pasta extract and lupine seed flour proteins showed IgE-binding protein bands at approximately 21 kd and in the range of 35 to 55 kd molecular weight [31].
• Valyl-tRNA, tryptophanyl-tRNA, and seryl-tRNA synthetases from yellow lupin seeds Lupinus luteus were purified to homogeneity by ammonium sulfate fractionation, hydrophobic chromatography on aminohexyl-Sepharose column and affinity chromatography on tRNA-Sepharose column [32].
• The 2C nuclear DNA content has been estimated by flow cytometry in 18 species and botanical forms of the genus Lupinus (family Fabaceae), using propidium iodide as a fluorescent dye [33].
• Liquid chromatography with ultraviolet and mass spectrometric detection was applied to monitor changes in profiles of isoflavonoid glycosides and free isoflavonoid aglycones in Lupinus albus L [34].

References