Disease relevance of Erythrina

• Cystic kidney cells in vitro stained positive for lectins from Cancanavalia ensiformis (concanavalin A), Triticum vulgaris, Erythrina cristagalli, Ulex europeaus, and Arachis hypogaea [1].
• Synergistic effects of mupirocin and an isoflavanone isolated from Erythrina variegata on growth and recovery of methicillin-resistant Staphylococcus aureus [2].
• A new mitogenic D-galactosephilic lectin isolated from seeds of the coral-tree Erythrina corallodendron. Comparison with Glycine max (soybean) and Pseudomonas aeruginosa lectins [3].

High impact information on Erythrina

• The three-dimensional structure of the lactose complex of the Erythrina corallodendron lectin (EcorL), a dimer of N-glycosylated subunits, was determined crystallographically and refined at 2.0 angstrom resolution to an R value of 0.19 [4].
• Thermodynamics of monosaccharide and disaccharide binding to Erythrina corallodendron lectin [5].
• Trypsin inhibitor DE-3 from Erythrina latissima seeds contains 172 amino acids, including 4 half-cystine residues, and resembles the Kunitz-type inhibitors [6].
• Purification of human tissue plasminogen activator with Erythrina trypsin inhibitor [7].
• The structures of the Erythrina corallodendron lectin (EcorL) and of its complexes with galactose, N-acetylgalactosamine, lactose and N-acetyllactosamine were determined at a resolution of 1.9 to 1.95 A [8].

Biological context of Erythrina

• Structural features of the combining site region of Erythrina corallodendron lectin: role of tryptophan 135 [9].
• The tissue-type plasminogen activator inhibitor ETIa from Erythrina variegata: structural basis for the inhibitory activity by cloning, expression, and mutagenesis of the cDNA encoding ETIa [10].
• A newly isolated lectin Erythrina cristagalli (ECL) was tested for separation of human alpha-fetoprotein (AFP) glycoforms by affinity electrophoresis at 0.5 mg/ml and separated AFP bands were detected by antibody-affinity blotting [11].
• Amino acid sequence of chymotrypsin inhibitor ECI from the seeds of Erythrina variegata (Linn.) var. Orientalis [12].
• The Erythrina variegata Kunitz family trypsin inhibitors, ETIa and ETIb, prolonged the activated partial thromboplastin time (APTT) and also the prothrombin time (PT) of human plasma, but the Kunitz family chymotrypsin inhibitor, ECI, and Bowman-Birk family inhibitor, EBI, from E. variegata hardly prolonged these times [13].

Anatomical context of Erythrina

• A D-galactose-binding lectin agglutinating human erythrocytes has been purified from the seeds of the Indian coral tree (Erythrina variegata (Linn.) var. orientalis (Linn.) Merrill] by affinity chromatography on acid-treated Sepharose-6B gel [14].
• The binding of PNA, BPA, RCA-I, Erythrina cristagalli agglutinin (ECA), PHA-E and Glycine max agglutinin (SBA) to the subendothelial region of iris blood vessels closely resembled their binding to exfoliation material [15].

Associations of Erythrina with chemical compounds

• The galactose-specific lectin from Erythrina rubrinervia crystallizes in the hexagonal space group P6, (or P6(5)) with unit cell dimensions a = b = d = 135.1 A, c = 83.0 A [16].
• The lectin from Erythrina corallodendron, specific for N-acetyllactosamine, crystallizes in the hexagonal space group P6(1) (P6(5)) with unit cell dimensions a = b = 136.3 A, c = 83.2 A and one dimer of Mr 60,000 in the asymmetric unit [17].
• Crystals of a chymotrypsin inhibitor from Erythrina caffra seeds have been grown out of lithium sulfate, by the hanging drop method of vapor diffusion [18].
• While the Erythrina lectins show greater affinities and -delta H values for lactose and N-acetyllactosamine, the soybean agglutinin possesses similar affinities for methyl beta-galactopyranoside, lactose, and N-acetyllactosamine and a greater -delta H value for the monosaccharide [19].
• In the present study, we have used quantitative precipitation analysis to compare the cross-linking activities of the Gal/GalNAc-specific lectin from Erythrina corallodendron (ECorL) and the recombinant protein (rECorL) which lacks the covalently linked heptasaccharide chains of the native lectin, with ASF [20].

Gene context of Erythrina

• To remove the sugar moiety, CHIP28 was enzymatically deglycosylated by PNGase F and purified by Q-Sepharose anion-exchange and Erythrina cristagalli lectin chromatography [21].
• PA of the Cur eluate fraction gave a more complex pattern in that it bound significantly to fibrin (like TPA), was completely inhibited by both anti-UK and anti-TPA antibodies, but was unaffected by Erythrina trypsin inhibitor [22].
• AIMS: To screen 16 isoflavonoids isolated from Erythrina variegata (Leguminosae) for their antibacterial activity against methicillin-resistant Staphylococcus aureus (MRSA) [23].
• The Erythrina protease inhibitor: interactions with tissue plasminogen activator [24].
• Kunitz-type soybean trypsin inhibitor revisited: refined structure of its complex with porcine trypsin reveals an insight into the interaction between a homologous inhibitor from Erythrina caffra and tissue-type plasminogen activator [25].

Analytical, diagnostic and therapeutic context of Erythrina

• Modification by site-directed mutagenesis of the specificity of Erythrina corallodendron lectin for galactose derivatives with bulky substituents at C-2 [26].
• Light and electron microscopy demonstrated highly heterogeneous labeling of the zymogen granule contents of specific acinar cells with the lectins Ulex europaeus agglutinin (UEA) and Erythrina cristagalli (ECA), which also showed preferential labeling of peri-insular acini [27].
• Methyl alpha-N-dansyl-D-galactosaminide was used as a fluorescent indicator ligand in continuous substitution titrations to determine the association constants of nonchromophoric carbohydrates with the N-acetyl-D-galactosamine specific lectin from Erythrina corallodendron [28].
• The stoichiometry of the interaction between Erythrina variegata chymotrypsin inhibitor ECI and chymotrypsin was reinvestigated by analysis of their complex with ultracentrifugation and with amino acid analysis of the components separated [29].
• A sialylation-sensitive cell-based in vitro bioassay for erythropoietin; incorporation of the galactose-binding Erythrina crista-galli lectin [30].

References