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PubMed2001

Cyclooxygenase inhibiting and anti-bacterial activities of South African Erythrina species.

Aqueous, ethanolic and ethyl acetate extracts of the bark and leaves of five South African Erythrina species Erythrina caffra, Erythrina humeana, Erythrina latissima, Erythrina lysistemon and Erythrina zeyheri were screened for prostaglandin synthesis-inhibitory and anti-bacterial activity. The bark generally displayed higher activity than the leaves in both bioassays. The highest cyclooxygenase inhibiting activity and anti-bacterial activity was recorded for the ethanol and ethyl acetate bark extracts of E. caffra, E. latissima and E. lysistemon. An anti-bacterial compound, 4',5,7-trihydroxy-6-prenylisoflavone, was isolated by bioassay-guided fractionation from bark of E. lysistemon.

Anti-Infective Agents↗
PubMed1991

Erythrina lectins detect the H/HI blood groups.

The lectin purified from Erythrina corallodendron seeds which binds N-acetyllactosamine greater than N-acetyl-D-galactosamine greater than alpha and beta galactosides greater than D-galactose was examined for its ABO(H) blood group specificity. It has been shown that this lectin causes the strongest hemagglutination of O(H) and weakest of Oh(Bombay) red blood cells, and interacts with the H antigen in association with the I antigen. The reactions of Erythrina corallodendron and Erythrina indica lectins (which are similar in sugar specificity) with erythrocytes of different ABO(H) and Ii blood groups (the I bloods were all from adults and the i from either cord or adult bloods) revealed the following order of activity: O(H)I greater than A2 I greater than O(H)i adult greater than A2BI greater than BI greater than O(H)i cord greater than A1I greater than A1i adult greater than Bi cord greater than A1BI greater than Ai cord greater than ABi cord greater than OhI. The Erythrina indica lectin showed a lower differentiation between the agglutination of O(H) and Oh erythrocytes. Both Erythrina lectins exhibited H/HI blood group preference but were not inhibited by the saliva from ABO(H) "secretors". Thus they may be classified with the Cytisus sessilifolius, Lotus tetragonolobus and Laburnum alpinum lectins which are inhibited by lactose but not by H blood group substances in secretions.

ABO Blood-Group System↗
PubMed1989

Binding and precipitating activities of Erythrina lectins with complex type carbohydrates and synthetic cluster glycosides. A comparative study of the lectins from E. corallodendron, E. cristagalli, E. flabelliformis, and E. indica.

Erythrina lectins possess similar structural and carbohydrate binding properties. Recently, tri- and tetra-antennary complex type carbohydrates with non-reducing terminal galactose residues have been shown to be precipitated as tri- and tetravalent ligands, respectively, with certain Erythrina lectins [Bhattacharyya L, Haraldsson M, Brewer CF (1988) Biochemistry 27:1034-41]. The present work describes a comparative study of the binding and precipitating activities of four Erythrina lectins, viz., E. corallodendron, E. cristagalli, E. flabelliformis, and E. indica, with multi-antennary complex type carbohydrates and synthetic cluster glycosides. The results show that though their binding affinities are very similar, the Erythrina lectins show large differences in their precipitating activities with the carbohydrates. The results also indicate significant dependence of the precipitating activities of the lectins on the core structure of the carbohydrates. These findings provide a new dimension to the structure-activity relationship of the lectins and their interactions with asparagine-linked carbohydrates.

Carbohydrate Conformation↗
PubMed1995

Purification and characterization of a lectin from the seeds of Erythrina costaricensis.

This work compares three methods used for the purification of the lectin of Erythrina costaricensis and presents new data regarding its physicochemical properties and N-terminal sequence. The lectin was isolated from the seeds of Erythrina costaricensis using O-alpha-D galactosyl polyacrylamide, galactose-derivatized Sepharose and ConA-Sepharose as affinity chromatography supports. The lectin content is about 110 mg/100 g dry flour. The protein agglutinates human and rabbit erythrocytes; other animal erythrocytes were not agglutinated. The agglutination is inhibited by galactosyl moieties, p-nitrophenyl-beta-galactoside being the strongest inhibitor. The lectin is a dimeric protein (56 kDa) with identical subunits, each with a mol. wt of 27.2 kDa. The lectin is a glycoprotein with 3.6% neutral sugars. The amino acid content shows a high proportion of acidic and hydroxy residues; cysteine is absent and there are 6 methionines/mol protein. The N-terminal sequence is similar to those of Erythrina lectins; Ala is the N-terminal amino acid. In summary this paper reports the isolation of a lectin which shares many structural and functional properties with other Erythrina lectins. However, differences in some of its characteristics (pI, interactions with animal erythrocytes, mitogenic ability) indicate some distinctions in structure amongst this group of proteins.

Amino Acid Sequence↗
PubMed1994

Differences in the cross-linking activities of native and recombinant Erythrina corallodendron lectin with asialofetuin. Evidence for carbohydrate-carbohydrate interactions in lectin-glycoprotein complexes.

A previous study showed that several multivalent galactose-specific lectins including the 14-kDa lectin from calf spleen and the lectins from Erythrina indica, Erythrina cristagalli, and soybean agglutinin formed specific cross-linked complexes with the glycoprotein asialofetuin (ASF) [Mandal, D. K., & Brewer, C. F. (1992) Biochemistry 31, 8465-8472]. 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. At low concentrations of ASF relative to the lectin, native dimeric ECorL binds to each of the three terminal Gal residues of the three N-linked triantennary chains of ASF and precipitates as a cross-linked complex at a ratio of 1:9 ASF/lectin (monomer). With increasing concentrations of ASF, the 1:9 complex changes to a 1:3 ASF/lectin complex, and at higher ASF concentrations, a 1:1 cross-linked complex forms. However, rECorL, which possesses the same specificity and binding affinity as the native lectin, forms only the 1:9 and 1:3 ASF/lectin complexes. Other Erythrina lectins examined, all of which have covalently attached carbohydrate and are structurally similar to ECorL, show the same cross-linking behavior as native ECorL. On the other hand, the dimeric 14-kDa calf spleen lectin which lacks covalently attached carbohydrate forms only 1:9 and 1:3 cross-linked complexes with ASF [Mandal, D. K., & Brewer, C. F. (1992) Biochemistry 31, 8465-8472].(ABSTRACT TRUNCATED AT 250 WORDS)

Asialoglycoproteins↗
PubMed2006

Antibacterial pterocarpans from Erythrina subumbrans.

Seven pterocarpans, erybraedin B (1), erybraedin A (2), phaseollin (3), erythrabyssin II (4), erystagallin A (5), erythrabissin-1 (6) and erycristagallin (7), two flavanones, 5-hydroxysophoranone (8) and glabrol (9), and one isoflavone, erysubin F (10), were isolated from the stems of Erythrina subumbrans (Leguminosae). Their structures were identified by means of spectroscopy. This is the first report of the isolation of the non-alkaloidal compounds from Erythrina subumbrans and the observed dehydration of 6a-hydroxypterocarpans 5 and 6 in CDCl(3) to the corresponding pterocarpenes 11 and 12, respectively. Compounds 8 and 9 were isolated for the first time from the genus Erythrina. Compounds 2 and 4 exhibited the highest degree of activity against Streptococcus strains with an MIC range of 0.78-1.56 microg/ml, whereas compound 7 exhibited the highest degree of activity against Staphylococcus strains, including drug-resistant strains (MRSA and VRSA), with an MIC range of 0.39-1.56 microg/ml. Interestingly, compounds 2, 4, 5 and 7 were more active against several strains of Streptococcus and Staphylococcus than the standard antibiotics vancomycin and oxacillin. Compound 7 showed the highest level of activity against all VRSA strains tested, with an MIC range of 0.39-1.56 microg/ml, which were resistant to both antibiotics. These compounds may prove to be potent phytochemical agents for antibacterial activity, especially against the MRSA and VRSA strains.

Anti-Bacterial Agents↗
PubMed1986

Affinity of four immobilized Erythrina lectins toward various N-linked glycopeptides and related oligosaccharides.

The behavior of N-acetyllactosamine-type oligosaccharides and glycopeptides on columns of four different Erythrina agglutinins immobilized on Sepharose was examined. The sugar-binding specificity of the four lectins is very similar and is directed toward unmasked N-acetyllactosamine sequences, the main difference between the four lectins being the relative strength of interaction of the lectins with a given glycan. Substitution of the N-acetyllactosamine sequences by sialic acid residues, either at O-3 or O-6 of galactose completely abolishes the affinity of the lectins for the saccharides. The presence of one or several alpha-Fuc-(1----3)-GlcNAc groups decreases or completely inhibits the interaction between the glycopeptides and the Erythrina lectins. Substitution of the beta-mannose residue by an additional bisecting beta-(1----4)-N-acetylglucosamine residue decreases the affinity of the lectins for these structures as compared to the unsubstituted ones. Surprisingly, the affinity of the lectins for the oligosaccharides tested is higher than for the corresponding glycopeptides. Our findings show that, after careful calibration with well-defined oligosaccharides and glycopeptides, the immobilized Erythrina agglutinin-Sepharose columns provide valuable tools for the fractionation of N-acetyllactosamine-containing oligosaccharides and glycopeptides.

Carbohydrate Conformation↗
PubMed2002

Purification, some properties of a D-galactose-binding leaf lectin from Erythrina indica and further characterization of seed lectin.

Lectin from a leaf of Erythrina indica was isolated by affinity chromatography on Lactamyl-Seralose 4B. Lectin gave a single band in polyacrylamide gel electrophoresis (PAGE). In SDS-gel electrophoresis under reducing and non-reducing conditions Erythrina indica leaf lectin (EiLL) split into two bands with subunit molecular weights of 30 and 33 kDa, whereas 58 kDa was obtained for the intact lectin by gel filtration on Sephadex G-100. EiLL agglutinated all human RBC types, with a slight preference for the O blood group. Lectin was found to be a glycoprotein with a neutral sugar content of 9.5%. The carbohydrate specificity of lectin was directed towards D-galactose and its derivatives with pronounced preference for lactose. EiLL had pH optima at pH 7.0; above and below this pH lectin lost sugar-binding capability rapidly. Lectin showed broad temperature optima from 25 to 50 degrees C; however, at 55 degrees C EiLL lost more than 90% of its activity and at 60 degrees C it was totally inactivated. The pI of EiLL was found to be 7.6. The amino acid analysis of EiLL indicated that the lectin was rich in acidic as well as hydrophobic amino acids and totally lacked cysteine and methionine. The N-terminal amino acids were Val-Glu-Thr-IIe-Ser-Phe-Ser-Phe-Ser-Glu-Phe-Glu-Ala-Gly-Asn-Asp-X-Leu-Thr-Gln-Glu-Gly-Ala-Ala-Leu-. Chemical modification studies of both EiLL and Erythrina indica seed lectin (EiSL) with phenylglyoxal, DEP and DTNB revealed an absence of arginine, histidine and cysteine, respectively, in or near the ligand-binding site of both lectins. Modification of tyrosine with NAI led to partial inactivation of EiLL and EiSL; however, total inactivation was observed upon NBS-modification of two tryptophan residues in EiSL. Despite the apparent importance of these tryptophan residues for lectin activity they did not seem to have a direct role in binding haptenic sugar as D-galactose did not protect lectin from inactivation by NBS.

Amino Acid Sequence↗
PubMed1996

Effect of disulfide bonds on the structure, function, and stability of the trypsin/tPA inhibitor from Erythrina caffra: site-directed mutagenesis, expression, and physiochemical characterization.

Erythrina trypsin/tPA inhibitor (ETI) from the seeds of Erythrina caffra retains its native structure and inhibitory function after reducing its two disulfide bonds. In order to elucidate the specific role of these crosslinks, alanine residues were substituted for cysteines after cloning the gene in Escherichia coli. Expression of the recombinant inhibitor and the substitution mutants, C83A, CC39, 83AA, and CC132, 139AA, led to inclusion bodies. After solubilization in guanidinium-chloride (GdmCl)/dithiothreitol and oxidation in glutathione buffer, activity could be recovered at yields up to 80%. The mutant proteins exhibit full inhibitory function without detectable alterations of their native structure. However, their stability is reduced: at acid pH, where the oxidized natural inhibitor retains its native structure, the reduced wildtype protein and the mutants undergo at least partial denaturation, reflected by decreased pH ranges of stability: pH 5-7 for the reduced inhibitor, pH 2.5-8.5 for CC132, 139AA, and pH 3.5-8.5 for C83A and CC39, 83AA. Urea and GdmCl denaturation at pH 7 show hysteresis for both the oxidized inhibitor and the double mutant CC132, 139AA. In contrast, the reduced protein and the other mutants exhibit true equilibrium transitions at pH 7, with urea half-concentrations of 0.9 M and 1.9 M and GdmCl half-concentrations of 0.5 M and 1.0 M, respectively. The stability of Erythrina trypsin/tPA inhibitor follows the sequence: oxidized ETI > CC132, 139AA > CC39, 83AA and C83A > reduced ETI.

Amino Acid Sequence↗
PubMed2003

Exploitation of Erythrina dominguezii Hassl. (Fabaceae) nectar by perching birds in a dry forest in western Brazil.

Among the vertebrate pollinated plants, the genus Erythrina includes tree species in which birds are the pollen vectors. Two groups in this genus may be distinguished: a) the hummingbird, and b) the perching bird pollinated species. Erythrina dominguezii is included in the second group and occurs in deciduous/semi-deciduous forests in the southwestern neotropics. I studied the exploitation of Erythrina dominguezii nectar by perching birds in a dry forest in western Brazil. Six perching bird species from two distinct groups (Psittacidae: Brotogeris chiriri, Nandayus nenday, Aratinga acuticaudata; Icterinae: Psarocolius decumanus, Icterus cayanensis, I. icterus) consumed its nectar. The two most important consumers were Brotogeris chiriri (51.5% of the flowers visited by birds) and Psarocolius decumanus (20%). While B. chiriri was a flower predator, P. decumanus removed the nectar without damaging the flowers which it opened by inserting its large bill between the standard and the keel. Nandayus nenday, Aratinga acuticaudata, and I. icterus exploited the nectar like P. decumanus, and presumably also contributed to pollen transfer. As the flowering in E. dominguezii was intense and synchronous during the dryest period of the year, and its nectar was highly consumed by birds, the present data suggest that the nectar of this species may be important as an alternative resource to frugivorous/omnivorous birds when other resources are scarce.

Animals↗