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Evaluation of antimicrobial activity of a lectin isolated and purified from Indigofera heterantha  [PDF]
Sakeena Qadir, Ishfak Hussain Wani, Shaista Rafiq, Showkat Ahmad Ganie, Akbar Masood, Rabia Hamid
Advances in Bioscience and Biotechnology (ABB) , 2013, DOI: 10.4236/abb.2013.411133

Indigofera heterantha commonly called indigo bush is a member of leguminoseae family found in the Himalayan region of Kashmir. A lectin has been isolated from the seeds of Indigofera heterantha by the purification procedure involving anion exchange chromatography on DEAE-cellulose followed by gel filtration chromatography on Sephadex G 100. Molecular characterization of the lectin was done by gel filtration and SDS-PAGE. Activity of the lectin was checked by hemagglutination assay and the sugar specificity by sugar inhibition tests. The antimicrobial activity of the purified lectin was carried out by Agar disc diffusion using appropriate standards. On the ion exchange column, the bound protein when eluted with 0-0.5 M NaCl gradient emerged as three peaks—peak I, peak II and peak III out of which only peak II showed the hemagglutinating activity. The lectin further resolved into two peaks G1 and G2 on gel filtration, with the lectin activity residing in G1, corresponding to a molecular weight of 70 KDa. The purified lectin named as Indigofera heterantha Lectin (IHL) produced a single band on SDS PAGE (18 KDa), revealing the tetrameric nature of the lectin. It agglutinated human erythrocytes (A, B, AB, and O). Hemagglutination was inhibited by D-galactose, Dmannose and D-arabinose. The lectin is reasonably thermostable showing full activity within a temperature range of 30°C to 90°C. pH stability of the lectin falls in the range of 2-9. IHL demonstrated a remarkable antibacterial activity against the pathogenic bacteria Klebsiella pneumoniae, Staphylococcus aureus, Escherichia coli, and Bacillus subtilis. IHL also inhibited the growth

Antimicrobial Activity of Indigofera suffruticosa  [PDF]
S nia Pereira Leite,Jeymesson Raphael Cardoso Vieira,Paloma Lys de Medeiros,Roberta Maria Pereira Leite,Vera Lúcia de Menezes Lima,Haroudo Satiro Xavier,Edeltrudes de Oliveira Lima
Evidence-Based Complementary and Alternative Medicine , 2006, DOI: 10.1093/ecam/nel010
Abstract: Various organic and aqueous extracts of leaves of Indigofera suffruticosa Mill (Fabaceae) obtained by infusion and maceration were screened for their antibacterial and antifungal activities. The extracts were tested against 5 different species of human pathogenic bacteria and 17 fungal strains by the agar-solid diffusion method. Most of the extracts were devoid of antifungal and antibacterial activities, except the aqueous extract of leaves of I. suffruticosa obtained by infusion, which showed strong inhibitory activity against the Gram-positive bacteria Staphylococcus aureus with a minimal inhibitory concentration (MIC) of 5000 μg ml−1. The MIC values to dermatophyte strains were 2500 μg ml−1 against Trichophyton rubrum (LM-09, LM-13) and Microsporum canis. This study suggests that aqueous extracts of leaves of I. suffruticosa obtained by infusion can be used in the treatment of skin diseases caused by dermatophytes.
Crystallization and Characterization of an Inflammatory Lectin Purified from the Seeds of Dioclea wilsonii  [PDF]
Thaiz Batista Azevedo Rangel,Ana Maria Sampaio Assreuy,Alana de Freitas Pires,Amanda Uliana de Carvalho,Raquel Guimar?es Benevides,Rafael da Concei??o Sim?es,Helton Colares da Silva,Maria Júlia Barbosa Bezerra,Antonia Samia Fernandes do Nascimento,Kyria Santiago do Nascimento,Celso Shiniti Nagano,Alexandre Holanda Sampaio,Plínio Delatorre,Bruno Anderson Matias da Rocha,Patricia Machado Bueno Fernandes,Benildo Sousa Cavada
Molecules , 2011, DOI: 10.3390/molecules16065087
Abstract: DwL, a lectin extracted from the seeds of Dioclea wilsonii, is a metalloprotein with strong agglutinating activity against rabbit and ABO erythrocytes, inhibited by glucose and mannose. DwL was purified by affinity chromatography on a Sephadex G-50 column and ion exchange chromatography on a HiTrap SP XL column. SDS-PAGE revealed three electrophoretic bands corresponding to the α (25,634 ± 2 Da), β (12,873 ± 2 Da) and γ (12,779 ± 2 Da) chains. Protein sequencing was done by Tandem Mass Spectrometry. The primary sequence featured 237 amino acids and was highly homologous to other reported Diocleinae lectins. A complete X-ray dataset was collected at 2.0 ? for X-Man-complexed DWL crystals produced by the vapor diffusion method. The crystals were orthorhombic and belonged to the space group I222, with the unit-cell parameters a = 59.6, b = 67.9 and c = 109.0 ?. DWL differed in potency from other ConA-like lectins and was found to induce neutrophil migration in rats, making it particularly useful in structural/functional studies of this class of proteins.
Carbohydrate specificity of lectin, purified from the fruiting bodies of Mycena pura /Fr./ Kumm. and its use in histochemical investigation  [PDF]
Antonyuk V. O.,Yastchenko A. M.,Antonyuk R. V.,Ambarova N. O.
Biopolymers and Cell , 2009,
Abstract: Aim. The purpose of this investigation was to research carbohydrate specificity of a new lectin from fruiting body of Mycena pura and possibilities of its application in histochemical studies. Methods. The lectin has been purified by affinity chromatography on vomucine . The lectin carbohydrate specificity has been determined by a reaction of inhibiting haemagglutination by haptens. Histological materials were fixed in 4 % neutral formalin solution. Alkaline phosphatase was revealed in the cryostat unfixed microscopical sections. Results. The lectin yield from fresh fruit bodies of raw material was 9 mg/kg. Mol. mass of the lectin is 40 kDa. The lectin poorly interacted with D-glucose and D-mannose in contrast to lectins from Pisum sativum and Leucojum vernum. The peculiarity of this lectin is its strong interaction with alkaline phosphatase, the highest among twenty tested lectins. However, the receptors for Mycena lectin binding in mammalian tissues are not limited by this enzyme being presented also by glycoconjugates of another structure, as it was shown for fetus calf small intestine and kidney of rat. Conclusions. An important role in the lectin interaction with glycoproteins probably belongs to the disaccharide links of GlcNAcb(1-2)Mana(1-6) or GlcNAcb(1- 2)Mana(1-2), which not necessarily are terminal
Biological Properties of Lectin from Sea Cucumber (Holothuria scabra Jaeger)  [PDF]
Elmer-Rico E. Mojica,Florinia E. Merca
Journal of Biological Sciences , 2005,
Abstract: A lectin isolated and purified by gel chromatography from the internal organs of Holothuria scabra Jaeger was assayed for different biological properties. The lectin was found to have hemolytic and mitogenic activities. It was also found to be a good inhibitor of seed germination and inhibited the germination of radish seeds. LC50 against Artemia salina is lower than commercial therapeutic agents. No antimicrobial, antiprotozoal, clastogenic, insecticidal and molluscicidal activities were observed.
Purification and Characterization of a D-Galactoside-Binding Lectin Purified from Bladder Moon Shell (Glossaulax didyma Roding)  [PDF]
Y. Fujii,S.M.A. Kawsar,R. Matsumoto,H. Yasumitsu
Journal of Biological Sciences , 2009,
Abstract: To find novel carbohydrate-binding proteins (lectins) from marine invertebrates to understand the binding mechanism of the protein and to apply it for glycan-dependent diagnostics and/or glycoconjugates capture technology. A D-galactoside-binding lectin was purified from foot of bladder moon shell, Glossaulax didyma by lactosyl-agarose affinity chromatography. The crude supernatant by Tris-buffered saline had strong hemagglutination activity against trypsinized and glutaraldehyde-fixed human erythrocyte. However, the activity was not inhibited by any tested saccharides and chilete reagents. On the other hand, the dialyzed crude supernatant obtained from the precipitates with 100 mM lactose in Tris-buffered saline had also hemagglutination activity inhibited by β-galactoside and D-galactose. The lectin was purified with lactosyl-agarose affinity chromatography. The molecular mass of the lectin was determined to be 60 kDa by SDS-PAGE under reducing and non-reducing conditions and being a 60 kDa polypeptide monomer by gel permeation chromatography. The association-rate constant (kass) and dissociation-rate constant (kdiss) determined for the lectin against asialofetuin was determined as 5.4x104 M-1sec-1 and 7.2x10-3sec-1, respectively. Lectin-conjugated Sepharose gel captured asialofetuin and eluted it by lactose-containing buffer from the gel, indicating that the lectin could catch the asialoglycoprotein. It was concluded that a many amount of a D-galactoside-binding lectin which can catch asialoglycoprotein presents in foot of the bladder moon shell.
Purification, Biochemical Characterization, and Bioactive Properties of a Lectin Purified from the Seeds of White Tepary Bean (Phaseolus Acutifolius Variety Latifolius)  [PDF]
Carmen Valadez-Vega,Ana María Guzmán-Partida,Francisco Javier Soto-Cordova,Gerardo álvarez-Manilla,José A. Morales-González,Eduardo Madrigal-Santillán,José Roberto Villagómez-Ibarra,Clara Zú?iga-Pérez,José Gutiérrez-Salinas,Marco A. Becerril-Flores
Molecules , 2011, DOI: 10.3390/molecules16032561
Abstract: The present work shows the characterization of Phaseolus acutifolius variety latifolius, on which little research has been published, and provides detailed information on the corresponding lectin. This protein was purified from a semi-domesticated line of white tepary beans from Sonora, Mexico, by precipitation of the aqueous extract with ammonium sulfate, followed by affinity chromatography on an immobilized fetuin matrix. MALDI TOF analysis of Phaseolus acutifolius agglutinin (PAA) showed that this lectin is composed of monomers with molecular weights ranging between 28 and 31 kDa. At high salt concentrations, PAA forms a dimer of 63 kDa, but at low salt concentrations, the subunits form a tetramer. Analysis of PAA on 2D-PAGE showed that there are mainly three types of subunits with isoelectric points of 4.2, 4.4, and 4.5. The partial sequence obtained by LC/MS/MS of tryptic fragments from the PAA subunits showed 90–100% identity with subunits from genus Phaseolus lectins in previous reports. The tepary bean lectin showed lower hemagglutination activity than Phaseolus vulgaris hemagglutinin (PHA-E) toward trypsinized human A and O type erythrocytes. The hemagglutination activity was inhibited by N-glycans from glycoproteins. Affinity chromatography with the immobilized PAA showed a high affinity to glycopeptides from thyroglobulin, which also has N-glycans with a high content of N-acetylglucosamine. PAA showed less mitogenic activity toward human lymphocytes than PHA-L and Con A. The cytotoxicity of PAA was determined by employing three clones of the 3T3 cell line, demonstrating variability among the clones as follows: T4 (DI50 51.5 μg/mL); J20 (DI50 275 μg/mL), and N5 (DI50 72.5 μg/mL).
Human neutrophil migration and activation by BJcuL, a galactose binding lectin purified from Bothrops jararacussu venom
Selene Elifio-Esposito, Luciane Tomazeli, Carolina Schwartz, Ana Gimenez, Gabriel M Fugii, Luiz Fernandes, Luciana FM Zishler, Patrícia M Stuelp-Campelo, Andréa N Moreno
BMC Immunology , 2011, DOI: 10.1186/1471-2172-12-10
Abstract: Utilizing fluorescence microscopy, we observed that biotinylated-BJcuL was evenly distributed on the neutrophil surface, selectively inhibited by D-galactose. Lectin was able to induce modification in the neutrophil morphology in a spherical shape for a polarized observed by optical microscopy and exposure to BJcuL in a Boyden chamber assay resulted in cell migration. After 30 minutes of incubation with BJcuL we found enhanced neutrophil functions, such as respiratory burst, zymozan phagocytosis and an increase in lissosomal volume. In addition, BJcuL delays late apoptosis neutrophils.These results demonstrate that BJcuL can be implicated in a wide variety of immunological functions including first-line defense against pathogens, cell trafficking and induction of the innate immune response since lectin was capable of inducing potent neutrophil activation.Neutrophils are key players in the innate immune response and their recruitment from the microvasculature to inflammation sites includes rolling, firm adhesion, and transmigration through the vessel wall [1]. Neutrophil activation leads to directed migration with changes in cell morphology from rounded cells covered with microvilli to elongated ruffled cells [2,3]. Neutrophils exert their bactericidal activity at the inflammatory site through recognition and phagocytosis of the infectious agent, generation of toxic oxygen derivatives, and release of microbicidal molecules from their specialized lysosomes and granules [4]. This sequential process relies on neutrophil interaction with chemoattractants, cytokines and other inflammatory mediators [5].Viperid and elapid snake venoms contain complex mixtures of pharmacologically active molecules, including enzymes and proteins without enzymatic activity, such as C-type lectins. Based on their structural and functional properties snake venom C-type lectins have been classified as true C-type lectins, which contain a carbohydrate recognition domain (CRD) and bind to a speci
Antimicrobial Peptides Purified from Penus chinensis

AN Xian-hui,LV Yi,LI Wei-guo,LIANG Jian-guo,XU Chun-hua,ZHANG Chong-xing,DONG Jing,LAI Ren,

动物学研究 , 2005,
Abstract: Two antimicrobial peptides were purified from Penus chinensis by Sephadex G-50 gel filtration and reverse phase high performance liquid chromatography. The molecular weights were 1 071 and 1 311 Da respectively, determined by matrix-assisted laser desorption ionization time-of-flight (MALDI-TOF) mass spectrometry. They inhibited the growth of Gram-positive and Gram-negative bacteria. The antimicrobial peptides strengthened the contractile response of isolated mice ileum. Serine proteases did not affect hydrolytic activities in our current experiments. These antimicrobial peptides play an important role in preventing microbial infection in P. chinensis.
Badri Tavasolian,S Mottaghian
Iranian Journal of Public Health , 1979,
Abstract: Iranian castor bean lectin was isolated and purified by several column chromatography methods. Then, the sugar and amino acid content of the purified lectin was identified. Castor bean lectin has some anti tumor and anti leukemia action. Thus it may be used commercially for medical and biochemical purposes.
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