N Gilboa-Garber

Chang Gung University, Taoyuan, Taiwan, Taiwan

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Publications (84)204.38 Total impact

  • Ofra Rachmaninov, Keren D Zinger-Yosovich, Nechama Gilboa-Garber
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    ABSTRACT: Ralstonia solanacearum wilts many plants, causing heavy agricultural losses. Its pathogenic strain ATCC 11696 produces 2 hemagglutinating lectins: RSL and RS-IIL. These lectins may bind to terminal l-fucose-, d-arabinose-, and d-mannose-bearing seedling xylem cell wall glycans, thus enabling pathogen adhesion to them, with devastating infection establishment. Blocking the active sites of these lectins with seed embryo-surrounding oligo- and poly-saccharides hampers binding of the lectins to the embryos. The current study shows that seeds of cashew, cocoa, coffee, pumpkin, and tomato contain low and high molecular mass glycans that block RSL and RS-IIL (like its homologous Pseudomonas aeruginosa PA-IIL lectin). The blocking of the pathogen lectins, which is attributable to the documented composition of the oligo- and poly-saccharides of these seeds, is similar to that observed with animal glycoproteins of avian egg whites (protecting their embryos from infections) and of milk and royal jelly, which likewise protect mammal and bee neonates, respectively. RSL was most strongly inhibited by cashew seed glycans, and RS-IIL by coffee seed glycans. Western blot analyses with these lectins instead of antibodies revealed the hitherto undescribed presence of lectin-binding glycoproteins in the coffee, pumpkin, tomato, and cashew (but not cocoa) seeds. The use of these lectins for unveiling potent embryo-protecting seed glycans might be helpful for seedling-bioprotection projects similar to those planned for animal protection against antibiotic-resistant infections.
    Canadian Journal of Microbiology 06/2012; 58(7):856-62. · 1.20 Impact Factor
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    ABSTRACT: Owing to the weak reactivities of monomeric DManα1 and Galβ1-->3/4GlcNAcβ (I(β)/II(β)) glycotopes with Ralstonia solanacearum lectin (RSL), their recognition roles were previously ignored. In this study, the interaction intensities of RSL toward four monomeric glycotopes LFucα1-->, DManα1--> and I(β)/II(β) within two combining sites were established by both enzyme-linked lectinosorbent and inhibition assays. It was found that high density of LFucα1--> complex enhanced the recognition intensities at LFucα1--> site, polyvalent DManα1--> was essential for binding at the DManα1--> site and polyvalent I(β)/II(β) was required at LFucα1--> site. The peculiar recognition systems of RSL are very different from other well known microbial lectins.
    FEBS letters 05/2012; 586(9):1294-9. · 3.54 Impact Factor
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    Ofra Rachmaninov, Keren D Zinger-Yosovich, Nechama Gilboa-Garber
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    ABSTRACT: Pseudomonas aeruginosa adhesion to animal/human cells for infection establishment involves adhesive proteins, including its galactose- and fucose-binding lectins PA-IL (LecA) and PA-IIL (LecB). The lectin binding to the target-cell receptors may be blocked by compatible glycans that compete with those of the receptors, functioning as anti-adhesion glycodecoys. The anti-adhesion treatment is of the utmost importance for abrogating devastating antibiotic-resistant P. aeruginosa infections in immunodeficient and cystic fibrosis (CF) patients. This strategy functions in nature in protecting embryos and neonates. We have shown that PA-IL, PA-IIL, and also CV-IIL (a PA-IIL homolog produced in the related pathogen Chromobacterium violaceum) are highly useful for revealing natural glycodecoys that surround embryos in diverse avian eggs and are supplied to neonates in milks and royal jelly. In the present study, these lectins were used as probes to search for seed embryo-protecting glycodecoys. The lectin-blocking glycodecoy activities were shown by the hemagglutination-inhibition test. Lectin-binding glycoproteins were detected by Western blotting with peroxidase-labeled lectins. The present work reports the finding - by using PA-IL, PA-IIL, and CV-IIL - of rich glycodecoy activities of low (< 10 KDa) and high MW (> 10 kDa) compounds (including glycoproteins) in extracts of cashew, cocoa, coffee, pumpkin, and tomato seeds, resembling those of avian egg whites, mammal milks, and royal jelly. Edible seed extracts possess lectin-blocking glycodecoys that might protect their embryos from infections and also might be useful for hampering human and animal infections.
    Nutrition Journal 02/2012; 11:10. · 2.65 Impact Factor
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    ABSTRACT: Milk indigested glycans hamper infections by blocking pathogen adhesion to babies’ cells via lectins (sugar-binding proteins). This study describes usage of five pathogenic bacterial lectins and two plant lectins for analyses of alpaca, buffalo, camel, cow, dog, fallow deer, giraffe, goat, horse, human, rabbit, and sheep milks, and also commercial human and cow milk lactoferrins. The lectins used differentially reacted with the 12 milks – most strongly with humans’ ones. Most of them (excluding Pseudomonas aeruginosa galactophilic PA-IL) were also sensitive to the human and cow lactoferrins. The fucophilic bacterial lectins were most sensitive to human lactoferrin, while the mannophilic ones – to the cow’s. The actual function of bacterial lectins in pathogen adhesion and their non-glycosylated structures (evading non-specific interactions) are advantageous for such studies. This study shows the efficiency of the bacterial lectins for milk analyses: differentiating between the diverse milks, estimating their anti-infection potentials, and probing their active glycans.
    Food Chemistry 02/2011; 124(4):1335-1342. · 3.33 Impact Factor
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    ABSTRACT: Among the ten different lectins discovered in the old biochemistry laboratory at Bar-Ilan University during the years 1972–2006 (Fig. 9.1), five were isolated from three soil bacteria: Pseudomonas aeruginosa (PA) [1–3], Ralstonia solanacearum (RS) [4, ], and Chromobacterium violaceum (CV) [6].
    Advances in experimental medicine and biology 01/2011; 705:155-211. · 1.83 Impact Factor
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    ABSTRACT: The worldwide-distributed Pseudomonas aeruginosa (PA) and the geographically restricted (confined to tropical and subtropical zones) Ralstonia solanacearum and Chromobacterium violaceum are Gram-negative proteobacteria that dwell in soil and water. They are essentially beneficial saprophytes that vigorously decompose plant and animal remnants and organic debris, contributing to world carbon and nitrogen cycling (Fig. 11.1). In accordance with their distinguished role in nature, these bacteria are endowed with very prosperous arsenals of cell-binding adhesins, toxicating proteinaceous and nonproteinaceous factors, and hydrolytic enzymes as virulence factors (VIFs), enabling them to home in on dead or damaged cells and molecules and attack them.
    Advances in experimental medicine and biology 01/2011; 705:229-56. · 1.83 Impact Factor
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    David Iluz, Miri Hoffman, Nechama Gilboa-Garber, Zohar Amar
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    ABSTRACT: Commiphora gileadensis is a plant that was cultivated in ancient times in the land of Israel, particularly in the oases of the Dead Sea Basin — Ein Gedi and Jericho. The plant, also known as balsam, was renowned for the expensive perfume that was produced from it, as well as for exceptional medicinal properties that were attributed to its sap, wood, bark, and seeds. This article presents the historical sources describing these health-related properties and preliminary laboratory studies demonstrating the pharmacological effects of balsam sap. Investigations of the antimicrobial activity of C. gileadensis showed the plant sap inhibitory effect against Bacillus cereus and the blocking of Pseudomonas aeruginosa lectins. These results corroborate the historical sources crediting the usefulness of balsam sap as an antiseptic agent.
    African journal of pharmacy and pharmacology 09/2010; 4:516-520. · 0.84 Impact Factor
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    Albert M Wu, Yu-Ping Gong, Chia-Chen Li, Nechama Gilboa-Garber
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    ABSTRACT: The study of Pseudomonas aeruginosa-II lectin (PA-IIL) complexes with Man derivatives as a recognition factor has been neglected since its monomer is a very weak ligand. Here, the roles of Man oligomers and complexes in PA-IIL carbohydrate-recognition were studied by both enzyme-linked lectinosorbent and inhibition assays. From the results obtained, it is proposed that high density weak -OH conformation as seen in yeast mannan is also an important PA-IIL recognition factor. This finding provides a peculiar concept of the duality of PA-IIL recognition system for LFucalpha1--> and related complexes and for high density Manalpha1--> complexes present in polymannosylated target macromolecules.
    FEBS letters 06/2010; 584(11):2371-5. · 3.54 Impact Factor
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    ABSTRACT: Pseudomonas aeruginosa and Chromobacterium violaceum morbid and mortal infections are initiated by bacterial adherence to host-cell receptors via their adhesins, including lectins (which also contribute to bacterial biofilm formation). Pseudomonas aeruginosa produces a galactophilic lectin, PA-IL (LecA), and a fucophilic (Lewis-specific) lectin, PA-IIL (LecB), and C. violaceum produces a fucophilic (H-specific) lectin, CV-IIL. The antibiotic resistance of these bacteria prompted the search for glycosylated receptor-mimicking compounds that would function as glycodecoys for blocking lectin attachment to human cell receptors. Lectins PA-IL and PA-IIL have been shown to be useful for such glycodecoy probing, clearly differentiating between human and cow milks. This article describes their usage, together with CV-IIL and the plant lectin concanavalin A, for comparing the anti-lectin-dependent adhesion potential of diverse mammalian milks. The results show that the diverse milks differ in blocking (hemagglutination inhibition) and differential binding (Western blots) of these lectins. Human milk most strongly inhibited the 3 bacterial lectins (with PA-IIL superiority), followed by alpaca, giraffe, and monkey milks, whereas cow milk was a weak inhibitor. Lectin PA-IL was inhibited strongly by human, followed by alpaca, mare, giraffe, buffalo, and monkey milks, weakly by camel milk, and not at all by rabbit milk. Lectins PA-IIL and CV-IIL were also most sensitive to human milk, followed by alpaca, monkey, giraffe, rabbit, and camel milks but negligibly sensitive to buffalo and mare milks. Plant lectin concanavalinA, which was used as the reference, differed from them in that it was much less sensitive to human milk and was equally as sensitive to cow milk. These results have provided important information on the anti-lectin-dependent adhesion potential of the diverse milks examined. They showed that human followed by alpaca, giraffe, and Rhesus monkey milks efficiently blocked the binding of both the galactophilic and fucophilic (>mannophilic) pathogen lectins. The results also proved the advantage of isolated pathogenic bacterial lectins as superb probes for unveiling bacterial adhesion-blocking glycodecoys. The chosen milks or their polymeric glycans might be implicated in blocking lectin-dependent adhesion of antibiotic-resistant pathogens leading to skin, eye, ear, and gastrointestinal infections.
    Journal of Dairy Science 02/2010; 93(2):473-82. · 2.57 Impact Factor
  • Keren D Zinger-Yosovich, Nechama Gilboa-Garber
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    ABSTRACT: Pseudomonas aeruginosa antibiotic resistance prompted the search for glycodecoys that would block its lectin-dependent adhesion to human cells. We have used the lectins of this pathogen, PA-IL (galactophilic LecA) and PA-IIL (fucophilic LecB), and two additional pathogenic bacterial lectins, CV-IIL (fucophilic, of Chromobacterium violaceum) and RS-IIL (mannophilic, of Ralstonia solanacearum), for assaying the pathogenic lectin-blocking abilities of some plant and microbial polysaccharidic food additives, adding the mannophilic plant lectin Con A as a reference. Locust-bean and guar galactomannans and acacia gum very strongly inhibited PA-IL. The other lectins, excluding CV-IIL, were very strongly inhibited by yeast mannan. Xanthan and inulin were weak inhibitors. The differential blocking of these lectins by galactosylated branches of plant polysaccharides and by mannan matched their inhibition by avian egg whites, human milk, and royal jelly (protecting animal embryos and neonates from infections). The nondigestability and nontoxicity of the food additives are advantageous for curing gastrointestinal and external infections.
    Journal of Agricultural and Food Chemistry 08/2009; 57(15):6908-13. · 3.11 Impact Factor
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    ABSTRACT: Ralstonia solanacearum lectin (RSL), that might be involved in phytopathogenicity, has been defined as LFuc>Man specific. However, the effects of polyvalency of glycotopes and mammalian structural units on binding have not been established. In this study, recognition factors of RSL were comprehensively examined with natural multivalent glycotopes and monomeric ligands using enzyme linked lectin-sorbent and inhibition assays. Among the glycans tested, RSL reacted strongly with multivalent blood group A(h) (GalNAcalpha1-3[Fucalpha1-2]Gal) and H (Fucalpha1-2Gal) active glycotopes, followed by B(h) (Galalpha1-3[Fucalpha1-2]Gal), Le(a) (Galbeta1-3[Fucalpha1-4]GlcNAc) and Le(b) (Fucalpha1-2Galbeta1-3[Fucalpha1-4]GlcNAc) active glycotopes. But weak or negligible binding was observed for blood group precursors having Galbeta1-3/4GlcNAcbeta1- (Ibeta/IIbeta) residues or Galbeta1-3GalNAcalpha1- (Talpha), GalNAcalpha1-Ser/Thr (Tn) bearing glycoproteins. These results indicate that the density and degree of exposure of multivalent ligands of alpha1-2 linked LFuc to Gal at the non-reducing end is the most critical factor for binding. An inhibition study with monomeric ligands revealed that the combining site of RSL should be of a groove type to fit trisaccharide binding with highest complementarity to blood group H trisaccharide (H(L); Fucalpha1-2Galbeta1-4Glc). The outstandingly broad RSL saccharide-binding profile might be related to the unusually wide spectrum of plants that suffer from R. solanacearum pathogenicity and provide ideas for protective antiadhesion strategies.
    Biochimica et Biophysica Acta 03/2009; 1790(4):249-59. · 4.66 Impact Factor
  • Nechama Gilboa-Garber, Keren Zinger-Yosovich, Batya Lerrer
    Journal of ApiProduct and ApiMedical Science 01/2009; 1(3):82-89.
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    Nava Katri, Nachman Chaim Garber, Gillar Kilfin, Nechama Gilboa-Garber
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    ABSTRACT: Despite Pseudomonas aeruginosa antibiotic resistance, erythromycin (ERM, a macrolide) at subinhibitory concentration (sub-MIC) reduces its pathogenicity. We assessed ERM effects on P. aeruginosa in cultures containing choline (Ch) without and with 1% ethanol (Et) addition. Ch, as an osmoprotectant, increases the following virulence factors (VIFs): lectins (haemagglutination); proteases (casein and elastin lysis); haemolytic phospholipase C (PLC-H; haemolysis); pyocyanin (pigment o.d.) and autoinducers (violacein bioassay). Ethanol also increases lectins, proteases, pyocyanin, autoinducers and rhamnolipid (RHAL; haemolysis) formation, but reduces Ch-induced PLC and protease (elastase) activities. ERM has been shown to totally suppress the Et-induced VIFs, whereas partially reducing the Ch-induced ones. Unexpectedly, ERM combination with 1% Et dramatically annuls the Ch-induced factors. Et contribution might be attributed to its effect on cell membrane, displaying synergism with ERM, whereas antagonizing Ch osmoprotective potential and shifting gene expression. This information is worth further molecular investigation and clinical consideration for skin infection therapy.
    The ISME Journal 09/2008; 2(12):1243-6. · 8.95 Impact Factor
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    ABSTRACT: Pseudomonas aeruginosa antibiotic resistance has led to the search of natural compounds, which would competitively block its fucose>fructose/mannose-binding lectin (PA-IIL) that mediates its biofilm formation and adhesion to animal cells. Such compounds were found in human milk (HM) and avian egg whites. The present research has revealed that honey and royal jelly (RJ), which are assigned to protect beehive progeny and are applied for human infection therapy, match HM in PA-IIL blocking. The function of their fructose (higher in honey) and mannosylated glycoproteins (higher in RJ) as powerful decoys in PA-IIL neutralization is of ecological/biological importance and implementability for the antibacterial adhesion therapeutic strategy.
    The ISME Journal 07/2007; 1(2):149-55. · 8.95 Impact Factor
  • Nava Katri, Nechama Gilboa-Garber
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    ABSTRACT: Pseudomonas aeruginosa is a serious pathogen involved in nosocomial infections. Its pathogenicity is owed to rich production of virulence factors (VIFs) regulated by several complex hierarchical signal systems depending on environmental conditions, medium composition, and the presence of certain active compounds in it. Choline (Ch), which exists in patient tissues, and ethanol (Et), whose consumption aggravates infections, were reported to augment this microbe virulence. The goal of the present study was to show the effect of Et addition to P. aeruginosa cultures in two media (minimal culture medium [MM] and Eagon-Grelet medium [EGM]) in the absence or presence of Ch on its VIF levels. In MM, Et sharply repressed the basal and Ch-induced levels of the P. aeruginosa lectins PA-IL (galactose-specific) and PA-IIL (fucose/mannose-binding) and proteolytic activities, while increasing C(6)-HSL (autoinducer), hemolytic phospholipase C (PLC-H), and phosphatase levels. In EGM, it profoundly increased lectin, protease, pyocyanin, rhamnolipid (RhaL), autoinducer, and slightly phosphatase levels, but reduced Ch-induced protease, PLC-H, and acid phosphatase activities, except the short-chain HSL levels, which were increased by Et in combination with Ch. The presented results enlighten part of the complex molecular basis of Et-induced aggravation of P. aeruginosa infections due to increasing the bacterium virulence, which runs in parallel to suppression of the patient's immunity.
    Current Microbiology 05/2007; 54(4):296-301. · 1.52 Impact Factor
  • A.M. Wu, J.H. Wu, T. Singh, J.-H. Liu, M.-S. Tsai, N. Gilboa-Garber
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    ABSTRACT: Pseudomonas aeruginosa Fuc > Man specific lectin, PA-IIL, is an important microbial agglutinin that might be involved in P. aeruginosa infections in humans. In order to delineate the structures of these lectin receptors, its detailed carbohydrate recognition profile was studied both by microtiter plate biotin/avidin-mediated enzyme–lectin–glycan binding assay (ELLSA) and by inhibition of the lectin–glycan interaction. Among 40 glycans tested for binding, PA-IIL reacted well with all human blood group ABH and Lea/Leb active glycoproteins (gps), but weakly or not at all with their precursor gps and N-linked gps. Among the sugar ligands tested by the inhibition assay, the Lea pentasaccharide lacto-N-fucopentaose II (LNFP II, Galβ1-3[Fucα1-4]GlcNAcβ1-3Galβ1-4Glc) was the most potent one, being 10 and 38 times more active than the Lex pentasaccharide (LNFP III, Galβ1-4 [Fucα1-3]GlcNAcβ1-3Galβ1-4Glc) and sialyl Lex (Neu5Acα2-3Galβ1-4[Fucα1-3] GlcNAc), respectively. It was 120 times more active than Man, while Gal and GalNAc were inactive. The decreasing order of PA-IIL affinity for the oligosaccharides tested was: Lea pentaose ≥ sialyl Lea tetraose > methyl αFuc > Fuc and Fucα1-2Gal (H disaccharide) > 2′-fucosyllactose (H trisaccharide), Lex pentaose, Leb hexaose (LNDFH I) and gluco-analogue of Ley tetraose (LDFT) > H type I determinant (LNFP I) > Lex trisaccharide (Galβ1-4[Fucα1-3]GlcNAc) > sialyl Lex trisaccharide >> Man >>> Gal, GalNAc, and Glc (inactive). The results presented here, in accordance with the crystal 3D structural data, imply that the combining site of PA-IIL is a small cavity-type best fitting Fucα1- with a specific shallow groove subsite for the remainder part of the Lea saccharides, and that polyvalent glycotopes enhance the reactivity. The Fuc > Man Ralstonia solanacearum lectin RSL, which resembles PA-IIL in sugar specificity, differs from it in it's better fit to the B and A followed by H oligosaccharides vs. Fuc, whereas, the second R. solanacearum lectin RS-IIL (the structural homologue of PA-IIL) binds Man > Fuc. These results provide a valuable information on PA-IIL interactions with mammalian glycoforms and the possible spectrum of attachment sites for the homing of this aggressive bacterium onto the target molecules. Such information might be useful for the antiadhesive therapy of P. aeruginosa infections.
    Biochimie 10/2006; 88(10):1479–1492. · 3.14 Impact Factor
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    ABSTRACT: The purple pigmented bacterium Chromobacterium violaceum is a dominant component of tropical soil microbiota that can cause rare but fatal septicaemia in humans. Its sequenced genome provides insight into the abundant potential of this organism for biotechnological and pharmaceutical applications and allowed an ORF encoding a protein that is 60% identical to the fucose binding lectin (PA-IIL) from Pseudomonas aeruginosa and the mannose binding lectin (RS-IIL) from Ralstonia solanacearum to be identified. The lectin, CV-IIL, has recently been purified from C. violaceum [Zinger-Yosovich, K., Sudakevitz, D., Imberty, A., Garber, N. C., and Gilboa-Garber, N. (2006) Microbiology 152, 457-463] and has been confirmed to be a tetramer with subunit size of 11.86 kDa and a binding preference for fucose. We describe here the cloning of CV-IIL and its expression as a recombinant protein. A complete structure-function characterization has been made in an effort to analyze the specificity and affinity of CV-IIL for fucose and mannose. Crystal structures of CV-IIL complexes with monosaccharides have yielded the molecular basis of the specificity. Each monomer contains two close calcium cations that mediate the binding of the monosaccharides, which occurs in different orientations for fucose and mannose. The thermodynamics of binding has been analyzed by titration microcalorimetry, giving dissociation constants of 1.7 and 19 microM for alpha-methyl fucoside and alpha-methyl mannoside, respectively. Further analysis demonstrated a strongly favorable entropy term that is unusual in carbohydrate binding. A comparison with both PA-IIL and RS-IIL, which have binding preferences for fucose and mannose, respectively, yielded insights into the monosaccharide specificity of this important class of soluble bacterial lectins.
    Biochemistry 07/2006; 45(24):7501-10. · 3.38 Impact Factor
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    ABSTRACT: The galactophilic lectins Aplysia gonad lectin (AGL) and Pseudomonas aeruginosa lectin (PA-IL), which detect human I and P1 RBC antigens, were examined for hemagglutination of H+ (group O and B) and H-deficient (Bombay and para-Bombay phenotype) RBCs. The results were compared with those obtained using two other galactophilic lectins, Maclura pomifera lectin (MPL) and Arachis hypogaea (peanut) agglutinin (PNA), which share T-antigen affinity, and two fucose-binding H-specific lectins, Ulex europaeus (UEA-I) and Pseudomonas aeruginosa lectin (PA-IIL), as well as with those achieved with anti-I serum. The results revealed that, in contrast to UEA-I and PA-IIL, which preferentially agglutinated H+ RBCs, and to MPL and PNA, which similarly agglutinated all examined RBCs, AGL, PA-IL, and the anti-I serum agglutinated the H-deficient RBCs more strongly than did the H+ RBCs. These findings could be attributed to increased levels of I and P1 antigens on those RBCs resulting from the use of the free common H-type 2 precursor for their synthesis. Since both PA-IL and PA-IIL are regarded as potential pathogen adhesins, it would be interesting to statistically compare the sensitivities of individuals of H+ and H-deficient RBC populations to P. aeruginosa infections.
    Immunohematology / American Red Cross 02/2006; 22(1):15-22.
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    ABSTRACT: Chromobacterium violaceum is a versatile, violet pigment (violacein)-producing beta-proteobacterium, confined to tropical and subtropical regions, dwelling in soil and water, like Pseudomonas aeruginosa and Ralstonia solanacearum. These three bacteria are saprophytes that occasionally become aggressive opportunistic pathogens virulently attacking animals (the first two) and plants (the third). The recent availability of their genome sequences enabled identification in the C. violaceum genome of an ORF (locus no. 1744) that is similar to those of P. aeruginosa and R. solanacearum lectins, PA-IIL and RS-IIL, respectively. A recombinant protein, CV-IIL, encoded by that ORF exhibited fucose>mannose-specific lectin activity resembling PA-IIL. This paper describes production and properties of the native CV-IIL, which, like PA-IIL and RS-IIL, is probably also a quorum-sensing-driven secondary metabolite, appearing concomitantly with violacein. Its formation is repressed in the CV026 mutant of C. violaceum, which lacks endogenous N-acylhomoserine lactone. The upstream extragenic sequence of its ORF contains a 20 bp sequence (5'-101-120) with partial similarities to the luxI-box and the related P. aeruginosa and R. solanacearum promoter boxes of quorum-sensing-controlled genes. The lectin level is augmented by addition of trehalose to the medium. The subunit size of CV-IIL (around 11.86 kDa) is similar to those of PA-IIL (11.73 kDa) and RS-IIL (11.60 kDa). Like PA-IIL, in the tetrameric form CV-IIL preferentially agglutinates alpha1-2 fucosylated H-positive human erythrocytes (regardless of their A, B or O type), as opposed to the O(h) Bombay type, but differs from it in having no interaction with rabbit erythrocytes and in displaying stronger affinity to l-galactose than to l-fucose. The greater similarity of CV-IIL to PA-IIL than to RS-IIL might be related to the selective adaptation of both C. violaceum and P. aeruginosa to animal tissues versus the preferential homing of R. solanacearum to plants.
    Microbiology 02/2006; 152(Pt 2):457-63. · 2.85 Impact Factor
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    ABSTRACT: Human milk, serum, saliva, and seminal fluid glycoproteins (gps) nourish and protect newborn and adult tissues. Their saccharides, which resemble cell membrane components, may block pathogen adhesion and infection. In the present study, they were examined by a battery of lectins from plants, animals, and bacteria, using hemagglutination inhibition and Western blot analyses. The lectins included galactophilic ones from Aplysia gonad, Erythrina corallodendron, Maclura pomifera (MPL), peanut, and Pseudomonas aeruginosa (PA-IL); fucose-binding lectins from Pseudomonas aeruginosa (PA-IIL), Ralstonia solanacearum (RSL), and Ulex europaeus (UEA-I), and mannose/glucose-binding Con A. The results demonstrated the chosen lectin efficiency for differential analysis of human secreted gps as compared to CBB staining. They unveiled the diversity of these body fluid gp glycans (those of the milk and seminal fluid being highest): the milk gps interacted most strongly with PA-IIL, followed by RSL; the saliva gps with RSL, followed by PA-IIL and MPL; the serum gps with Con A and MPL, followed by PA-IIL and RSL, and the seminal plasma gps with RSL and MPL, followed by UEA-I and PA-IIL. The potential usage of these lectins as probes for scientific, industrial, and medical purposes, and for quality control of the desired gps is clearly indicated.
    Electrophoresis 01/2006; 26(23):4396-401. · 3.26 Impact Factor

Publication Stats

1k Citations
204.38 Total Impact Points

Institutions

  • 2000–2012
    • Chang Gung University
      • • College of Medicine
      • • School of Medicine
      Taoyuan, Taiwan, Taiwan
  • 1971–2012
    • Bar Ilan University
      • Faculty of Life Sciences
      Ramat Gan, Tel Aviv, Israel
  • 2005
    • Masaryk University
      • Ústav biochemie
      Brno, South Moravian Region, Czech Republic
  • 2004–2005
    • University Joseph Fourier - Grenoble 1
      • Centre de Recherche sur les MAcromolécules Végétales
      Grenoble, Rhone-Alpes, France
    • French National Centre for Scientific Research
      • Centre de Recherches sur les Macromolécules Végétales
      Lutetia Parisorum, Île-de-France, France