Anti-galactan activity in Tridacna maxima (Roding) haemolymph. Calcium dependence of the haemagglutinins and precipitins.
(49/925)
A powerful natural agglutinin with haemagglutinating and precipitating properties has been found in the haemolymph from the elongate clam Tridacna maxima (Roding). The agglutinin shows anti-galactan properties and reacts with a variety of bacteria-, plant-, invertebrate- and vertebrate-derived galactans, glycopeptides and polysaccharides. Previous studies which showed that the agglutinin-combining sites were inhibited by 2-acetamido-2-deoxy-D-galactose and D-galactose also revealed some anomalies in the reactions of the agglutinin with different saccharide-containing macromolecules. In an attempt to resolve these anomalies, the present study further examines the precipitating and haemagglutinating properties of the agglutinin and illustrates a requirement of the agglutinin for Ca2+. The ability of the T. maxima agglutinin to precipitate with structures containing terminal beta-linked 2-acetamido-2-deoxy-D-galactopyranosyl or D-galactopyranosyl groups suggests that the Tridacna haemolymph and purified lectin will find considerable application in the study of many biologically important carbohydrates. (+info)
Interactions of C-reactive protein with the complement system. III. Complement-dependent passive hemolysis initiated by CRP.
(50/925)
Interactions of CRP with various substrates in the presence of human serum have been shown to result in efficient activation of C components C1-C5. We now report the ability of CRP to initiate C-dependent hemolysis. For this purpose CRP was isolated by affinity chromatography using pneumococcal CPS and gel filtration; its purity was established by several criteria. Erythrocytes were coated with CPS (E-CPS) and passively sensitized with CRP. C-dependent lysis of these cells was observed upon the addition of suitably absorbed human serum, and the efficiency of hemolysis compared favorably with that initiated by rabbit IgG anti-CPS antibody. CRP also sensitized E-CPS for lysis by guinea pig C; partial lysis was seen when C4-deficient guinea pig serum was used, suggesting that CRP also shares with antibody the ability of CRP to fully activate the C system and provide further evidence for a role for CRP similar to that of antibody in the initiation and modulation of inflammatory reactions via the complete system. (+info)
Primary structure and characteristics of a lectin from skin mucus of the Japanese eel Anguilla japonica.
(51/925)
Two types of lactose-binding lectins, AJL-1 and AJL-2, were purified from the skin mucus extract of the Japanese eel Anguilla japonica by lactose affinity chromatography and subsequent gel filtration. The molecular masses of AJL-1 and AJL-2 were 16,091 and 31,743 Da, respectively. Intact AJL-1 was comprised of two identical 16-kDa subunits having blocked N termini and no disulfide bonds. AJL-2 was a homodimer with disulfide bonds. Based on the N-terminal amino acid sequence of the AJL-2 monomer, the nucleotide sequence of cDNA encoding this lectin was determined by 3'- and 5'-rapid amplification of cDNA ends. The deduced amino acid sequence showed approximately 30% homology with C-type lectins, which bind to carbohydrates in a Ca(2+)-dependent manner. In addition, AJL-2 exhibited highly conserved consensus amino acid residues of the C-type carbohydrate recognition domain, although this lectin showed Ca(2+)-independent activity. Gene expression of AJL-2 was detected only in the skin by Northern blot analysis, and this lectin localization was demonstrated in the club cells by immunohistochemistry. These results indicate that AJL-2 is secreted on the body surface and function as a component of skin mucus. AJL-2 agglutinated Escherichia coli and suppressed its growth, suggesting that this lectin is involved in host defense. (+info)
An O-glycoside of sialic acid derivative that inhibits both hemagglutinin and sialidase activities of influenza viruses.
(52/925)
The compound Neu5Ac3alphaF-DSPE (4), in which the C-3 position was modified with an axial fluorine atom, inhibited the catalytic hydrolysis of influenza virus sialidase and the binding activity of hemagglutinin. The inhibitory activities to sialidases were independent of virus isolates examined. With the positive results obtained for inhibition of hemagglutination and hemolysis induced by A/Aichi/2/68 virus, the inhibitory effect of Neu5Ac3alphaF-DSPE (4) against MDCK cells was examined, and it was found that 4 inhibits the viral infection with IC50 value of 5.6 microM based on the cytopathic effects. The experimental results indicate that compound 4 not only inhibits the attachment of virus to the cell surface receptor but also disturbs the release of the progeny viruses from infected cells by inhibiting both hemagglutinin and sialidase of the influenza viruses. The study suggested that the compound is a new class of bifunctional drug candidates for the future chemotherapy of influenza. (+info)
Nutritional quality of extruded kidney bean (Phaseolus vulgaris L. var. Pinto) and its effects on growth and skeletal muscle nitrogen fractions in rats.
(53/925)
The influence of extrusion cooking on the protein content, amino acid profile, and concentration of antinutritive compounds (phytic acid, condensed tannins, polyphenols, trypsin, chymotrypsin, alpha-amylase inhibitors, and hemagglutinating activity) in kidney bean seeds (Phaseolus vulgaris L. var. Pinto) was investigated. Growing male rats were fed diets based on casein containing raw or extruded kidney beans with or without methionine supplementation for 8 or 15 d. Rates of growth, food intake, and protein efficiency ratio were measured and the weight of the gastrocnemius muscle and the composition of its nitrogenous fraction was determined. Extrusion cooking reduced (P < 0.01) phytic acid, condensed tannins, and trypsin, chymotrypsin, and (alpha-amylase inhibitory activities. Furthermore, hemagglutinating activity was abolished by extrusion treatment. Protein content was not affected by this thermal treatment. Rats fed raw kidney bean lost BW rapidly and the majority died by 9 d. Pretreatment of the beans by extrusion cooking improved food intake and utilization by the rats and they gained BW. Supplementation of extruded kidney bean with methionine further enhanced (P < 0.01) food conversion efficiency and growth. However, BW gains and muscle composition still differed (P < 0.01) from those of rats fed a high-quality protein. (+info)
Lipoplex-induced hemagglutination: potential involvement in intravenous gene delivery.
(54/925)
We report a study aiming to characterize the interaction of blood and blood components with lipoplexes under conditions relevant to in vivo intravenous transfection. In this study we focus on the interaction of lipoplexes with red blood cells (RBC). It was found that no significant hemolysis occurred during several hours' incubation using lipoplex compositions and lipoplex/red blood cell ratios in the range commonly used for in vivo transfection. However, the interaction of RBC with lipoplexes resulted in massive agglutination, which occurs irrespective of the type of cationic lipid or helper lipid. Agglutination was also induced by polyplexes (such as dendrimer/DNA complexes) and lipoplexes in the presence of spermidine or protamine sulfate (the latter induced hemagglutination by itself). DSPE-PEG(2000) inserted into the lipoplexes inhibits hemagglutination somewhat. In order to understand the effect of serum on the agglutination better, plasma was separated into its high molecular weight components (HMWC, >14 kDa) and its low molecular weight components (LMWC, < or = 14 kDa). These fractions were characterized for their level of proteins, primary amino groups, osmotic pressure, and electrical conductivity, and compared with saline (0.15 M NaCl). It was found that both LMWC and HMWC inhibit agglutination by themselves, although whole serum demonstrates better hemagglutination inhibition than each fraction separately. The inhibitory effect of the serum (or plasma) is explained by its effect on the electrostatics of the lipoplexes, reducing their positive charge, as was demonstrated using fluorescein-phosphatidylethanolamine-labeled lipoplexes. The effect of LMWC was related to ionic strength and was equal to the effect of 0.15 M NaCl. The level of agglutination was reduced with increasing lipoplex DNA(-)/cationic lipid(+) (DNA(-)/L(+)) ratio. However, at the low DNA(-)/L(+) ratio needed to achieve significant in vivo transfection after i.v. administration, massive agglutination occurred. These data suggest that i.v. administration of lipoplexes and polyplexes may lead to RBC agglutination, and the agglutinates formed may explain the localization of lipoplexes and expression of their transgenes in the lungs. (+info)
Production, properties and specificity of a new bacterial L-fucose- and D-arabinose-binding lectin of the plant aggressive pathogen Ralstonia solanacearum, and its comparison to related plant and microbial lectins.
(55/925)
The worldwide distributed plant aggressive pathogen Ralstonia solanacearum, which causes lethal wilt in many agricultural crops, produces a potent L-fucose-binding lectin (RSL) exhibiting sugar specificity similar to that of PA-IIL of the human aggressive opportunistic pathogen Pseudomonas aeruginosa. Both lectins show L-fucose > L-galactose > D-arabinose > D-mannose specificity, but the affinities of RSL to these sugars are substantially lower. Unlike Ulex europaeus anti-H lectin, but like PA-IIL and Aleuria aurantia lectin (AAL), RSL agglutinates H-positive human erythrocytes regardless of their type, O, A, B, or AB, and animal erythrocytes (papain-treated ones more strongly than untreated ones). It also interacts with H and Lewis chains in the saliva of "secretors" and "nonsecretors." RSL purification is easier than that of PA-IIL since R. solanacearum extracts do not contain a galactophilic PA-IL-like activity. Mass spectrometry and 35 N-terminal amino acid sequencing enabled identification of the RSL protein (subunit approximately 9.9 kDa, approximately 90 amino acids) in the complete genome sequence of this bacterium. Despite the greater phylogenetic proximity of R. solanacearum to P. aeruginosa, and the presence of a PA-IIL-like gene in its genome, the RSL structure is not related to that of PA-IIL, but to that of the fucose-binding lectin of the mushroom (fungus) Aleuria aurantia, which like the two bacteria is a soil inhabitant. (+info)
The lectin from leaves of Japanese cycad, Cycas revoluta Thunb. (gymnosperm) is a member of the jacalin-related family.
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A novel lectin was isolated from leaves of the Japanese cycad, Cycas revoluta Thunb. (gymnosperm), and its characteristics including amino acid composition, molecular mass, carbohydrate binding specificity and partial amino acid sequences were examined. The inhibition analysis of hemagglutinating activity with various sugars showed that the lectin has a carbohydrate-binding specificity similar to those of mannose recognizing, jacalin-related lectins. Partial amino acid sequences of the lysylendopeptic peptides shows that the lectin might have a repeating structure and belong to the jacalin-related lectin family. (+info)