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Query: UMLS:C0519030 (Klebsiella)
 21,988 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Extracts of twenty seeds were tested against twenty six organisms belonging to Klebsiella, Proteus, Salmonella, Shigella and Cholera species. Extracts of eleven seeds showed agglutinating activity against twenty four various organism. S. typhi and Kl. aerogenes did not react against any lectin. On the basis of the results it was possible to differentiate various Shigella and Salmonella organisms by various seed extracts. Different isolates of cholera organisms of same serotype and phage type showed different reaction suggesting that probably these organisms possess different antigenic characters. Thus phytagglutinins may be of some help in the identification and subtyping of these organisms.
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PMID:Studies on the effect of phytagglutinins on some members of Enterobacteriaceae. 79 2

The binding of a membrane proteoglycan from a non-encapsulated strain of Klebsiella pneumoniae (Kp-MPG) and four derivatives thereof, to human leukocytes, was investigated by indirect immunofluorescence using biotinylated F(ab')2 fragments of anti-Kp-MPG antibodies and the streptavidin-phycoerythrin amplification system in flow cytometry. Four Kp-MPG derivatives were studied: 1/ an acylpoly(1,3)galactoside (APG), 2/ an APG preparation submitted to acid hydrolysis which removed all fatty acids, but left intact the galactose chain of APG (GC-APG), 3/ a preparation obtained by mild alkaline hydrolysis, containing additional ester-linked C14 and C16 fatty acids bound to the APG molecule (EFA-APG) and 4/ a polymer of the latter compound (APG pol). Kp-MPG, APG and EFA-APG were shown to bind exclusively to monocytes at the lowest concentrations (from 0.15 to 3 microM APG). At higher concentrations, these compounds interacted with polymorphonuclear leukocytes, and with lymphocyte subsets in the following decreasing order: B cells, NK cells, CD8+ and CD4+ lymphocytes. Neither APG pol or GC-APG nor K. pneumoniae smooth LPS showed significant binding to leukocytes. However Kp-LPS treated by drastic alkaline hydrolysis displayed binding properties similar to those of APG. Removal of the ester-linked C14 and C16 fatty acids from EFA-APG did not affect the binding of the molecule. The capacity of cells from the myelomonocytic lineage to bind Kp-MPG and APG was very low in phenotypically immature cell lines (HL60 and U937) as compared with monocytes or polymorphonuclear cells. Treatment of U937 cells with interferon-gamma up-regulated their APG binding capacity along with the expression of the integrin CD 11 b and the CD 14 molecule, whereas monocytes exposed to interferon-gamma showed an increased binding of APG associated with an elevated expression of the galactose specific lectin Mac-2. The data demonstrate a preferential binding of Kp-MPG and APG to cells of the monocyte/macrophage lineage. APG binding does not involve the poly (1,3) galactose chain and the ester-linked C14 and C16 fatty acids but requires the presence of the hydrophobic part of the molecule.
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PMID:Binding of a membrane proteoglycan from Klebsiella pneumoniae and its derivatives to human leukocytes. 149 Jul 26

Tissue-binding specificity of the type-3 fimbriae of pathogenic enteric bacteria was determined using frozen sections of human kidney. A wild-type Klebsiella sp. strain and the recombinant strain Escherichia coli HB101(pFK12), both expressing type-3 fimbriae, as well as the purified type-3 fimbriae effectively bound to sites at or adjacent to tubular basement membranes, Bowman's capsule, arterial walls, and the interstitial connective tissue. Bacterial adherence to kidney was decreased after collagenase treatment of the tissue sections. Recombinant strains expressing type-3 fimbriae specifically adhered to type V collagen immobilized on glass slides, whereas other collagens, fibronectin or laminin did not support bacterial adherence. In accordance with these findings, specific binding of purified type-3 fimbriae to immobilized type V collagen was demonstrated. Specific adhesion to type V collagen was also seen with the recombinant strain HB101(pFK52/pDC17), which expresses the mrkD gene of the type-3 fimbrial gene cluster in association with the pap-encoded fimbrial filament of E. coli, showing that the observed binding was mediated by the minor lectin (MrkD) protein of the type-3 fimbrial filament. The interaction is highly dependent on the conformation of type V collagen molecules since type V collagen in solution did not react with the fimbriae. Specific binding to type V collagen was also exhibited by type-3 fimbriate strains of Yersinia and Salmonella, showing that the ability to use type V collagen as tissue target is widespread among enteric bacteria.
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PMID:Type V collagen as the target for type-3 fimbriae, enterobacterial adherence organelles. 198 Jul 13

Macrophages express a mannose/N-acetylglucosamine-specific lectin which serves as a receptor for nonopsonic phagocytosis of mannose-coated particles. We have examined the binding to guinea pig alveolar macrophages in a serum-free medium of 16 Klebsiella pneumoniae serotypes and of the capsular polysaccharides isolated from 7 of these serotypes. Only five polysaccharides containing the repeating sequence Man alpha 2/3Man or L-Rha alpha 2/3-L-Rha bound to the macrophages. Of the 11 bacterial serotypes expressing such disaccharides in their capsular polysaccharides, 7 bound efficiently, 2 bound poorly, and 2 did not bind at all. No binding occurred with five serotypes lacking these disaccharides. Binding of the bacteria was inhibited by homologous and heterologous capsular polysaccharides that contain the disaccharide sequences, by mannan, and by (Man)25BSA (where BSA is bovine serum albumin). Man alpha 2/3Man-containing oligosaccharides were potent inhibitors compared with monosaccharides. Binding was dependent on Ca2+, modulated by cultivating the macrophages on mannan-coated surfaces, and increased in human monocyte-derived macrophages compared with monocytes. The bulk of the bacteria bound to the macrophages was internalized and killed. The data taken together suggest that Klebsiella pneumoniae cells undergo lectinophagocytosis mediated by capsular disaccharides recognized by the mannose/N-acetylglucosamine-specific lectin of macrophages. This may enhance clearance of the organisms from the serum-poor environment of the lung.
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PMID:Lectinophagocytosis of encapsulated Klebsiella pneumoniae mediated by surface lectins of guinea pig alveolar macrophages and human monocyte-derived macrophages. 201 37

A wide spectrum of formalin-killed bacteria have been tested for their ability to release histamine from human dispersed lung and tonsillar mast cells. Escherichia coli, Enterobacter cloacae, Staphylococcus epidermidis, Proteus vulgaris, Klebsiella oxytoca and K. pneumoniae were the most effective histamine releasers. Further studies on tonsillar mast cells showed that E. coli-induced histamine release differed from IgE-dependent release with respect to its kinetics, temperature and pH profiles and its sensitivity to calcium deprivation and metabolic inhibitors. A lectin-mediated mechanism may operate, but other non-immunological mechanisms might also be involved in the release. Escherichia coli and anti-IgE did not synergize in inducing histamine release. The production of PGD2 and the failure to detect lactate dehydrogenase following incubation of mast cells with E. coli suggests that histamine release is not due to cytotoxicity.
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PMID:Non-IgE-dependent bacteria-induced histamine release from human lung and tonsillar mast cells. 244

Serum amyloid P component (SAP), a normal plasma glycoprotein, has recently been shown to have Ca2+-dependent binding specificity for methyl 4,6-O-(1-carboxyethylidene)-beta-D-galactopyranoside (MO beta DG) [Hind, Collins, Renn, Cook, Caspi, Baltz & Pepys (1984) J. Exp. Med. 159, 1058-1069]. SAP was found to bind in vitro to Klebsiella rhinoscleromatis, the cell wall of which is known to contain this particular cyclic pyruvate acetal of galactose. SAP also bound in similar amounts (approx. 6000 molecules per organism) to group A Streptococcus pyogenes, but very much less was taken up on Xanthomonas campestris, which contains the 4,6-cyclic pyruvate acetal of mannose. No SAP bound to Escherichia coli, which contains the 4,6-cyclic pyruvate acetal of glucose, or to Streptococcus pneumoniae type 4, which contains the 2,3-cyclic pyruvate acetal of alpha- rather than beta-galactopyranoside, or to other organisms (Streptococcus agalactiae, Staphylococcus aureus and Staphylococcus epidermidis), the carbohydrate structures of which are less well characterized. Binding of SAP to those organisms which it did recognize was completely inhibited or reversed by millimolar concentrations of free MO beta DG. SAP, a human plasma protein, thus behaves as a lectin and may be a useful probe for its particular specific ligand in the cell walls of bacteria and other organisms.
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PMID:Human serum amyloid P component, a circulating lectin with specificity for the cyclic 4,6-pyruvate acetal of galactose. Interactions with various bacteria. 388 85

RU 41.740, a glycoprotein extract from Klebsiella pneumoniae, is a polyclonal B cell activator in the thymus-independent category, and both RU 41.740 and its fraction F1 induce the production of interleukin 1 (IL 1). RU 41.740 alone appears to have no direct effect on T-enriched cells. However, we show here that when given in conjunction with concanavalin A (Con A), RU 41.740 enabled nylon wool-passed T cells, which had been accessory cell depleted and lost responsiveness to Con A, to proliferate in response to Con A. Analysis of this observation indicated that RU 41.740 probably acted via a residual accessory cell population and that contact of this cell with the T cell was necessary for Con A activation of the T cell. Because both lectin/antigen and a source of IL 1 are required to stimulate accessory cell-depleted T cells, the mechanism of action of RU 41.740 in this system may be by induction of IL 1 from residual accessory cells in the nylon wool-passed, T-enriched cell population. However, two other agents that stimulate IL 1 production, lipopolysaccharide (LPS) and F1, do not enable T-enriched cells to respond to Con A in this system.
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PMID:Influence of RU 41.740, a glycoprotein extract from Klebsiella pneumoniae, on the murine system. II. RU 41.740 facilitates the response to Con A in otherwise unresponsive T-enriched cells. 388 53

A large number of linear and branched oligosaccharides and several glycosides of D-mannose were tested for their inhibitory activity on the agglutination of yeast cells or guinea pig erythrocytes by three D-mannose-specific enteric bacteria possessing type 1 fimbriae. With Escherichia coli 346, the best inhibitors found are the alpha glycosides of the branched oligosaccharides alpha-D-Manp-(1 leads to 3)-[alpha-D-Manp-(1 leads to 6)]-alpha-D-Manp-(1 leads to 6)-alpha-D-Manp-(1 leads to 3)-D-Manp and alpha-D-Manp-(1 leads to 3)-[alpha-D-Manp-(1 leads to 6)]-alpha-D-Manp- (1 leads to 6)-[alpha-D-Manp-(1 leads to 2)-alpha-D-Manp-(1 leads to 3) ]-D-Manp and the trisaccharide alpha-D-Manp-(1 leads to 3)-beta-D-Manp-(1 leads to 4)-D-GlcNAc, all of which are 21-30 times more inhibitory than methyl alpha-D-mannopyranoside. The aromatic glycoside p-nitrophenyl alpha-D-mannopyranoside was also a strong inhibitor (30 times more inhibitory than methyl alpha-D-mannopyranoside), whereas the corresponding beta-D-glycoside was only a weak inhibitor (approximately as methyl alpha-D-mannopyranoside). A nearly identical pattern of inhibitory activity was observed with the fimbriae. This suggests that the combining site of the E. coli fimbrial lectin is in the form of an extended pocket on the surface of the lectin corresponding to the size of a trisaccharide and fitting best the structure alpha-D-Manp-(1 leads to 3)-beta-D-Manp-(1 leads to 4)-D-GlcNAc. Since p-nitrophenyl alpha-D-mannopyranoside is a strong inhibitor, the existence of a hydrophobic region in the combining site or close to it was assumed. The combining site of the Klebsiella pneumoniae fimbrial lectin is probably similar to that of E. coli, but that of the Salmonella typhimurium fimbrial lectin differs considerably. It appears that the combining sites of the three bacterial lectins tested exhibit preference for structures found in N-glycosylic oligomannoside units of mammalian cell surface glycoproteins.
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PMID:Carbohydrate specificity of the surface lectins of Escherichia coli, Klebsiella pneumoniae, and Salmonella typhimurium. 613 49

Exposure of thioglycollate-elicited murine peritoneal macrophages to wheat germ agglutinin (WGA) increased markedly the uptake of six different bacteria, which have surface receptors for the lectin. Uptake of Staphylococcus aureus H was higher by 3-5-fold, of S. aureus 52A2 by 1.8-fold, of S. aureus 52A5 by 1.7-fold, of S. albus by 2.3-fold, of Shigella flexneri by 6-fold and of Micrococcus luteus by 6.5-fold. Klebsiella pneumoniae, devoid of receptors for WGA, was not phagocytosed following pretreatment of macrophages with the lectin. Pretreatment of the bacteria with the lectin also resulted, in most cases, in an increase in phagocytosis. Interaction of WGA with the macrophages and with the bacteria, as well as the potentiation of phagocytosis, was abolished by tri-N-acetylchitotriose, a saccharide that binds specifically to WGA, but not by monosaccharides which do not interact with this lectin. With non-elicited macrophages, enhancement of phagocytosis by WGA was less pronounced, probably because of the higher number of lectin-binding sites (5-fold) on the elicited cells. Peanut agglutinin and soybean agglutinin, that bind to macrophages but not to the bacteria studied, lack the ability to potentiate phagocytosis. Macrophage surface sugars thus appear to play an important role in phagocytosis by serving as receptors for lectins that form bridges between the macrophages and the microorganisms.
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PMID:Wheat germ agglutinin potentiates uptake of bacteria by murine peritoneal macrophages. 654 90

A total of 393 clinical bacterial isolates were tested for their ability to agglutinate yeast cells of either Saccharomyces cerevisiae or Candida albicans. A positive agglutination of yeasts that could be prevented by methyl alpha-D-mannoside was taken as an indication for the possible presence of a mannose-specific lectin (carbohydrate-binding protein) on the surface of the tested bacteria. Agglutination tests on glass slides showed that 38% of all the isolates tested were positive in their capacity to agglutinate yeasts. Among the various strains tested, all isolates of Serratia marcescens, Proteus morganii, and Citrobacter diversus, as well as 94% of Klebsiella pneumoniae, were positive. On the other hand, only 46% of the Escherichia coli, 48% of the salmonellae, 44% of the Citrobacter freundii, and 71% of the Aeromonas hydrophila isolates were positive. A quantitative determination of the lectin activity done by observing the agglutination of yeasts in microtiter plates showed that S. marcescens isolates were the most avid binders to the yeast, whereas Klebsiella and Citrobacter isolates were the weakest.
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PMID:Screening of bacterial isolates for mannose-specific lectin activity by agglutination of yeasts. 698 54


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