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Query: UNIPROT:P43026 (lipopolysaccharide)
 62,215 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

It is well established that plasmids are involved in the expression of lipopolysaccharide in certain species of Shigella. In Shigella sonnei, both the biosynthesis of oligosaccharide side chains (O antigen), and cell invasiveness are controlled exclusively by a 120 megadalton (MDa) plasmid. In Shigella dysenteriae 1, a 10 kilobase (kb) plasmid is required for O-antigen production. Shigella dysenteriae 1 strains devoid of this plasmid lose the ability to synthesize O antigen. Interestingly, this 10-kb plasmid is not stably maintained in Escherichia coli K-12 strains, where it is lost spontaneously at a high frequency. Our genetic analyses of Shigella dysenteriae 1 strain IDBM11 and its derivatives indicate that the stability of this plasmid is associated with the histidine region of the chromosome which is unique to Shigella dysenteriae. Furthermore, the 10-kb plasmid is stably maintained in wild-type IDBM11 with an intact histidine locus. However, this plasmid is not stable in IDBM11 derivatives (e.g., IDBM11-1 and IDBM11-2), in which the his locus has been substituted with the histidine region of an E. coli K-12 chromosome. The S. dysenteriae IDBM11 strain, and its derivatives (lacking a 10-kb plasmid), displayed an invasive property as demonstrated by their internalization by HeLa cells in an in vitro assay. Thus the 10-kb plasmid of Shigella dysenteriae 1 is required for O-antigen synthesis but not for cell invasion.
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PMID:The stability of O-antigen plasmid is determined by a chromosomal region of Shigella dysenteriae 1. 245 51

Fifteen monoclonal antibodies (MAbs) directed against Salmonella typhi were produced and characterized. The specificities of the antibodies were determined by their binding patterns in an enzyme immunoassay, with a panel of lipopolysaccharides isolated from different bacteria. Seven MAbs reacted with S. typhi, Salmonella enteritidis, and Salmonella dublin (all belonging to serogroup D). One MAb also reacted with Salmonella paratyphi A and S. paratyphi B. Five MAbs reacted with S. typhi, S. enteritidis, S. dublin, and S. paratyphi B. Two MAbs did not bind to any lipopolysaccharide but showed reactivity with bacterial sonic extracts isolated from S. typhi, S. paratyphi A, S. paratyphi B, Escherichia coli, and Shigella sonnei. These antibodies would be helpful in studying the complexity of antigenic determinants expressed by S. typhi and the nature of the antibody response during typhoid and paratyphoid fevers and also in the diagnosis of the disease.
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PMID:Monoclonal antibodies delineate multiple epitopes on the O antigens of Salmonella typhi lipopolysaccharide. 246 68

The dose-dependent action of Shigella sonnei lipopolysaccharide (LPS) on the development of acute erythroleukocytosis, as well as Rauscher chronic myeloid and lymphoid leukosis, in BALB/c mice sensitive to Rauscher virus was shown. Bordetella pertussis LPS in the doses used in this investigation stimulated the development of both acute erythroleukosis and chronic myeloid and lymphoid leukosis in BALB/c mice infected with Rauscher virus. Lipid A isolated from B. pertussis LPS was found to produce a stimulating effect on the development of Rauscher leukosis in mice. After the treatment of B. pertussis LPS with polymyxin B blocking lipid A no stimulating effect of B. pertussis LPS on the development of Rauscher leukosis was observed. A suggestion is made that lipid A is the active principle contributing to the stimulation of the development of Rauscher leukosis in BALB/c mice.
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PMID:[The effect of gram-negative bacteria lipopolysaccharides on the development of Rauscher leukosis in BALB/c mice]. 254 69

Enterobacterial common antigen (ECA) is a family-specific surface antigen shared by all members of the Enterobacteriaceae and is restricted to this family. It is found in freshly isolated wild-type strains as well as in laboratory strains like Escherichia coli K-12. The family specificity of ECA can be used for taxonomic and diagnostic purposes. ECA is located in the outer leaflet of the outer membrane. It is a glycophospholipid built up by an aminosugar heteropolymer linked to an L-glycerophosphatidyl residue. In a few rough mutants, in addition, the sugar chain can be bound to the complete lipopolysaccharide (LPS) core. Recently, for Shigella sonnei a lipid-free cyclic form of ECA was reported. The genetical determination of ECA is closely related to that of lipopolysaccharide. For biosynthesis of ECA and LPS partly the same sugar precursors and the same carrier lipid is used.
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PMID:ECA, the enterobacterial common antigen. 307 44

Shigella sonnei phase II core oligosaccharide (OSPhII) was linked covalently with protein (bovine serum albumin or tetanus toxoid) to obtain a conjugate (OSPhII-protein) of good immunogenicity in rabbits. Anti-OSPhII-protein conjugate sera contained high levels of immunoglobulin G antibodies against the complete core region of Sh. sonnei lipopolysaccharide. The antigenic relationships between lipopolysaccharides of R1, R3 and R4 core types using anti-OSPhII-protein sera were studied. These antisera may be used for the rapid determination of core types in unknown enterobacterial strains.
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PMID:Characterization and diagnostic application of a lipopolysaccharide core oligosaccharide-protein conjugate. 309 54

To study presumptive diarrhoeagenic and invasive properties of Plesiomonas shigelloides, adult conditioned rabbits (n = 75) were fed 10(10) CFU of 3 isolates (2 from diarrhoea patients and one from river water) of the organism, and one isolate of Shigella sonnei (from a dysentery patient as positive control) or brain-heart infusion broth (as negative control). Each rabbit received in succession i.v. cimetidine (50 mg/kg body weight), two 15 ml oral doses of 5% NaHCO3 at 15 and 30 minutes respectively, prompt bacterial or sham inoculum followed 30 minutes by 2 ml of i.p. tincture of opium. Rabbits fed with P. shigelloides did not die or develop diarrhoea, but in a majority of them, histopathological examinations of the intestine revealed mild acute inflammation of the mucosa, mainly in the ileum. There was no serum antibody response by indirect haemagglutination against the lipopolysaccharide of the homologous strains of P. shigelloides. The culture filtrates of the organism also did not show any cytotoxic morphological changes on CHO and Y1 adrenal cell cultures. By contrast, rabbits fed with S. sonnei developed clinical diarrhoea, small to widespread severe acute inflammation of the gut mucosa, and all died on day 7. It may be concluded that P. shigelloides are able to provoke a mild inflammatory lesions of the gut mucosa in this rabbit model; but there is little prospect of using this model to assess easily the virulence of the organism.
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PMID:Enteropathogenicity of plesiomonas shigelloides by oral inoculation in adult conditioned rabbits. 327 Apr 56

We studied the adaptation of a filtration instrument to an assay for cell migration experiments. The commercially available Nuclepore filter holders were modified so that isolated human polymorphonuclear leucocytes (PMNs) were allowed to penetrate a porous filter membrane and to enter a compartment under the membrane. The total number of PMNs which had passed the pores during an hour of incubation could be counted. In this way we carried out experiments using Shigella sonnei lipopolysaccharide and dilutions of E. coli culture supernatant as chemoattractants for healthy human PMNs. These studies showed that the method can distinguish between random and directed movements of PMNs and it is sensitive to the concentrations of chemoattractant. Furthermore, the data obtained using PMNs from the same subject on different days seem to be comparable.
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PMID:A new simplified assay for evaluation of motile activity of human polymorphonuclear leucocytes. 328 87

We described previously (W.M. Shafer, L.E. Martin, and J.K. Spitznagel, Infect. Immun. 45:29-35, 1984) the presence of a 37-kilodalton cationic antimicrobial protein (37K CAP) in extracts of granules prepared from human polymorphonuclear granulocytes (PMN). In this investigation, we prepared 37K CAP from PMN granule extracts by sequential ion-exchange and molecular-sieve chromatography and examined its antimicrobial activity against a number of gram-negative and gram-positive bacteria. At concentrations of 5 micrograms/ml or lower, 37K CAP exerted selective antimicrobial activity against gram-negative bacteria. These bacteria included Acinetobacter lwoffii, Escherichia coli, Neisseria gonorrhoeae, Pseudomonas aeruginosa, Pseudomonas cepacia, Salmonella typhi, Salmonella typhimurium, and Shigella sonnei. However, at 5 micrograms of 37K CAP per ml, Proteus mirabilis, Proteus vulgaris, and Serratia marcescens resisted this antimicrobial activity. The bactericidal activity of 37K CAP was greatest in acidic (pH 5.5) as opposed to alkaline (pH 7.5) media. The level of S. typhimurium resistance to 37K CAP correlated with the presence of O antigen in the lipopolysaccharide. In the absence of O antigen repeat units, resistance was proportional to the length of the core oligosaccharide. These results suggest that 37K CAP may contribute significantly to the ability of PMN to kill gram-negative bacteria by nonoxidative means, particularly as the maturing phagolysosome becomes acidified.
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PMID:Late intraphagosomal hydrogen ion concentration favors the in vitro antimicrobial capacity of a 37-kilodalton cationic granule protein of human neutrophil granulocytes. 352 87

Phage P1C(-), in a state of the phage not infective to Escherichia coli K12, was able to form plaques on a wild-type strain of E. coli C and on Shigella sonnei in the presence of Mg2+. Citrobacter freundii, Enterobacter aerogenes, and a Salmonella typhimurium galE mutant were not lysed by, but were lysogenized with P1cinC(-), whereas Klebsiella pneumoniae, Proteus rettgeri, and S. typhimurium LT2 were not susceptible to either P1cinC(-) or P1cinC(+). The lipopolysaccharide structure of E. coli C and Sh. sonnei is discussed with reference to receptors for P1cinC(-) and P1cinC(+).
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PMID:Magnesium-dependent plaque formation by bacteriophage P1cinC(-) on Escherichia coli C and Shigella sonnei. 353 35

1. The transfer of type K. colicinogeny to Shigella sonnei Phase II has been described. 2. The colicine elaborated by this microorganism is a lipopolysaccharide-protein complex which resembles the somatic antigen of the noncolicinogenic parent. 3. Although the colicine K of Escherichia coli K235 and of Sh. sonnei differ both chemically and serologically, they resemble each other in that both elicit type K colicine-neutralizing antibodies and both have the same bactericidal specificity. 4. The nature of the chemical changes brought about in the somatic antigen of Sh. sonnei through the acquisition of colicinogeny remains unknown
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PMID:Colicine K. VII. The transfer to type K colicinogeny to Shigella sonnei. 532 16


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