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

The structures of the polysaccharide part of lipopolysaccharides isolated from eight Escherichia coli K12/Shigella dysenteriae type 1 hybrids have been determined using sugar and methylation analysis plus 1H- and 13C-nuclear magnetic resonance spectroscopy. The hybrids express parts of the S. dysenteriae type 1 O-antigen tetrasaccharide repeating unit because of the presence of pSS3, a plasmid expressing an alpha-galactosyl: lipopolysaccharide transferase and pSS9, a pBR322 plasmid expressing S. dysenteriae type 1 rfb genes. The various classes of hybrids are the result of transposon Tn 1000 insertions in pSS9 inactivating different rfb genes. The following structural elements were found. E. coli K12 (pSS3) and E. coli K12 (pSS3, pSS9-6; a class I hybrid); alpha-D-Galp(1-->3)beta-D-GlcpNAc(1-->. Class IV hybrids: E. coli K12 (pSS3, pSS9-36); (pSS3, pSS9-107) and (pSS3, pSS9-114); alpha-L-Rhap(1-->2)alpha-D-Galp(1-->3)beta-D-GlcpNAc(1-->. Class V hybrids: E. coli K12 (pSS3, pSS9-78) and (pSS3, pSS9-111); alpha-L-Rhap(1-->3)alpha-L-Rhap(1-->2)alpha-D-Galp(1-->3)bet a-D-GlcpNAc(1-->. The structural sequences are identical to those found in the lipopolysaccharide from native S. dysenteriae type 1. In the hybrid strains, the terminal non-reducing GlcNAc residue of the E. coli K12 core is fully substituted by S. dysenteriae type 1 repeating units, or parts thereof.
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PMID:Expression of the Shigella dysenteriae type-1 lipopolysaccharide repeating unit in Escherichia coli K12/Shigella dysenteriae type-1 hybrids. 768 45

A novel form of bacterial variation found in an FhuA- mutant of Escherichia coli K12 was characterized by the alternation of (1) simultaneous resistance to lipopolysaccharide-specific phage U3 and to FhuA-specific agents (Ufr phenotype); and (2) a return to the sensitivity pattern of the initial strain (Ufs). In Ufr cells, loss of the U3 receptor permitted C21 adsorption without modifying the sensitivity to other tested phages or colicins. Genetic analysis revealed that Ufr variants were altered at two distinct loci. Ufr bacteria, though derived from a strain F- devoid of classical gene transfer mechanisms, were transiently able to promote mating between themselves and, to some extent, with other bacteria, including Rec-. Heterogenic matings resulted in the formation of persistent heterozygotes segregating Ufr- and Ufs-like bacteria. Pedigree analysis and subcloning of heterozygotic isolates indicate that they were diploids, as was the initial Ufr strain. Functional genetic complementation between these two genomes was only transient and the alternative forms were likely to result from the expression of a single chromosome of the heterozygotes. Mutation occurred in either form without causing any change in the alternative form.
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PMID:Ufr/s variation in Escherichia coli K12: a reversible double-mutation or alternate chromosome expression in non-complementing diploids? 799 44

An OmpA-deficient mutant of an OmpF/OmpC-free Escherichia coli B strain was selected using phage K3. The mutant strain was characterized by SDS-gel electrophoresis, immunoblotting, and electron microscopy. All major outer membrane proteins, including OmpA, were absent. This strain was then transformed with the plasmid pMY222 encoding the K12 OmpF porin or with pBlue-script-derived plasmids, encoding the porins OmpC, PhoE, and maltoporin, respectively. Following SDS extraction of outer membrane sacculi from strains expressing individual porins, crystalline porin arrays that allowed in situ structural analysis to be performed were observed. Furthermore, the absence of endogenous major outer membrane proteins facilitated the purification of native porin-lipopolysaccharide complexes, the functionally active channels, from the sacculi of transformed strains.
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PMID:Direct in situ structural analysis of recombinant outer membrane porins expressed in an OmpA-deficient mutant Escherichia coli strain. 800 82

In the study of interactions between facultative intracellular pathogens and macrophages, monocytic cell lines have the advantages of showing defined states of activation and lacking genetic variation among donors, thus yielding reproducible results. Nonpathogenic Escherichia coli K12 were killed at similar rates in the U937 cell line differentiated into macrophage-like cells by phorbol myristate acetate (PMA) or by the combination of retinoic acid (RA) and vitamin D3 (VD). Complete elimination was reached only when cells were activated by lipopolysaccharide for 30 min prior to infection, and it was further enhanced when bacteria were opsonized by specific immunoglobulin G. Both types of differentiation led to intracellular multiplication of virulent Listeria monocytogenes and to elimination of the animal pathogen Listeria ivanovii. For both strains, conditions for intracellular survival were more favorable in PMA-differentiated U937. During infection, RA/VD-differentiated U937 could discriminate between the human pathogen Brucella suis S1, which strongly multiplied, and the animal pathogen Brucella canis, which survived without multiplication. U937 cells differentiated by RA and VD therefore represent a basic model in bacteria-human macrophage interactions.
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PMID:Differentiated U937 cells exhibit increased bactericidal activity upon LPS activation and discriminate between virulent and avirulent Listeria and Brucella species. 807 93

The lpcA locus has been identified in Escherichia coli K12 novobiocin-supersensitive mutants that produce a short lipopolysaccharide (LPS) core which lacks glyceromannoheptose and terminal hexoses. We have characterized lpcA as a single gene mapping around 5.3 min (246 kilobases) on the E. coli K12 chromosome and encoding a 22.6-kDa cytosolic protein. Recombinant plasmids containing only lpcA restored a complete core LPS in the E. coli strain chi711. We show that this strain has an IS5-mediated chromosomal deletion of 35 kilobases that eliminates lpcA. The LpcA protein showed discrete similarities with a family of aldose/ketose isomerases and other proteins of unknown function. The isomerization of sedoheptulose 7-phosphate, into a phosphosugar presumed to be D-glycero-D-mannoheptose 7-phosphate, was detected in enzyme reactions with cell extracts of E. coli lpcA+ and of lpcA mutants containing the recombinant lpcA gene. We concluded that LpcA is the phosphoheptose isomerase used in the first step of glyceromannoheptose synthesis. We also demonstrated that lpcA is conserved among enteric bacteria, all of which contain glyceromannoheptose in the inner core LPS, indicating that LpcA is an essential component in a conserved biosynthetic pathway of inner core LPS.
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PMID:Biosynthesis of inner core lipopolysaccharide in enteric bacteria identification and characterization of a conserved phosphoheptose isomerase. 863 69

A panel of monoclonal antibodies (MAbs) directed against lipopolysaccharide (LPS) of Salmonella serogroups A, B, and D was generated. Nine most productive hybrid clones were selected from several fusions of mouse myeloma cells with splenocytes from BALB/c mice, immunized with the corresponding heat-killed bacteria. The MAbs were characterized by enzyme immunoassay, Western blot analysis, and dot-immunoblotting with LPS and whole bacteria of Salmonella serogroups A-E and some other representatives of the Enterobacteriaceae family. Seven MAbs were reactive with the sole Salmonella strain used as an immunogen; one MAb, SD:10D9H, reacted with the five major serogroups of Salmonella species (A, B, D, E1, and E2); and one MAb, SA:5D12A, reacted with Salmonella serogroups A-E and a rough strain of S. cholerae-suis. None of the MAbs reacted with LPS of E. coli 055:B5 or whole bacteria of E. coli K12, Klebsiella pneumoniae, or Proteus vulgaris. The typical ladder-like patterns of bands were observed after immunoblotting of MAbs against electrophoretically resolved LPS from Salmonella serogroups A-E, which thus confirmed their LPS-directed specificity. MAbs affinity constants were determined by noncompetitive enzyme immunoassay using serial dilutions of both LPS as antigen (coating the plate) and antibodies. On the base of the results obtained, the presumed epitopes for each of the MAbs were discussed. The usefulness of MAbs generated for diagnostic and protective purposes was declared.
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PMID:Monoclonal antibodies directed against unique and common determinants on the lipopolysaccharide molecule of Salmonella serogroups A, B, and D. 877 Jun 43

Structural and serological studies were performed with the lipopolysaccharide (LPS) expressed by Escherichia coli K12 strains No. 30 and No. 64, into which cosmid clones derived from Vibrio cholerae O1 NIH 41 (Ogawa) and NIH 35A3 (Inaba) had been introduced, respectively. The two recombinant strains, No. 30 (Ogawa) and No. 64 (Inaba), produced LPS that included, in common, the O-polysaccharide chain composed of an alpha (1-->2)-linked N-(3-deoxy-L-glycero-tetronyl)-D-perosamine (4-amino-4,6-dideoxy-D-manno-pyranose) homopolymer attached to the core oligosaccharide of the LPS of E. coli K12. Structural analysis revealed the presence of N-(3-deoxy-L-glycero-tetronyl)-2-O-methyl-D-perosamine at the non-reducing terminus of the O-polysaccharide chain of LPS from No. 30 (Ogawa) but not from No. 64 (Inaba). Serological analysis revealed that No. 30 (Ogawa) and No. 64 (Inaba) LPS were found to share the group antigen factor A of V. cholerae O1. They were distinguished by presence of the Ogawa antigen factor B [co-existing with relatively small amounts of the Inaba antigen factor (c)] in the former LPS and the Inaba antigen factor C in the latter LPS. It appears, therefore, that No. 30 (Ogawa) and No. 64 (Inaba) have O-antigenic structures that are fully consistent with the AB(c) structure for the Ogawa and the AC structure for the Inaba O-forms of V. cholerae O1, respectively. Thus, the present study clearly confirmed our previous finding that the Ogawa antigenic factor B is substantially related to the 2-O-methyl group at the non-reducing terminus of the alpha (1-->2)-linked N-(3-deoxy-L-glycero-tetronyl)-D-perosamine homopolymer that forms the O-polysaccharide chain of LPS of V. cholerae O1 (Ogawa).
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PMID:Lipopolysaccharides of Escherichia coli K12 strains that express cloned genes for the Ogawa and Inaba antigens of Vibrio cholerae O1: identification of O-antigenic factors. 890 6

The cell surface of E. coli initial parent strain K12 J62 his-, chemotype Ra, and E. coli transductant strain K12 J62 his+, acquiring the capacity for synthesizing primary S-specific side chains of the lipopolysaccharide of S. flexneri O-antigen (group-specific factor 3,4), was studied by the method of atomic force microscopy. The comparative analysis of the images of the genetically linked pair of E.coli strains K12 J62 revealed the presence of essential differences in the topography of the surface structure of the compared bacterial cells, differing in their capacity for synthesizing S. flexneri factor 3,4 represented by repeating chains of L-rhamnose and N-acetyl-D-glucosamine.
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PMID:[Differences in the cellular surface of hybrid Escherichia coli K12 bacteria inheriting the rfb a3,4 gene of Shigella flexneri detected using atomic-force microscopy]. 946 Aug 57

ADP-L-glycero-D-mannoheptose 6-epimerase is a 240 kDa NAD-dependent nucleotide diphosphosugar epimerase from Escherichia coli K12 which catalyzes the interconversion of ADP-D-glycero-D-mannoheptose and ADP-L-glycero-D-mannoheptose. ADP-L-glycero-D-mannoheptose is a required intermediate for lipopolysaccharide inner-core and outer-membrane biosynthesis in several genera of pathogenic and non-pathogenic Gram-negative bacteria. ADP-L-glycero-D-mannoheptose 6-epimerase was overexpressed in E. coli and purified to apparent homogeneity by chromatographic methods. Three crystal forms of the epimerase were obtained by a hanging-drop vapor-diffusion method. A native data set for crystal form III was collected in-house on a Rigaku R-AXIS-IIC image plate at 3.0 A resolution. The form III crystals belong to the monoclinic space group P21. The unit-cell parameters are a = 98.94, b = 110.53, c = 180.68 A and beta = 90.94 degrees. Our recent results show that these crystals diffract to 2.0 A resolution at the Cornell High Energy Synchrotron Source. The crystal probably contains six 40 kDa monomers per asymmetric unit, with a corresponding volume per protein mass (Vm) of 4.11 A3 Da-1 and a solvent fraction of 70%.
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PMID:Crystallization and preliminary X-ray diffraction studies of the lipopolysaccharide core biosynthetic enzyme ADP-L-glycero-D-mannoheptose 6-epimerase from Escherichia coli K-12. 1008 70

To gain insight into the value of lipopolysaccharide (LPS) core determinants for cross-protective immunisation the serological relationships between six complete (LPS) core types from Enterobacteriaceae were investigated. Hyperimmune sera were raised in mice by repeated immunisation with heat-killed strains of Salmonella choleraesuis (Ra core type) or Escherichia coli (core types R1, R2, R3, R4 and K12) and characterised for reactivity with complete and incomplete core chemotypes by ELISA and immunoblotting. Three sera (anti-Ra, anti-R2 and anti-R3) reacted strongly with 3-5 different complete core types whereas the other three (anti-R1, anti-R4 and anti-K12) reacted strongly only with their homologous core types in these assays. Two approaches were used to examine further the structural bases for cross-reactivity between these cores. By the first approach the anti-complete-core sera were tested for cross-reactivity with truncated forms of the Salmonella species core (incomplete cores) derived from core-defective mutants. By the second approach, antisera raised against some core-defective mutants were tested for cross-reactivity with complete cores. The results of these investigations revealed that several pair-wise combinations of core types can be used as immunogens to elicit immune responses that recognise all six core types and that the major determinants which mediate cross-reactivity between complete cores are localised in the outer core region.
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PMID:Cross-reactivity between six Enterobacteriaceae complete lipopolysaccharide core chemotypes. 1022 40


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