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  • American Society for Microbiology  (24)
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  • American Society for Microbiology  (24)
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  • 1
    Online Resource
    Online Resource
    American Society for Microbiology ; 1982
    In:  Journal of Bacteriology Vol. 149, No. 1 ( 1982-01), p. 15-21
    In: Journal of Bacteriology, American Society for Microbiology, Vol. 149, No. 1 ( 1982-01), p. 15-21
    Abstract: The distribution of mannosamine, mannosaminuronic acid, and the enzymes responsible for the formation of these saccharides was studied in nine species (18 strains) of Bacillus. Whereas UDP-N-acetylglucosamine 2-epimerase activity was detected in all of the strains examined, UDP-N-acetylmannosamine dehydrogenase, as well as the activity incorporating N-acetylmannosaminuronic acid residues from UDP-N-acetylmannosaminuronic acid into polymer, was found only in four strains of B. megaterium and one strain each of B. subtilis and B. polymyxa. The cell walls prepared from the six above-named strains were shown to contain mannosaminuronic acid in amounts of 135 to 245 nmol/mg. In contrast, mannosamine had a wide distribution. The cell walls from two strains of B. cereus and one strain each of B. circulans, B. polymyxa, B. sphaericus, and B. cereus subsp. mycoides contained mannosamine in amounts of 370 to 470 nmol/mg. In addition, the cell walls from five strains of B. subtilis, two strains of B. megaterium, and one strain each of B. cereus. B. coagulans, and B. licheniformis also contained this amino sugar in amounts as small as 10 to 35 nmol/mg. On the basis of analytical data, it is suggested that the mannosamine present in small amounts may be a common constituent of linkage units between peptidoglycan and other cell wall components such as glycerol teichoic acid.
    Type of Medium: Online Resource
    ISSN: 0021-9193 , 1098-5530
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1982
    detail.hit.zdb_id: 1481988-0
    SSG: 12
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  • 2
    Online Resource
    Online Resource
    American Society for Microbiology ; 1992
    In:  Journal of Bacteriology Vol. 174, No. 3 ( 1992-02), p. 1063-1067
    In: Journal of Bacteriology, American Society for Microbiology, Vol. 174, No. 3 ( 1992-02), p. 1063-1067
    Abstract: Escherichia coli K-12 harboring a part of the structural genes for the Klebsiella K2 capsular polysaccharide (cpsK*) expresses a large amount of K2 capsular polysaccharide as a thick capsule in the presence of plasmids carrying rmpA and rcsB. We have previously shown that expression of the Klebsiella K2 capsule in E. coli HB101 harboring cpsK* depends on the presence of rmpA, a regulatory gene from a large plasmid of Klebsiella pneumoniae Chedid (O1:K2). E. coli K-12 JM109, however, produces only a small amount of K2 capsular polysaccharide, even in the presence of plasmids carrying rmpA as well as the cpsK* structural genes. Introduction of the rcsB gene, a positive regulator of colanic acid capsule synthesis in E. coli K-12 which was cloned from HB101 on a plasmid, into JM109 cells carrying cpsK* and rmpA, results in the expression of a thick K2 capsule. By Northern (RNA) hybridization analysis, rcsB has been found to enhance transcription of a long strand of mRNA (longer than 14 kb) from cpsK*. These E. coli transformants which produce a thick K2 capsule also express colanic acid production at high levels. Therefore, rcsB can act as a positive regulator of Klebsiella K2 capsule production and two capsular polysaccharides can be expressed in E. coli simultaneously. With a somewhat different strain background, we have found that both of the colanic acid regulators, rcsA and rcsB, contribute to the basal level of Klebsiella K2 capsule expression but that the presence of multicopy rcsB in either an rcsB or an rcsA mutant of E. coli is sufficient to increase the expression of K2 capsular polysaccharide. These results suggest further parallels between the regulation of colanic acid synthesis in E. coli and the regulation of Klebsiella K2 capsule synthesis.
    Type of Medium: Online Resource
    ISSN: 0021-9193 , 1098-5530
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1992
    detail.hit.zdb_id: 1481988-0
    SSG: 12
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  • 3
    In: Infection and Immunity, American Society for Microbiology, Vol. 59, No. 6 ( 1991-06), p. 2043-2050
    Abstract: The genes determining the biosynthesis of type 2 (K2) capsular polysaccharide [3----beta Glc1,4----beta Man(1,3----beta GlcUA) 1,4----alpha Glc1----] of Klebsiella pneumoniae Chedid (O1:K2), which is highly virulent for mice, were cloned and introduced into Escherichia coli HB101 and into four noncapsulated mutants derived from K. pneumoniae reference strains of K1, K7, K9, and K28. The recombinant plasmid pCPS7B06 carried 23 kb of a chromosomal DNA fragment of strain Chedid and encoded a part of the Klebsiella cps gene cluster. However, pCPS7B06 encoded enough genetic information for the production of Klebsiella K2 capsular polysaccharide on the cell surfaces of four noncapsulated mutants of K. pneumoniae. On the other hand, both pCPS7B06 and pROJ3 carrying the rmpA gene locus derived from a resident large plasmid of Chedid were required for the biosynthesis of Klebsiella K2 capsular polysaccharide on the cell surface of E. coli HB101. The insertion inactivation analysis using Tn5 revealed that the cps gene cluster occupied more than 15 kb of the chromosome of Chedid. We conclude that rmpA, which has been known to enhance the biosynthesis of colanic acid in E. coli, is also involved in the biosynthesis of Klebsiella capsular polysaccharide in E. coli HB101.
    Type of Medium: Online Resource
    ISSN: 0019-9567 , 1098-5522
    RVK:
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1991
    detail.hit.zdb_id: 1483247-1
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  • 4
    Online Resource
    Online Resource
    American Society for Microbiology ; 1990
    In:  Journal of Bacteriology Vol. 172, No. 7 ( 1990-07), p. 4082-4089
    In: Journal of Bacteriology, American Society for Microbiology, Vol. 172, No. 7 ( 1990-07), p. 4082-4089
    Abstract: The introduction of a newly cloned Enterobacter cloacae chromosomal gene romA, into Escherichia coli and E. cloacae resulted in enhancement of resistance to quinolones, beta-lactams, chloramphenicol, and tetracycline. The primary effect of romA on a multicopy vector in E. coli was almost complete inhibition of OmpF expression in the outer membrane. From the experiments with ompR and envZ mutants or with ompF-lacZ and ompC-lacZ fusion plasmids, it was concluded that this inhibition is posttranscriptional. The introduction of romA on a multicopy vector into strains with micF deletion elicited only a moderate decrease in OmpF protein expression. This indicates that reduction of OmpF expression by romA is partly mediated posttranscriptionally by the activation of micF. Moreover, the overexpression of RomA protein from an isopropyl-beta-D-thiogalactopyranoside (IPTG)-inducible promoter resulted in nearly complete inhibition of expression of OmpC and OmpA, as well as OmpF. Taken together with an observation in a recent study that overexpressed OmpC inhibited the synthesis of OmpA and LamB, a possible inhibitory mechanism at the translational stage of the synthesis of outer membrane proteins should also be considered. By Southern hybridization, romA was generally detected in the chromosomes of all E. cloacae strains tested but not in the E. coli K-12 chromosome. Sequence data show that there is an open reading frame specifying 368 amino acids residues including a putative signal peptide. RomA appears to belong to the outer membrane protein family since it was extractable from an outer membrane preparation, but no sequence homology to other outer membrane proteins was detected.
    Type of Medium: Online Resource
    ISSN: 0021-9193 , 1098-5530
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1990
    detail.hit.zdb_id: 1481988-0
    SSG: 12
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  • 5
    In: Journal of Clinical Microbiology, American Society for Microbiology, Vol. 31, No. 5 ( 1993-05), p. 1173-1178
    Abstract: In order to study the relationships among the clinical features of hepatitis C patients, the presence of hepatitis C virus (HCV) RNA in their blood, and their serum antibody titers against the core protein of virus and to study the antibody levels in asymptomatic HCV carriers, a recombinant vaccinia virus containing a core protein gene was constructed. The recombinant virus expressed a protein with a molecular mass of 22 kDa in RK-13 cells as determined by Western blot (immunoblot) analysis. By using the cell lysate of virus-infected cells and serially diluted serum samples, core antibody titers in the groups of patients in the chronic hepatitis phase and in the convalescent phase as well as in asymptomatic carriers were determined by enhanced chemiluminescence Western blot analysis. Almost all patients in the chronic phase were shown to have high antibody titers of more than 1:500,000 and with no exception had of HCV RNA in their sera. On the other hand, patients who had recovered naturally and were in the convalescent phase were shown to have significantly lower antibody titers, and the antibody was not detected in the lowest serum dilution of 1:500 in 43% of these patients (three of seven total patients). Antibody levels of patients who showed a good response to interferon treatment decreased to intermediate levels between those of patients in the chronic phase and those of patients in convalescent phase. The antibody titers in asymptomatic carriers varied considerably from 1:500,000 to 1:500, and 41% (11 of 27 total individuals) of these carriers showed a high titer equivalent to that of those in the chronic phase. Core antibody was detected consistently in the individuals in whom HCV RNA was detected. This system for core antibody might be useful for identifying the stage of an apparent HCV infection.
    Type of Medium: Online Resource
    ISSN: 0095-1137 , 1098-660X
    RVK:
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1993
    detail.hit.zdb_id: 1498353-9
    SSG: 12
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  • 6
    Online Resource
    Online Resource
    American Society for Microbiology ; 1989
    In:  Journal of Bacteriology Vol. 171, No. 7 ( 1989-07), p. 3629-3633
    In: Journal of Bacteriology, American Society for Microbiology, Vol. 171, No. 7 ( 1989-07), p. 3629-3633
    Abstract: The rfb gene, involved in the synthesis of the O-specific polysaccharide (a mannose homopolymer) of Escherichia coli O9 lipopolysaccharide (LPS), was cloned in E. coli K-12 strains. The O9-specific polysaccharide covalently linked to the R core of K-12 was extracted from the K-12 strains harboring the O9 rfb gene. All the other genes required for the synthesis of rfe-dependent LPS are therefore considered to be present in the K-12 strains. It was found that bacteria harboring some clones with deletions of the ca. 20-kilobase-pair (kbp) BglII-StuI fragment no longer synthesized the O9-specific polysaccharide. However, bacteria harboring clones del 21, del 22, and del 25, which carry deletions of the 10-kbp PstI-StuI fragment, synthesized an O-specific polysaccharide antigenically distinct from E. coli O9 LPS. Although this new O-specific polysaccharide consisted solely of mannose and the mannose residues were combined only through alpha-1,2 linkage, it was still composed of a repeating oligosaccharide unit, possibly a trisaccharide unit,----2)alpha Man-(1----2)alpha Man-(1----2)alpha Man-(1----. It is therefore likely that this new O-specific polysaccharide was derived from a part of the O9-specific polysaccharide----3)alpha Man-(1----3)alpha Man-(1----2)alpha Man-(1----2)alpha Man-(1----2)alpha Man-(1----and that the deleted part of the clones was responsible for the synthesis of alpha-1,3 linkages of the O9-specific polysaccharide.
    Type of Medium: Online Resource
    ISSN: 0021-9193 , 1098-5530
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1989
    detail.hit.zdb_id: 1481988-0
    SSG: 12
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  • 7
    In: Journal of Clinical Microbiology, American Society for Microbiology, Vol. 46, No. 8 ( 2008-08), p. 2766-2773
    Abstract: The pandemic spread of Vibrio parahaemolyticus is an international public health issue. Because of the outbreak potential of the organism, it is critical to establish an internationally recognized molecular subtyping protocol for V. parahaemolyticus that is both rapid and robust as a means to monitor its further spread and to guide control measures in combination with epidemiologic data. Here we describe the results of a multicenter, multicountry validation of a new PulseNet International standardized V. parahaemolyticus pulsed-field gel electrophoresis (PFGE) protocol. The results are from a composite analysis of 36 well-characterized V. parahaemolyticus isolates from six participating laboratories, and the isolates represent predominant serotypes and various genotypes isolated from different geographic regions and time periods. The discriminatory power is very high, as 34 out of 36 sporadic V. parahaemolyticus strains tested fell into 34 distinguishable PFGE groups when the data obtained with two restriction enzymes (SfiI and NotI) were combined. PFGE was further able to cluster members of known pandemic serogroups. The study also identified quality measures which may affect the performance of the protocol. Nonadherence to the recommended procedure may lead to high background in the PFGE gel patterns, partial digestion, and poor fragment resolution. When these quality measures were implemented, the PulseNet V. parahaemolyticus protocol was found to be both robust and reproducible among the collaborating laboratories.
    Type of Medium: Online Resource
    ISSN: 0095-1137 , 1098-660X
    RVK:
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 2008
    detail.hit.zdb_id: 1498353-9
    SSG: 12
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  • 8
    Online Resource
    Online Resource
    American Society for Microbiology ; 1996
    In:  Infection and Immunity Vol. 64, No. 8 ( 1996-08), p. 3188-3195
    In: Infection and Immunity, American Society for Microbiology, Vol. 64, No. 8 ( 1996-08), p. 3188-3195
    Abstract: To determine the role of listeriolysin O (LLO) of Listeria monocytogenes in the host response at the initial stage of infection, cytokine gene expression in mouse peritoneal exudate macrophages and spleen cells was examined by reverse transcription-PCR. Expression of various cytokine mRNAs, especially those of interleukin-1 (IL-1), tumor necrosis factor alpha, gamma interferon (IFN-gamma), and IL-12, was observed to occur in spleen cells after direct stimulation with an LLO preparation purified to a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Induction of mRNA expression by LLO was not blocked by cholesterol, which abrogated the hemolytic activity of LLO. After the depletion of NK cells in spleen cells by treatment with anti-asialo GM1 antibody plus complement, LLO-induced expression of IFN-gamma was decreased, indicating that NK cells were the main source of IFN-gamma. After depletion of macrophages by passing spleen cells over a Sephadex G-10 column, expression of macrophage-derived cytokines, including IL-1alpha, tumor necrosis factor alpha, and IL-12, was diminished. In addition, IFN-gamma mRNA expression was impaired, indicating that IFN-gamma mRNA expression from NK cells required signaling from macrophages. It is suggested that LLO is capable of inducing endogenous cytokines of mice, and both NK cells and macrophages are involved in the host cytokine response to LLO.
    Type of Medium: Online Resource
    ISSN: 0019-9567 , 1098-5522
    RVK:
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1996
    detail.hit.zdb_id: 1483247-1
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  • 9
    In: Infection and Immunity, American Society for Microbiology, Vol. 72, No. 3 ( 2004-03), p. 1318-1325
    Abstract: Bacteroides forsythus is a gram-negative, anaerobic, fusiform bacterium and is considered to be an etiological agent in periodontal disease. A lipoprotein fraction prepared from B. forsythus cells by Triton X-114 phase separation (BfLP) activated human gingival fibroblasts and a human monocytic cell line, THP-1, to induce interleukin-6 production and tumor necrosis factor alpha production. BfLP was found to be capable of inducing nuclear factor-κB translocation in human gingival fibroblasts and THP-1 cells. By using Chinese hamster ovary K1 cells transfected with Toll-like receptor genes together with a nuclear factor-κB-dependent CD25 reporter plasmid, it was found that signaling by BfLP was mediated by Toll-like receptor 2 but not by CD14 or Toll-like receptor 4. BfLP induced apoptotic cell death in human gingival fibroblasts, KB cells (an oral epithelial cell line), HL-60 cells (a human myeloid leukemia cell line), and THP-1 cells but not in MOLT4 cells (a T-cell leukemia cell line). Caspase-8, an initiator caspase in apoptosis, was found to be activated in these cells in response to BfLP stimulation. Thus, this study suggested that BfLP plays some etiological roles in oral infections, especially periodontal disease, by induction of cell activation or apoptosis.
    Type of Medium: Online Resource
    ISSN: 0019-9567 , 1098-5522
    RVK:
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 2004
    detail.hit.zdb_id: 1483247-1
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  • 10
    Online Resource
    Online Resource
    American Society for Microbiology ; 1993
    In:  Infection and Immunity Vol. 61, No. 8 ( 1993-08), p. 3164-3174
    In: Infection and Immunity, American Society for Microbiology, Vol. 61, No. 8 ( 1993-08), p. 3164-3174
    Abstract: We determined the complete nucleotide sequence of a 2.1-kb HindIII-EcoRI fragment that was cloned from a resident large plasmid of Klebsiella pneumoniae Chedid, a highly virulent and mucoviscous strain of the O1:K2 serotype. This fragment encoded an ability to enhance K2 capsular polysaccharide synthesis in K. pneumoniae, and a 636-bp open reading frame (rmpA2) was found. The 411-bp rmpA reported to be involved in the virulence and mucoid phenotypes of K. pneumoniae by Nassif et al. (Mol. Microbiol. 3:1349-1359, 1989) was a part of rmpA2. Eighty percent homology in nucleotide sequence was found between rmpA2 and rmpA in the corresponding regions. The central domain of the deduced amino acid sequence of RmpA2 showed considerable homology to the central domains of NtrC of K. pneumoniae and Escherichia coli, to which the sigma factor of RNA polymerase binds. The C-terminal domain of RmpA2 also demonstrated considerable homology with the putative helix-turn-helix motifs of LuxR of Vibrio fischeri and FixJ of Rhizobium meliloti. Moreover, RmpA2 also showed some homology in its N- and C-terminal regions to those of RcsA, a transcriptional activator for colanic acid synthesis in E. coli. On the other hand, a sequence upstream of rmpA2 was found to be highly homologous to insertion sequence 3 of members of the family Enterobacteriaceae. Southern hybridization analysis suggested that rmpA2 exists on the large plasmids of all mucoviscous virulent K2 strains but not on those of the slightly mucoviscous avirulent strains. Freeze substitution electron microscopy and fluorescent-antibody staining with anti-K2 serum revealed that K. pneumoniae Chedid has a dense and thick capsule (180 nm) with dense extracapsular substance, whereas K. pneumoniae K2-215, one of the slightly mucoviscous and avirulent strains, has a capsule which is looser and thinner (120 nm) than that of strain Chedid and no extracapsular substance. Introduction of rmpA2 into K2-215 as well as reference strains K. pneumoniae K9 and K72 resulted in a change of the colony phenotype to highly mucoviscous through abundant production of extracapsular substance which reacted with anti-K2, -K9, or -K72, respectively, as did their parental strains. From these results, it is suggested that RmpA2 belongs to the family of transcriptional regulators and confers a highly mucoviscous phenotype on cells of various serotypes of K. pneumoniae by enhancing extracapsular polysaccharide synthesis.
    Type of Medium: Online Resource
    ISSN: 0019-9567 , 1098-5522
    RVK:
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1993
    detail.hit.zdb_id: 1483247-1
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