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1.
Mycopathologia ; 184(1): 13-21, 2019 Feb.
Article in English | MEDLINE | ID: mdl-30291485

ABSTRACT

Aspergillus species are the most common pathogenic fungi involved in otomycosis, an infection of the outer ear canal. In this study, we examined the incidence of Aspergillus infections and the antifungal susceptibilities of 30 Aspergillus species isolates from patients with otomycosis who visited Saiseikai Utsunomiya Hospital between August 2013 and July 2016. Based on the morphological test results, the strains were identified as Aspergillus niger sensu lato (20 strains), A. terreus sensu lato (7 strains), and A. fumigatus sensu lato (3 strains). In contrast, the molecular identifications based on analyzing the isolates' partial ß-tubulin gene sequences revealed them to be A. niger sensu stricto (12 strains), A. tubingensis (8 strains), A. terreus sensu stricto (7 strains), and A. fumigatus sensu stricto (3 strains). The antifungal susceptibility test results indicated that strains of A. tubingensis and A. niger sensu stricto displayed lower susceptibilities to ravuconazole, compared with the other isolates. The Aspergillus strains from this study showed low minimum inhibitory concentrations toward the azole-based drugs efinaconazole, lanoconazole, and luliconazole. Therefore, these topical therapeutic agents may be effective for the treatment of otomycosis.


Subject(s)
Antifungal Agents/pharmacology , Aspergillosis/microbiology , Aspergillus/classification , Aspergillus/isolation & purification , Otomycosis/microbiology , Adult , Aged , Aged, 80 and over , Aspergillosis/epidemiology , Aspergillus/drug effects , Aspergillus/genetics , Azoles/pharmacology , Female , Humans , Incidence , Japan/epidemiology , Male , Microbial Sensitivity Tests , Middle Aged , Otomycosis/epidemiology , Tubulin/genetics
2.
J Infect Chemother ; 20(4): 274-7, 2014 Apr.
Article in English | MEDLINE | ID: mdl-24486169

ABSTRACT

Desulfovibrio spp. can be found in soil, water, and sewage, as well as in the digestive tracts of animals and humans. We report a case of Desulfovibrio desulfuricans bacteremia during hospitalization with acute cerebral infarction following aspiration bronchopneumonia and severe diarrhea, and the case strongly suggests that Desulfovibrio spp. bacteremia can occur as an infection due to disturbance of endogenous gut flora including antibiotic administration. Because Desulfovibrio spp. is difficult to detect in short-time incubation, its bacteremia is possibly overlooked in hospitalized patients. A few clinical cases of D. desulfuricans bacteremia have been reported in Japan, and they are reviewed briefly in this article.


Subject(s)
Bacteremia/microbiology , Cerebral Infarction/microbiology , Desulfovibrio desulfuricans/isolation & purification , Desulfovibrionaceae Infections/microbiology , Aged, 80 and over , Humans , Japan , Male
3.
Eur J Immunol ; 33(10): 2842-52, 2003 Oct.
Article in English | MEDLINE | ID: mdl-14515268

ABSTRACT

We show that Proteus vulgaris O25 (PO25) lipopolysaccharide (LPS) induced an anaphylactoid reaction not only in wild-type and in lipid A non-responding mice but also in recombinase-activating gene-2-deficient (RAG-2(-/-)) and in mast cell-deficient (W/Wv) animals. Western blot analysis indicated that PO25 LPS bound to Ra-reactive factor (RaRF), the complex of mannan-binding lectins (MBL) and MBL-associated serine proteases. Binding of RaRF to PO25 LPS led to the activation of C4 component without participation of either C1 or Ig, via the lectin pathway. Relative concentration of RaRF and hemolytic activity in mouse serum decreased rapidly during the process of anaphylactoid reaction. A significant drop of MBL-A, but not MBL-C level was observed. Administrationwith antiserum to RaRF prevented animals from death as a consequence of the inhibition of interaction of RaRF with the carbohydrate target and complement activation. These results indicate that complement-lectin pathway activation is responsible for the anaphylactoid reaction induced with LPS in muramyldipeptide-primed mice. RaRF also activated fibrinogen in vitro suggesting the involvement of the coagulation system in the process investigated.


Subject(s)
Anaphylaxis/etiology , Complement Activation , Lipopolysaccharides/toxicity , Mannose-Binding Lectin/physiology , Serine Endopeptidases/physiology , Animals , Fibrinogen/metabolism , Mannose-Binding Protein-Associated Serine Proteases , Mice , Mice, Inbred BALB C , Mice, Inbred C3H
4.
Microbiol Immunol ; 46(11): 761-6, 2002.
Article in English | MEDLINE | ID: mdl-12516772

ABSTRACT

An immunoglobulin enriched bovine colostrum preparation, IMMULAC (New Zealand Dairy Group, Cambridge, New Zealand), contains antibodies against various bacterial antigens. In the present study, we investigated the protective effects of a commercial bovine colostrum preparation against infections with enterohaemorrhagic Escherichia coli (EHEC) O157:H7 in a murine model. Balb/c mice were given drinking water containing streptomycin for 3 days before and following oral challenge with streptomycin-resistant EHEC O157:H7 strain (O157-SM(R)). In mice pretreated with streptomycin, EHEC O157:H7 maintained stable levels of bacterial colonization in the intestines for the 3-week experimental time period. Oral administration of colostrum resulted in rapid decrease in the bacteria numbers compared with administration of skim-milk. Colostrum showed no direct in vitro bactericidal properties against either EHEC O157:H7. When sections prepared from cecum walls of streptomycin-pretreated mice were incubated in vitro with EHEC O157:H7, the colostrum significantly prevented the attachment of the organisms to the sections when compared with skim-milk. These results indicate that oral administration of bovine colostrum effectively protects mice against food-borne infections by inhibiting bacterial attachment to the intestinal mucous membrane, colonization and growth in the intestinal tract.


Subject(s)
Colostrum/immunology , Escherichia coli Infections/prevention & control , Escherichia coli O157/pathogenicity , Escherichia coli Vaccines/immunology , Immunoglobulins/immunology , Aging/immunology , Animals , Anti-Bacterial Agents/therapeutic use , Cattle , Cecum/microbiology , Colony Count, Microbial , Disease Models, Animal , Drug Resistance, Bacterial , Escherichia coli O157/drug effects , Female , Mice , Mice, Inbred BALB C , Streptomycin/therapeutic use
5.
J Med Microbiol ; 50(10): 865-869, 2001 Oct.
Article in English | MEDLINE | ID: mdl-11599735

ABSTRACT

As assessed by the lipopolysaccharide (LPS)-specific chromogenic Limulus amoebocyte lysate (LAL) assay, Helicobacter pylori LPS extracted by the phenol-water procedure showed full potency to coagulate LAL, as did LPS from Salmonella minnesota and Escherichia coli. However, pretreatment of H. pylori LPS with polymyxin B, which easily destroys the endotoxic activity of enterobacterial LPS/lipid A, had little effect on the LAL coagulation activity, although the same treatment of E. coli LPS markedly diminished its activity. The H. pylori LPS induced very weak production of nitric oxide (NO) or tumour necrosis factor (TNF) by murine macrophages and TNF by human peripheral whole blood in vitro in comparison with S. minnesota LPS. These findings indicate that H. pylori LPS has the unique endotoxic characteristic of retaining full LAL coagulation activity with polymyxin B resistance, despite losing its endotoxic potencies such as the ability to induce NO and TNF production.


Subject(s)
Helicobacter pylori/metabolism , Lipopolysaccharides/pharmacology , Adult , Animals , Cells, Cultured , Female , Helicobacter Infections/microbiology , Helicobacter pylori/chemistry , Helicobacter pylori/isolation & purification , Humans , Limulus Test , Lipopolysaccharides/isolation & purification , Lipopolysaccharides/toxicity , Macrophages, Peritoneal/drug effects , Macrophages, Peritoneal/metabolism , Male , Mice , Mice, Inbred C3H , Nitric Oxide/analysis , Nitric Oxide/biosynthesis , Polymyxin B/pharmacology , Tumor Necrosis Factor-alpha/analysis , Tumor Necrosis Factor-alpha/biosynthesis
6.
J Med Microbiol ; 49(2): 127-138, 2000 Feb.
Article in English | MEDLINE | ID: mdl-10670563

ABSTRACT

The saccharide constituents of lipopolysaccharides (LPS) of Proteus spp. vary with the strain and contain unique components about which little is known. The biological activities of LPS and lipid A from S- and R-forms of 10 Proteus strains were examined. LPS from all S-form Proteus strains was lethal to D-(+)-galactosamine (GalN)-loaded, LPS-responsive, C3H/HeN mice, but not to LPS-hypo-responsive C3H/HeJ mice. P. vulgaris 025 LPS evoked strong anaphylactoid reactions in N-acetylmuramyl-L-alanyl-D-isoglutamine (MDP)-primed C3H/HeJ mice. LPS from S- and R-form Proteus strains induced production of nitric oxide (NO) and tumour necrosis factor (TNF) by macrophages isolated from C3H/HeN but not C3H/HeJ mice. Lipid A from Proteus strains also induced NO and TNF production, although lipid A was less potent than LPS. The effects of LPS were mainly dependent on CD14; LPS-induced NO and TNF production in CD14+ J774.1 cells was significantly greater than in CD14-J7.DEF.3 cells. All LPS from Proteus strains, and especially from P. vulgaris 025, exhibited higher anti-complementary activity than LPS from Escherichia coli or Pseudomonas aeruginosa. Polymyxin B inactivated proteus LPS in a dose-dependent manner, but these LPS preparations were more resistant to polymyxin B than E. coli LPS. CAP18(109-135), a granulocyte-derived peptide, inhibited proteus LPS endotoxicity only when the LPS:CAP18(109-135) ratio was appropriate, which suggests that CAP18(109-135) acts through a different mechanism than polymyxin B. The results indicate that LPS from Proteus spp. are potently endotoxic, but that the toxicity is different from that of LPS from E. coli or Salmonella spp. and even varies among different Proteus strains. The variation in biological activities among proteus LPS may be due to unique components within the respective LPS.


Subject(s)
Antimicrobial Cationic Peptides , Carrier Proteins/pharmacology , Lipopolysaccharides/toxicity , Peptide Fragments/pharmacology , Polymyxin B/pharmacology , Proteus/drug effects , Proteus/pathogenicity , Acetylmuramyl-Alanyl-Isoglutamine/administration & dosage , Amino Acid Sequence , Anaphylaxis/chemically induced , Animals , Carbohydrate Sequence , Carrier Proteins/chemistry , Cathelicidins , Complement Inactivator Proteins/pharmacology , Female , Galactosamine/administration & dosage , Lipid A/antagonists & inhibitors , Lipid A/toxicity , Lipopolysaccharide Receptors/immunology , Lipopolysaccharides/antagonists & inhibitors , Macrophage Activation , Male , Mice , Mice, Inbred C3H , Molecular Sequence Data , Nitric Oxide/biosynthesis , Proteus/metabolism , Proteus mirabilis/drug effects , Proteus mirabilis/metabolism , Proteus mirabilis/pathogenicity , Proteus vulgaris/drug effects , Proteus vulgaris/metabolism , Proteus vulgaris/pathogenicity , Tumor Necrosis Factor-alpha/biosynthesis
7.
J Med Microbiol ; 48(5): 471-477, 1999 May.
Article in English | MEDLINE | ID: mdl-10229544

ABSTRACT

The ability of several Pseudomonas aeruginosa exo-enzymes, including exotoxin A (ETA), to induce inflammation and their influence on endotoxin-induced tumour necrosis factor (TNF) production in murine lung were evaluated. Intratracheal administration of lipopolysaccharide (LPS; 0.1-10 microg/mouse), 2(-1) LD50 of P. aeruginosa alkaline protease (7.5 microg/mouse) and elastase (1.2 microg/mouse) elevated total cell number and the percentage of neutrophils in broncho-alveolar lavage fluid (BALF), whereas ETA (0.1 microg/mouse) did not. LPS induced TNF production in BALF in a dose-dependent manner, whereas the P. aeruginosa exo-enzymes did not. When ETA was inoculated into the respiratory tract before LPS, production of TNF in BALF was significantly suppressed in a dose-dependent manner. ETA also suppressed TNF production by alveolar macrophages (AMs) stimulated with LPS in vitro. Flow cytometric analysis showed that ETA markedly reduced the expression of CD14 and CD11c/CD18 on the surface of AMs. ETA also depressed partially the expression of TNF-alpha mRNA in AMs. These findings suggest that ETA regulates TNF production in murine lung by suppressing LPS receptor expression, mRNA expression and protein synthesis and/or secretion of TNF.


Subject(s)
ADP Ribose Transferases , Bacterial Proteins , Bacterial Toxins , Exotoxins/toxicity , Lipopolysaccharides/toxicity , Lung/drug effects , Tumor Necrosis Factor-alpha/biosynthesis , Virulence Factors , Animals , Bronchoalveolar Lavage Fluid/cytology , CD18 Antigens/analysis , Down-Regulation , Integrin alphaXbeta2/analysis , Lethal Dose 50 , Lipopolysaccharide Receptors , Macrophages, Alveolar , Male , Metalloendopeptidases/toxicity , Mice , RNA, Messenger/analysis , Serine Endopeptidases/toxicity , Tumor Necrosis Factor-alpha/genetics , Pseudomonas aeruginosa Exotoxin A
8.
Microbiol Immunol ; 26(7): 585-597, 1982 Jul.
Article in English | MEDLINE | ID: mdl-28941250

ABSTRACT

Butanol-extracted water-soluble adjuvant (Bu-WSA) obtained from Bacterionema matruchotii was cultured with peripheral blood mononuclear cells (PBM) in the presence of sub- and/or supra-optimal mitogenic concentrations of concanavalin A (Con A). The addition of Bu-WSA resulted in increased tritiated thymidine incorporation above that produced by Con A alone. Bu-WSA by itself is not mitogenic for PBM and in fact produced a decrease in thymidine uptake compared to the control. We investigated the response of subpopulation(s) of PBM to Bu-WSA, Con A and a mixture of Bu-WSA and Con A. Separation of PBM into purified T cells, B cells and macrophages showed that cell-cell cooperation of T cells with B cells or macrophages is necessary for the observed synergistic effect of Bu-WSA with Con A. A marked increase in thymidine incorporation by the mixture of T and B cell populations occurred, while only a small amount of thymidine was incorporated when the B cell population was absent. Mitomycin treatment revealed that the response could be ascribed to the T-cell response with a B-cell helper effect. Moreover, Con A and Bu-WSA appeared to act on the same T cell population. This model may provide unique information about the activation of human peripheral blood T cells compared with the activation of these cells by other mitogens.

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