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PubMed1984

Corneal ulcer due to Achromobacter xylosoxidans.

We report a case of corneal ulcer caused by the opportunistic organism Achromobacter xylosoxidans which developed during chronic topical steroid treatment of an eye with neovascular glaucoma. A. xylosoxidans has probably been underreported as a cause of ocular infection because of confusion between this organism and other Gram-negative organisms, particularly pseudomonas. A. xylosoxidans is resistant to aminoglycosides and some cephalosporins but not carbenicillin. This difference in antibiotic sensitivity patterns between A. xylosoxidans and pseudomonas makes an accurate differentiation between the 2 organisms important. This case was successfully treated after substituting topical carbenicillin for topical gentamicin and amikacin.

Administration, Topical↗
PubMed1977

Strains of Achromobacter xylosoxidans from clinical material.

Eleven strains of Achromobacter xylosoxidans have been received from among 1106 strains of Gram-negative, non-fermentative bacteria submitted to the National Collection of Type Cultures for computer-assisted identification since 1 January 1972. The strains showed resistance to a wide range of antimicrobial agents and five of the isolates possibly played a pathogenic role. The biochemical characteristics of these 11 strains were compared with those of three culture collection strains.

Alcaligenes↗
PubMed1978

Cerebral ventriculitis associated with Achromobacter xylosoxidans.

Six patients in the neurosurgical ward of Fukushima Medical College Hospital suffering from ventriculitis due to Achromobacter xylosoxidans infection had undergone craniotomy or cranial trepanation before the infection. The strains of A. xylosoxidans isolated from the patients were resistant to streptomycin, ampicillin, cephaloridine, gentamicin, and colistin. They were also resistant to chlorhexidine digluconate (Hibitane) in a concentration of 2%. When a study of the chlorhexidine used in the hospital was carried out four strains of A. xylosoxidans were isolated from 20 containers of chlorhexidine solution in the surgical ward but not from those in the operating theatre.

Alcaligenes↗
PubMed1986

Electron paramagnetic resonance studies of heme c and its nitrosyl derivative in Vibrio (Achromobacter) fischeri nitrite reductase.

Interactions of Vibrio (formerly Achromobacter) fischeri nitrite reductase were studied by electron paramagnetic resonance spectroscopy. The spectrum of the oxidized enzyme showed a number of features which were attributed to two low-spin ferric hemes. These comprised an unusual derivative peak at g = 3.7 and a spectrum at g = 2.88, 2.26, and 1.51. Neither heme was reactive in the oxidized state with the substrate nitrite and with cyanide and azide. When frozen under turnover conditions (i.e., reduction in the presence of excess nitrite), the enzyme showed the spectrum of a nitrosyl heme derivative. The g = 2.88, 2.26, and 1.51 signals reappeared partially on reoxidation by nitrite, indicating that the nitrosyl species which remained arose from the g = 3.7 heme. The nitrosyl derivative showed a 14N nuclear hyperfine splitting, Az = 1.65 mT. The nitrosyl derivative was produced by treatment of the oxidized nitrite reductase with nitric oxide or hydroxylamine. Exchange of nitric oxide between the nitrosyl derivative and NO gas in solution was observed by using the [15N]nitrosyl compound. A possible reaction cycle for the enzyme is discussed, which involves reduction of the enzyme followed by binding of nitrite to one heme and formation of the nitrosyl intermediate.

Electron Spin Resonance Spectroscopy↗
PubMed2002

Histidine 210 mutant of a trypsin-type Achromobacter protease I shows broad optimum pH range.

Achromobacter protease I (API), a lysine-specific serine protease, shows one order of magnitude higher activity than bovine trypsin, while its optimum pH is in the alkaline region at about pH 9. To improve the optimum pH range, mutant enzyme His 210 replaced by Ser(H210S), Ala (H210A), and Lys (H210K) were constructed. The optimum pH of H210S shifted from about pH 9 (wild-type enzyme) to about pH 7, retaining its high activity. The putative electrostatic interaction between His 210 and catalytic Asp 113 was elucidated by the optimum-pH shift of H210K and H210A. These results indicate that this unconserved His 210 in API, which plays a key role in generating the useful peptidase, broadened the optimum-pH range without decreasing lysylendo-peptidase activity.

Journal Article↗
PubMed1994

Hydrolysis of S-2-aminoethylcysteinyl peptide bond by Achromobacter protease I.

The substrate specificity of Achromobacter protease I (API) was examined for S-2-aminoethyl(AE)cysteinyl bonds in Bz-AEC-OMe/OEt, Bz-AEC-NH2, and AE-insulin B chain. The protease hydrolyzed all of the tested AE-cysteinyl bonds at the same rate as that of lysyl bonds. Kinetic parameters were estimated for this hydrolysis reaction.

Alcaligenes↗
PubMed1999

The subunit structure of nitrite reductase purified from the denitrifier Achromobacter cycloclastes.

The copper-containing nitrite reductase of Achromobacter cycloclastes has been considered to be a homotrimer with three identical subunits both in the crystal and in solution. In this study, however, the enzyme was found to be a heterotrimer consisting of two subunits with molecular masses of 37 kDa and 36.2 kDa, and the 37 kDa subunit was 6 amino acid residues longer than the smaller subunit. Signal-peptide cleavage sites in its N-terminal region are discussed.

Alcaligenes↗
PubMed1989

Biological effects of lipopolysaccharide from Achromobacter stenohalis on lymphocytes and macrophages.

The immunopotentiating activities of lipopolysaccharide from Achromobacter stenohalis (A-LPS) were examined. A-LPS was structurally atypical and gave no endotoxin shock in A-LPS-inoculated mice. Analysis in vitro showed that A-LPS was a potent activator of both macrophages and B-lymphocytes. After macrophage stimulation with A-LPS, interleukin-1 (IL-1) secretion, interferon (IFN) production and chemiluminescence (CL) response were induced. A-LPS was a potent mitogen for spleen lymphocytes. However, induction of interleukin-2 (IL-2) secretion in T lymphocytes was not observed. These activities of A-LPS were similar to or higher than that of enterobacterial LPS.

Alcaligenes↗
PubMed1982

Experimental infection of immunocompromised mice with Achromobacter xylosoxidans.

The natural resistance of mice to Achromobacter (A.) xylosoxidans was decreased to 1/80 by a single dose of 250 mg of cylophosphamide (CY) per kg intraperitoneally. When mice were infected with 1 X 10(9) A. xylosoxidans, the numbers of organisms in the liver, spleen, kidneys, lungs and heart blood reached to more than 10(6) per g at 6 hr after infection, and then decreased to less than 10(4) at 96 hr after infection. However, in the CY-treated mice, the numbers of organisms in these organs began to increase rapidly at 6 hr after infection and exceeded 10(9) per g at 48 hr when the mice died. Seventeen of 18 immunocompromised mice and 23 of 24 normal mice which were infected with 1 to 2 X 10(9) organisms of A. xylosoxidans, respectively, were still living until 4 weeks after infection when they were killed and examined. Thirteen of the 33 surviving mice which were examined for bacteriological assay were chronically infected with A. xylosoxidans, some in the spleen, others in the kidney, lung, brain and/or heart blood but none were infected in the liver. Most of the infected and surviving mice had produced an antibody against A. xylosoxidans and its titer was higher in the bacteriologically "cured" group than in the chronically infected one. All surviving mice were resistant to the 2nd challenge with a lethal dose of A. xylosoxidans even when they received an effective dose of CY. The surviving mice showed activated cellular immunity and rather depressed humoral immunity as compared with normal mice or the mice which were infected with killed A. xylosoxidans.

Animals↗
PubMedDate not supplied

[Use of Pseudomonas and Achromobacter species bacteria--degraders of surface-active agents--for detection and destruction of polycyclic aromatic hydrocarbons].

The developed biosensor models were based on the use of immobilized Pseudomonas and Achromobacter cells for polycyclic aromatic hydrocarbons and surfactants detection. The responses of biosensors based on bacteria-degraders of anionic surfactants for organic substrates, which related to different classes of surfactants, aromatic and policyclic aromatic hydrocarbons (PAH) were investigated. The sensor showed the highest sensitivity to anionic surfactants and PAH. The lower limit of sodium dodecyl sulfate detection is within a range of 0.25-0.5 mg/l (0.86-1.73 microM). The sensors showed the highest sensitivity to naphthalene (1-6 mM) and anthracene, fluorene, phenanthrene. All strains that have been investigated may be used as a receptor element of biosensors for detection of PAH and surfactants.

Alcaligenes↗
PubMedDate not supplied

[Decomposition of cholesterol by Achromobacter candicans].

The decomposition of cholesterol by the cell suspensions of Achromobacter candicans 42 and by the cell-free extracts of this bacterium was studied. The decomposition of cholesterol in the presence of the wet biomass during four hours of the incubation was 72.5 percent, and with the cells that were preliminarily lyophilized or treated by acetone 49.8 and 23.0 percent, respectively. The activity decreased from 70.0 to 50.0 percent if the biomass was kept at minus 3 degrees C during 70 days. The decomposition of cholesterol by the cell-free preparations (supernatant and protein after precipitation with ammonium sulphate to 0.7 saturation) constituted 40.0 percent of the cholesterol contained in a sample. One of the intermediate products of cholesterol decomposition was delta4-cholesten-3-one.

Acetone↗
PubMedDate not supplied

[Biosynthesis of chitinase by Achromobacter liquefaciens].

Bacterial cultures under study synthesize exocellular chitinase on a medium containing chitin or demineralized crab shells as a source of carbon and nitrogen. Conditions for biosynthesis of chitinase by the cells of Achromobacter liquefaciens 301a were investigated under periodic and continuous conditions of cultivation. The preparation of chitinase isolated from the cultural broth of A. liquefaciens 301a hydrolysed colloid and native chitin at the optimum pH 6.5 and temperature 40degreesC. The terminal products of the reaction are chitobiose and N-acetylglucosamine.

Acetylglucosamine↗
PubMed1992

Vibrio alginolyticus ("Achromobacter") collagenase: biosynthesis, function and application.

Bacterial collagenase from aerobic non-pathogenic Vibrio alginolyticus chemovar iophagus ("Achromobacter" collagenase, EC 3.4.24.08) is an inducible extracellular metallo-proteinase. Production of Vibrio collagenase is induced specifically by collagen or by its macromolecular fragments. On the cell surface is expressed a specific receptor recognizing collagen structure. The study of natural inducers led to synthetic peptides with inducing properties. Vibrio collagenase cleaves collagen helical chains preferentially at 3/4 from the N-terminal. Its specific activity on synthetic substrate, 180,000 ukat/mg, represents the highest value for known collagenases. Its specificity differs from that of Clostridium: The enzyme cleaves preferentially sequences with Gly or Ala in position P'1 and Pro in position P2 or P'2. Highly specific cleavages were obtained in beta-casein, prolactin, myosin, adenylate kinase and fibronectin. Autolysis yields partially degraded forms still active on native collagen and peptide substrate. The determination of the sequence of Vibrio collagenase is nearly achieved; the enzyme was not yet obtained in crystalline form. On basis of the already known sequence and structure of Hypoderma collagenase (EC 3.4.21.49), a hypothesis is advanced on the character of collagen binding site loops. Vibrio collagenase can be produced in kilogram quantities at low cost. It was found highly efficient in debridement of necrotic burns, ulcers and decubitus.

Amino Acid Sequence↗
PubMed1989

Action of a bacterial Achromobacter collagenase on the soft carious dentine: an in vitro study with the scanning electron microscope.

Samples of carious human teeth treated in vitro for 48-92 hours with a bacterial Achromobacter collagenase in solution in borate buffer at 33 degrees were examined with the scanning electron microscope. The enzyme was seen to destroy soft carious dentine but not sound layers of dentine beneath the lesion. This finding may have clinical implications.

Adult↗
PubMed1989

Fatal neonatal meningitis and ventriculitis caused by multiresistant Achromobacter xylosoxidans. A case report.

Meningitis and ventriculitis in a 6-day-old neonate caused by a Gram-negative glucose-non-fermenting organism, Achromobacter xylosoxidans, was resistant to most antibiotics except ceftazidime and imipenem. The organism became resistant after 28 days treatment with ceftazidime. When the infant was 7 weeks old, imipenem became available but, in spite of 3 days of intravenous treatment, the organism was still recovered from ventricular cerebrospinal fluid and the child died. This would appear to be only the second report of neonatal meningitis caused by this organism.

Alcaligenes↗
PubMed1989

Achromobacter xylosoxidans corneal ulcer in a therapeutic soft contact lens wearer.

Achromobacter xylosoxidans is an opportunistic organism that is usually seen in immunocompromised or immunosuppressed patients. It is an aerobic gram-negative rod, often confused with other more commonly seen gram-negative bacteria such as Pseudomonas aeruginosa. The organism is usually sensitive to extended spectrum penicillins such as carbenicillin and usually resistant to aminoglycosides and first generation cephalosporins. We wish to describe a corneal ulcer from A. xylosoxidans that developed in a patient wearing a therapeutic soft contact lens. The patient did not have a preexisting microbial keratitis and was not receiving corticosteroid therapy.

Aged↗
PubMed1988

Resonance Raman spectra of the copper-sulfur chromophores in Achromobacter cycloclastes nitrite reductase.

Resonance Raman spectroscopy at ambient temperature and 77 K has been used to probe the structures of the copper sites in Achromobacter cycloclastes nitrite reductase. This enzyme contains three copper ions per protein molecule and has two principal electronic absorption bands with lambda max values of 458 and 585 nm. Comparisons between the resonance Raman spectra of nitrite reductase and blue copper proteins establish that both the 458 and 585 nm bands are associated with Cu(II)-S(Cys) chromophores. A histidine ligand probably is also present. Different sets of vibrational frequencies are observed with 457.9 nm (ambient) or 476.1 nm (77 K) excitation as compared with 590 nm (ambient) or 593 nm (77 K) excitation. Excitation profiles indicate that the 458 and 585 nm absorption bands are associated with separate [Cu(II)-S(Cys)N(His)] sites or with inequivalent and uncoupled cysteine ligands in the same site. The former possibility is considered to be more likely.

Alcaligenes↗
PubMed1988

Studies on ampicillin resistance in Achromobacter xylosoxidans. Brief report.

Population analyses of susceptibility to ampicillin in ampicillin-susceptible and ampicillin-resistant strains of Achromobacter xylosoxidans revealed the existence of ampicillin-resistant subpopulations in ampicillin-susceptible isolates. Bacteria resistant to a concentration four times the one that inhibited the majority population had a frequency of 10(-3) to 10(-4). Strains isolated from aqueous environments are often found susceptible to ampicillin, while sporadic cases of infections with A. xylosoxidans are often caused by ampicillin-resistant strains. We suggest that the isolation from clinical specimens of ampicillin-susceptible strains, therefore, may be an indication of nosocomial infections due to recently contaminated aqueous solutions or medical equipment.

Alcaligenes↗