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PubMed1989

A new D-stereospecific amino acid amidase from Ochrobactrum anthropi.

A new D-stereospecific amino acid amidase has been partially purified from Ochrobactrum anthropi SCRC SV3, which had been isolated and selected from soil. The Mr of the enzyme was estimated to be about 38,000, and its isoelectric point was 5.3. The enzyme catalyzes the stereospecific hydrolysis of D-amino acid amide to yield D-amino acid and ammonia. The major substrates included D-phenylalanine amide, D-tyrosine amide, D-tryptophan amide, D-leucine amide, and D-alanine amide.

Alcaligenes↗
PubMed1994

An outbreak of Ochrobactrum anthropi bacteraemia in five organ transplant patients.

Nosocomial bacteraemia caused by Ochrobactrum anthropi occurred over a 1-month period in five organ transplant recipients, four of whom were in the same renal and pancreatic transplant unit. Bacteraemia occurred with cyclosporin A, azathioprine and steroids, and with a rabbit anti-thymocyte globulin (RATG) during the induction phase. RATG appeared to be the only common factor among the five cases. Over the period described, 71.4% of all patients receiving RATG developed O. anthropi bacteraemia. Three patients presented with fever and chills during or shortly after RATG infusion. Analysis of residues of the infusion, and the used vials of RATG, showed the presence of O. anthropi in concentrations of between 20 and 1000 cfu ml-1 in 5.3% of samples. Unused vials were found to be heavily contaminated with either O. anthropi or Microbacterium spp. in 23.5% of samples. All positive vials were of one particular lot number suggesting a malfunction in the manufacturing process. Many parenteral drugs such as the RATG used here do not contain preservatives and, although aseptically prepared, will not withstand thermal sterilization. Bacterial contamination of these small volume medications is not always easily detectable by conventional methods. This outbreak highlights the need for accurate quality control testing to detect small inocula that may occur during or after the manufacturing process.

Adult↗
PubMed1998

Structural studies on the lipopolysaccharide from a rough strain of Ochrobactrum anthropi containing a 2,3-diamino-2,3-dideoxy-D-glucose disaccharide lipid A backbone.

A degradation protocol using de-O-acylation and subsequent alkaline de-N-acylation was applied to the lipopolysaccharide of Ochrobactrum anthropi rough strain LMG 3301. Three main oligosaccharide bisphosphates containing core-lipid A backbone structures were obtained after fractionation by anion-exchange HPLC. Using 1H and 13C NMR spectroscopy, including two-dimensional COSY, TOCSY, and NOE spectroscopy (ROESY and NOESY), the following structures were established: [formula: see text] where Kdo is 3-deoxy-D-manno-octulosonic acid, D-GlcN3N is 2,3-diamino-2,3-dideoxy-D- glucose and R is H or alpha-D-GalpA or 4-deoxy-beta-L-threo-hex-4-enopyranuronic acid, the latter sugar being derived from alpha-D-GalpA by beta-elimination of a substituent attached to 0-4. This is the first report on the isolation from a lipopolysaccharide of an oligosaccharide containing GlcN3N in the lipid A backbone [beta-D-GlcpN3N4P-(1-->6)-alpha-D-GlcpN3N1 P]. Sugar and methylation analysis confirmed the presence of the GalA-->Kdo disaccharide and non-stoichiometric substitution of GalA. It is suggested that Glc is the substituent at 0-4 in GalA and that in the non-degraded lipopolysaccharide the amino group of GlcN is not acylated.

Carbohydrate Sequence↗
PubMedDate not supplied

Intravenous line infection due to Ochrobactrum anthropi (CDC Group Vd) in a normal host.

Ochrobactrum anthropi, formerly known as Achromobacter species (CDC group Vd), is an aerobic, gram-negative bacillus widely distributed in aquatic environments. Most important, it has been implicated as a cause of intravenous line infection in immunocompromised hosts with solid tumors or hematologic malignancies. Trimethoprim-sulfamethoxazole and aminoglycosides are usually active against O. anthropi, but this organism is usually resistant to beta-lactam antibiotics. Because O. anthropi is a low-virulence organism, patients with intravenous-line infections have been cured without removal of the intravenous catheter. We describe a case of intravenous-line infection in a normal host that was successfully resolved alter catheter removal.

Catheterization, Central Venous↗
PubMed2003

Heavy metal biosorption by biomass of Ochrobactrum anthropi producing exopolysaccharide in activated sludge.

The removal of chromium, cadmium and copper, toxic metals of high environmental priority due to their toxicity, from dilute aqueous solutions has been studied in the present work, applying a dead exopolysaccharide producing bacterium, Ochrobactrum anthropi, isolated from activated sludge. Particularly, the effect of pH, metal concentration and the effects of contact time were considered. Optimum adsorption pH values of chromium(VI), cadmium(II) and copper(II) were 2.0, 8.0 and 3.0 respectively. Experimental results also showed the influence of initial metal concentration on the metal uptake for dried biomass. Both the Freundlich and Langmuir adsorption models were suitable for describing the short-term biosorption of chromium(VI), cadmium(II) and copper(II) by O. anthropi.

Absorption↗
PubMed2004

Paraquat resistance of transgenic tobacco plants over-expressing the Ochrobactrum anthropi pqrA gene.

Transgenic tobacco plants over-expressing the Ochrobactrum anthropi pqrA gene, which encodes a membrane transporter mediating resistance to paraquat, were generated. Transgenic plants displayed higher resistance against paraquat than wild-type plants, as estimated by plant viability, ion leakage and chlorophyll loss, but no resistance against other active oxygen generators, such as H2O2 and menadione. Moreover, lower levels of paraquat accumulated in transgenic plants, compared to wild-type plants, indicating that the PqrA protein detoxifies paraquat either via increased efflux or decreased uptake of the herbicide, but not by removing active oxygen species. The results collectively demonstrate that the bacterial paraquat resistance gene, pqrA, can be functionally expressed in plant cells, and utilized for the development of paraquat-resistant crop plants.

Bacterial Proteins↗
PubMed1998

Molecular cloning, expression and site-directed mutagenesis of glutathione S-transferase from Ochrobactrum anthropi.

The gene coding for a novel glutathione S-transferase (GST) has been isolated from the bacterium Ochrobactrum anthropi. A PCR fragment of 230 bp was obtained using oligonucleotide primers deduced from N-terminal and 'internal' sequences of the purified enzyme. The gene was obtained by screening of a genomic DNA partial library from O. anthropi constructed in pBluescript with a PCR fragment probe. The gene encodes a protein (OaGST) of 201 amino acids with a calculated molecular mass of 21738 Da. The product of the gene was expressed and characterized; it showed GST activity with substrates 1-chloro-2, 4-dinitrobenzene (CDNB), p-nitrobenzyl chloride and 4-nitroquinoline 1-oxide, and glutathione-dependent peroxidase activity towards cumene hydroperoxide. The overexpressed product of the gene was also confirmed to have in vivo GST activity towards CDNB. The interaction of the recombinant GST with several antibiotics indicated that the enzyme is involved in the binding of rifamycin and tetracycline. The OaGST amino acid sequence showed the greatest identity (45%) with a GST from Pseudomonas sp. strain LB400. A serine residue in the N-terminal region is conserved in almost all known bacterial GSTs, and it appears to be the counterpart of the catalytic serine residue present in Theta-class GSTs. Substitution of the Ser-11 residue resulted in a mutant OaGST protein lacking CDNB-conjugating activity; moreover the mutant enzyme was not able to bind Sepharose-GSH affinity matrices.

Amino Acid Sequence↗
PubMedDate not supplied

Ochrobactrum anthropi bacteremia.

Ochrobactrum Anthropi (O. anthropi ), formerly known as Achromobacter CDC group Vd, is a gram-negative bacillus that is aerobic, oxidase producing, and nonlactose fermenting. This organism has been found in environmental and hospital water sources and has pathogenic potential in humans. Most reports in the literature of O. anthropi bacteremia are associated with intravenous line infections. We describe a case of bacteremia with O. anthropi in a 33-month-old boy with acute osteomyelitis. O. anthropi bacteremia also has been reported in immunocompromised hosts. Rarely, O. anthropi has been a cause of soft tissue or bone infection.

Alcaligenes↗
PubMed1992

Catheter-associated sepsis caused by Ochrobactrum anthropi: report of a case and review of related nonfermentative bacteria.

Ochrobactrum anthropi, formerly known as CDC group Vd, is an oxidase-producing, gram-negative, non-lactose-fermenting bacillus that oxidizes glucose and grows readily on MacConkey agar. Only occasionally isolated from human clinical specimens, this organism has rarely been found to be pathogenic. We describe the first reported case of infection due to O. anthropi in a child, that of bacteremia in a 3-year-old girl undergoing chemotherapy for retinoblastoma. In addition, we review the literature concerning cases of infection due to this and closely related bacterial species, namely Alcaligenes xylosoxidans subspecies xylosoxidans, Agrobacterium radiobacter, and "Achromobacter" group B. Finally, we attempt to clarify the confusing history and taxonomy of these organisms as well as make recommendations regarding antimicrobial therapy for infections caused by them.

Anti-Bacterial Agents↗
PubMed1994

Infections with the unusual human pathogens Agrobacterium species and Ochrobactrum anthropi.

Agrobacterium species and Ochrobactrum anthropi are generally considered innocuous in clinical settings, yet during the last decade a number of sporadic cases of human infection due to these organisms have been reported. We studied nine cases of infection (septicemia and peritonitis) caused by Agrobacterium-like microorganisms in eight patients. All patients were immunocompromised and had permanent central venous or peritoneal dialysis catheters in place. Seven patients were women, and eight infections were community acquired. Six isolates were identified as Agrobacterium species and three as O. anthropi. These two groups of strains differed in the production of beta-galactosidase and of acid from lactose, erythritol, salicin, and cellobiose. All strains were strictly aerobic, peritrichous, gram-negative bacilli that produced oxidase, urease, and acid from glucose, fructose, arabinose, xylose, mannitol, inositol, and ethanol. The in vitro adherence of isotope-labeled bacteria to silicone tubes was similar to that of staphylococci. We conclude that Agrobacterium species and O. anthropi can be pathogenic in immunocompromised patients with permanent catheters.

Adult↗
PubMed1996

Pyogenic infections due to Ochrobactrum anthropi.

Ochrobactrum anthropi is a nonfermentative gram-negative bacillus that has been isolated with increasing frequency from human clinical specimens. Previously, its pathogenic niche was believed to involve the causation of catheter-associated bacteremic illnesses. We describe three cases of pyogenic infection due to O. anthropi, thereby expanding the known pathogenic potential of this organism.

Adult↗
PubMed1996

Ochrobactrum anthropi meningitis in pediatric pericardial allograft transplant recipients.

An epidemiologic investigation was done after 3 patients contracted Ochrobactrum anthropi meningitis at one hospital in October 1994. Neurosurgical patients with pericardial tissue implants were at greater risk of infection than other neurosurgical patients (3/14 vs. 0/566; P<.001). Cultures of implants removed from 2 case-patients, an implant at implantation, a nonimplanted pericardial tissue, and an unwrapped but unopened bottle of Hank's balanced salt solution (HBSS) grew O. anthropi. Patient and tissue isolates had identical genotypes; the isolate from the HBSS bottle had a unique genotype. Culture samples from an unopened HBSS bottle and from pericardial tissue grew Pseudomonas stutzeri of the same genotype; however, no P. stutzeri infections were detected. The investigation documented intrinsic P. stutzeri contamination of HBSS. O. anthropi contamination of tissues occurred during processing, possibly due to extrinsic contamination of HBSS. Active surveillance is needed to detect infection in patients receiving transplanted tissues, and rigorous infection control practice are necessary during tissue harvesting and processing to ensure sterility.

Alcaligenes↗
PubMed1998

Purification and characterization of a novel glutathione transferase from Ochrobactrum anthropi.

Glutathione transferase was purified from Ochrobactrum anthropi and its N-terminal sequence was determined to be MKLYYKVGACSLAPHIILSEAGLPY. The apparent molecular mass of the protein (24 kDa) was determined by SDS-polyacrylamide gel electrophoresis analysis. The amino acid sequence obtained showed similarities with known bacterial glutathione transferases in the range of 72-64%. Immunoblotting experiments performed with antisera raised against glutathione transferase from O. anthropi did not show cross-reactivity with two bacterial glutathione transferases belonging to Serratia marcescens and Proteus mirabilis.

Antibody Specificity↗
PubMed1996

Effects of atrazine on Ochrobactrum anthropi membrane fatty acids.

Ochrobactrum anthropi is a gram-negative bacillus recognized as a human opportunist pathogen isolated in clinical specimens and not of clinical significance. We report a new aspect of this bacterium, that it has been isolated from activated sludge. In fact, it is able to grow on atrazine (2-chloro-4-ethylamino-6-isopropyl-amine-s-triazine) by utilizing it as the only source of carbon. Our results show that atrazine (0.03 g/liter) causes a dramatical increase in the degree of saturation of membrane fatty acids. Analysis and identification of bacterial fatty acids were performed by gas chromatography and gas chromatography-mass spectrometry techniques.

Alcaligenes↗
PubMed1997

Antibody and delayed-type hypersensitivity responses to Ochrobactrum anthropi cytosolic and outer membrane antigens in infections by smooth and rough Brucella spp.

Immunological cross-reactions between Brucella spp. and Ochrobactrum anthropi were investigated in animals and humans naturally infected by Brucella spp. and in experimentally infected rams (Brucella ovis infected), rabbits (Brucella melitensis infected), and mice (B. melitensis and Brucella abortus infected). In the animals tested, O. anthropi cytosolic proteins evoked a delayed-type hypersensitivity reaction of a frequency and intensity similar to that observed with B. melitensis brucellin. O. anthropi cytosolic proteins also reacted in gel precipitation tests with antibodies in sera from Brucella natural hosts with a frequency similar to that observed with B. melitensis proteins, and absorption experiments and immunoblotting showed antibodies to both Brucella-specific proteins and proteins common to Brucella and O. anthropi. No antibodies to O. anthropi cytosolic proteins were detected in the sera of Brucella-free hosts. Immunoblotting with sera of Brucella-infected sheep and goats showed immunoglobulin G (IgG) to Brucella group 3 outer membrane proteins and to O. anthropi proteins of similar molecular weight. No IgG to the O-specific polysaccharide of O. anthropi lipopolysaccharide was detected in the sera of Brucella-infected hosts. The sera of sheep, goats, and rabbits infected with B. melitensis contained IgG to O. anthropi rough lipopolysaccharide and lipid A, and B. ovis and O. anthropi rough lipopolysaccharides showed equal reactivities with IgG in the sera of B. ovis-infected rams. The findings show that the immunoresponse of Brucella-infected hosts to protein antigens is not necessarily specific for brucellae and suggest that the presence of O. anthropi or some related bacteria explains the previously described reactivities to Brucella rough lipopolysaccharide and outer membrane proteins in healthy animals.

Animals↗
PubMed1997

Meningitis due to Ochrobactrum anthropi: an emerging nosocomial pathogen. A report of 3 cases.

We describe 3 cases of Ochrobactrum anthropi meningitis following the implantation of pericardial allograft tissue to cover dural defects following craniotomy. Following an extensive epidemiologic investigation, the tissue allograft was found to have been contaminated with this unusual organism during the harvesting and processing of the tissue in the tissue bank. This organism was only susceptible to imipenem, tetracycline, gentamicin, and ciprofloxacin. The clinical presentation of these patients was subacute. Two of the patients developed osteomyelitis of the bone flap; while another developed a relapse of infection along a former ventriculoperitoneal shunt track 6 months after the initial infection. Appropriate clinical outcome was only observed after removal of tissue allograft implants, debridement of devitalized tissue and bone, removal of shunt devices, and prolonged courses of antibiotics. No deaths were observed.

Adolescent↗
PubMed1999

The DmpA aminopeptidase from Ochrobactrum anthropi LMG7991 is the prototype of a new terminal nucleophile hydrolase family.

The DmpA (d-aminopeptidase A) protein produced by Ochrobactrum anthropi hydrolyses p-nitroanilide derivatives of glycine and d-alanine more efficiently than that of l-alanine. When regular peptides are utilized as substrates, the enzyme behaves as an aminopeptidase with a preference for N-terminal residues in an l configuration, thus exemplifying an interesting case of stereospecificity reversal. The best-hydrolysed substrate is l-Ala-Gly-Gly, but tetra- and penta-peptides are also efficiently hydrolysed. The gene encodes a 375-residue precursor, but the active enzyme contains two polypeptides corresponding to residues 2-249 (alpha-subunit) and 250-375 (beta-subunit) of the precursor. Residues 249 and 250 are a Gly and a Ser respectively, and various substitutions performed by site-directed mutagenesis result in the production of an uncleaved and inactive protein. The N-terminal Ser residue of the beta-subunit is followed by a hydrophobic peptide, which is predicted to form a beta-strand structure. All these properties strongly suggest that DmpA is an N-terminal amidohydrolase. An exploration of the databases highlights the presence of a number of open reading frames encoding related proteins in various bacterial genomes. Thus DmpA is very probably the prototype of an original family of N-terminal hydrolases.

Amidohydrolases↗