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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
MeSH Review


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Disease relevance of Ochrobactrum

  • The response to Brucella spp. and Ochrobactrum anthropi LPS was only significant at the concentration of 10 microg/ml [1].
  • Sodium dodecyl sulphate-polyacrylamide gel electrophoresis protein patterns and fatty acid methyl ester analysis identified six populations, representing 54% of the isolated bacteria, as belonging to the genera Acinetobacter and Ochrobactrum [2].
  • However, monoclonal antibodies A53/09G03/D02 and A53/01C10/A10 reacted with Phyllobacterium rubiacearum and/or Ochrobactrum anthropi, both bacteria of the alpha-2 subdivision of the class Proteobacteria [3].
  • Beneficial role of hydrophytes in removing Cr(VI) from wastewater in association with chromate-reducing bacterial strains Ochrobactrum intermedium and Brevibacterium [4].
  • 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 [5].

High impact information on Ochrobactrum

  • A gene homologous to MsrA was identified in a chromosomal fragment from the bacterium Ochrobactrum anthropi, and this gene is located just downstream of a GST gene identified previously (OaGST) [Favaloro, Tamburro, Angelucci, De Luca, Melino, Di Ilio and Rotilio (1998) Biochem. J. 335, 573-579] [6].
  • B. abortus and Ochrobactrum smooth LPS aggregates had similar size and zeta potential (-12 to -15 mV) [7].
  • Modulation of the glutathione S-transferase in Ochrobactrum anthropi: function of xenobiotic substrates and other forms of stress [8].
  • The gluthathione S-transferase gene of the atrazine-degrading bacterium Ochrobactrum anthropi (OaGST) encodes a single-subunit polypeptide of 201 amino acid residues (Favaloro et al. 1998, Biochem. J. 335, 573-579) [8].
  • Although Ochrobactrum was sensitive to polymyxin, self-promoted uptake and bacterial lysis occurred without OM morphological changes, suggesting an unusual OM structural rigidity [7].

Chemical compound and disease context of Ochrobactrum

  • 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 [9].
  • However, Ochrobactrum LPS, but not B. abortus LPS, contained galacturonic acid [7].
  • Purification, characterization, and gene cloning of purine nucleosidase from Ochrobactrum anthropi [10].
  • The L-leucyl, L-valyl and L-isoleucyl derivatives were hydrolysed readily to MTX by aminopeptidase M (EC, while the L-pyroglutamyl and D-alanyl compounds were activated by pyroglutamate aminopeptidase (EC (from Bacillus amyloliquefaciens) and D-aminopeptidase (from Ochrobactrum anthropi), respectively [11].
  • The transport of ammonium and methylammonium was studied in a strain of Ochrobactrum anthropi, a microorganism isolated from garden soil and able to degrade methyleneureas which are used as slow-release nitrogen fertilizer [12].

Biological context of Ochrobactrum


Gene context of Ochrobactrum

  • The gene coding for a novel glutathione S-transferase (GST) has been isolated from the bacterium Ochrobactrum anthropi [15].
  • Ochrobactrum anthropi is resistant to most cephalosporins and penicillins due, at least in part, to the inducible expression of a single beta-lactamase [16].
  • The gene encoding the D-stereospecific amino-acid amidase from Ochrobactrum anthropi SV3 was cloned and sequenced [17].
  • Iso 196(T) therefore represents a new species, for which the name Ochrobactrum gallinifaecis sp. nov. is proposed, with the type strain Iso 196(T) (= DSM 15295(T) = CIP 107753(T)) [18].
  • Commercial identification systems such as API 20NE and VITEK 2 were tested for their ability to identify Ochrobactrum anthropi and to detect other members of the genus Ochrobactrum [19].


  1. Interaction of endotoxins with Toll-like receptor 4 correlates with their endotoxic potential and may explain the proinflammatory effect of Brucella spp. LPS. Dueñas, A.I., Orduña, A., Crespo, M.S., García-Rodríguez, C. Int. Immunol. (2004) [Pubmed]
  2. Diversity of chromium-resistant and -reducing bacteria in a chromium-contaminated activated sludge. Francisco, R., Alpoim, M.C., Morais, P.V. J. Appl. Microbiol. (2002) [Pubmed]
  3. Localization and characterization of a specific linear epitope of the Brucella DnaK protein. Vizcaíno, N., Zygmunt, M.S., Verger, J.M., Grayon, M., Cloeckaert, A. FEMS Microbiol. Lett. (1997) [Pubmed]
  4. Beneficial role of hydrophytes in removing Cr(VI) from wastewater in association with chromate-reducing bacterial strains Ochrobactrum intermedium and Brevibacterium. Faisal, M., Hasnain, S. International journal of phytoremediation. (2005) [Pubmed]
  5. Heavy metal biosorption by biomass of Ochrobactrum anthropi producing exopolysaccharide in activated sludge. Ozdemir, G., Ozturk, T., Ceyhan, N., Isler, R., Cosar, T. Bioresour. Technol. (2003) [Pubmed]
  6. Bacterial peptide methionine sulphoxide reductase: co-induction with glutathione S-transferase during chemical stress conditions. Tamburro, A., Allocati, N., Masulli, M., Rotilio, D., Di Ilio, C., Favaloro, B. Biochem. J. (2001) [Pubmed]
  7. Brucella abortus and its closest phylogenetic relative, Ochrobactrum spp., differ in outer membrane permeability and cationic peptide resistance. Velasco, J., Bengoechea, J.A., Brandenburg, K., Lindner, B., Seydel, U., González, D., Zähringer, U., Moreno, E., Moriyón, I. Infect. Immun. (2000) [Pubmed]
  8. Modulation of the glutathione S-transferase in Ochrobactrum anthropi: function of xenobiotic substrates and other forms of stress. Favaloro, B., Tamburro, A., Trofino, M.A., Bologna, L., Rotilio, D., Heipieper, H.J. Biochem. J. (2000) [Pubmed]
  9. The DmpA aminopeptidase from Ochrobactrum anthropi LMG7991 is the prototype of a new terminal nucleophile hydrolase family. Fanuel, L., Goffin, C., Cheggour, A., Devreese, B., Van Driessche, G., Joris, B., Van Beeumen, J., Frère, J.M. Biochem. J. (1999) [Pubmed]
  10. Purification, characterization, and gene cloning of purine nucleosidase from Ochrobactrum anthropi. Ogawa, J., Takeda, S., Xie, S.X., Hatanaka, H., Ashikari, T., Amachi, T., Shimizu, S. Appl. Environ. Microbiol. (2001) [Pubmed]
  11. Activation and cytotoxicity of 2-alpha-aminoacyl prodrugs of methotrexate. Smal, M.A., Dong, Z., Cheung, H.T., Asano, Y., Escoffier, L., Costello, M., Tattersall, M.H. Biochem. Pharmacol. (1995) [Pubmed]
  12. Ammonium and methylammonium uptake in a fertilizer-degrading strain of Ochrobactrum anthropi. Ewen, H., Kaltwasser, H., Jahns, T. Antonie Van Leeuwenhoek (2000) [Pubmed]
  13. Nuclear magnetic resonance timecourse studies of glyphosate metabolism by microbial soil isolates. Gard, J.K., Feng, P.C., Hutton, W.C. Xenobiotica (1997) [Pubmed]
  14. Glutathione-dependent biotransformation of the fungicide chlorothalonil. Kim, Y.M., Park, K., Joo, G.J., Jeong, E.M., Kim, J.E., Rhee, I.K. J. Agric. Food Chem. (2004) [Pubmed]
  15. Molecular cloning, expression and site-directed mutagenesis of glutathione S-transferase from Ochrobactrum anthropi. Favaloro, B., Tamburro, A., Angelucci, S., Luca, A.D., Melino, S., di Ilio, C., Rotilio, D. Biochem. J. (1998) [Pubmed]
  16. Characterization, cloning and sequence analysis of the inducible Ochrobactrum anthropi AmpC beta-lactamase. Higgins, C.S., Avison, M.B., Jamieson, L., Simm, A.M., Bennett, P.M., Walsh, T.R. J. Antimicrob. Chemother. (2001) [Pubmed]
  17. Gene cloning, nucleotide sequencing, and purification and characterization of the D-stereospecific amino-acid amidase from Ochrobactrum anthropi SV3. Komeda, H., Asano, Y. Eur. J. Biochem. (2000) [Pubmed]
  18. Towards a standardized format for the description of a novel species (of an established genus): Ochrobactrum gallinifaecis sp. nov. Kämpfer, P., Buczolits, S., Albrecht, A., Busse, H.J., Stackebrandt, E. Int. J. Syst. Evol. Microbiol. (2003) [Pubmed]
  19. Molecular and phenotypic features for identification of the opportunistic pathogens Ochrobactrum spp. Teyssier, C., Marchandin, H., Jean-Pierre, H., Diego, I., Darbas, H., Jeannot, J.L., Gouby, A., Jumas-Bilak, E. J. Med. Microbiol. (2005) [Pubmed]
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