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Disease relevance of Pseudoalteromonas


High impact information on Pseudoalteromonas

  • In this context, we have constructed a double mutant (Q58C/A99C) of the cold-active and heat-labile alpha-amylase from the Antarctic bacterium Pseudoalteromonas haloplanktis, defined on the basis of its strong similarity with the mesophilic enzyme from pig pancreas [4].
  • We previously reported a new marine bacterium, Pseudoalteromonas phenolica sp. nov [5].
  • Fifteen strains of polycyclic aromatic hydrocarbon (PAH)-catabolizing bacteria, identified as Pseudoalteromonas spp. were isolated from Eagle Harbor, Puget Sound, USA, using a most probable number procedure in which naphthalene or phenanthrene was the sole carbon and energy source [6].
  • Cold-adapted beta-galactosidase from the Antarctic psychrophile Pseudoalteromonas haloplanktis [7].
  • Cycloprodigiosin hydrochloride (cPrG.HCl) obtained from a marine bacterium Pseudoalteromonas denitrificans induces apoptotic cell death in various cancerous cell lines. cPrG.HCl alone caused a little cytotoxicity in HeLa cells, but it enhanced the apoptotic process progressively when co-administered with tumor necrosis factor (TNF)alpha [8].

Chemical compound and disease context of Pseudoalteromonas

  • These results suggest that Pseudoalteromonas sp. strain A28 produced an extracellular serine protease which was responsible for the algicidal activity of this marine bacterium [9].
  • The phenotypic features of the isolates were similar to these of Pseudoalteromonas rubra ATCC 29570T, but they could be differentiated using 10 traits (growth at 37 degrees C, requirement for organic growth factors, bacteriolytic activity, utilization of sucrose, N-acetylglucosamine, fumarate, succinate, D-galactose, L-proline and acetate) [2].
  • The phenotypic features of Pseudoalteromonas elyakovii strains were closely related to that of Pseudoalteromonas espejiana IAM 12640T, but utilization of three carbon compounds (D-mannose, L-tyrosine and trehalose) distinguished both species [10].
  • According to the polyphasic evidence presented in this study, it is proposed that strain KMM 636T (= LMG 19692T = CIP 106859T) be classified as Pseudoalteromonas maricaloris sp. nov. and [P. aurantia] NCIMB 2033 be reclassified as Pseudoalteromonas flavipulchra NCIMB 2033T (= KMM 3630T = LMG 20361T) sp. nov [11].
  • The effect of low mean power laser irradiations with short pulse duration from an Nd:YAG (neodymium-doped yttrium aluminium garnet) laser on a marine biofilm-forming bacterium, Pseudoalteromonas carrageenovora, was investigated in the laboratory [12].

Biological context of Pseudoalteromonas

  • SIGNIFICANCE AND IMPACT OF THE STUDY: The production of glycosidases by Pseudoalteromonas issachenkonii KMM 3549(T) was significantly improved by using a simple nutrient medium containing peptone (2.5 g l(-1)) and xylose (5.0 g l(-1)) in 100% natural seawater [13].

Gene context of Pseudoalteromonas


  1. Elongation factor Ts from the Antarctic eubacterium Pseudoalteromonas haloplanktis TAC 125: biochemical characterization and cloning of the encoding gene. Raimo, G., Lombardo, B., Masullo, M., Lamberti, A., Longo, O., Arcari, P. Biochemistry (2004) [Pubmed]
  2. Pseudoalteromonas bacteriolytica sp. nov., a marine bacterium that is the causative agent of red spot disease of Laminaria japonica. Sawabe, T., Makino, H., Tatsumi, M., Nakano, K., Tajima, K., Iqbal, M.M., Yumoto, I., Ezura, Y., Christen, R. Int. J. Syst. Bacteriol. (1998) [Pubmed]
  3. Purification and characterization of the recombinant arylsulfatase cloned from Pseudoalteromonas carrageenovora. Kim, D.E., Kim, K.H., Bae, Y.J., Lee, J.H., Jang, Y.H., Nam, S.W. Protein Expr. Purif. (2005) [Pubmed]
  4. Dual effects of an extra disulfide bond on the activity and stability of a cold-adapted alpha-amylase. D'Amico, S., Gerday, C., Feller, G. J. Biol. Chem. (2002) [Pubmed]
  5. MC21-A, a bactericidal antibiotic produced by a new marine bacterium, Pseudoalteromonas phenolica sp. nov. O-BC30(T), against methicillin-resistant Staphylococcus aureus. Isnansetyo, A., Kamei, Y. Antimicrob. Agents Chemother. (2003) [Pubmed]
  6. Isolation and characterization of Pseudoalteromonas strains with divergent polycyclic aromatic hydrocarbon catabolic properties. Hedlund, B.P., Staley, J.T. Environ. Microbiol. (2006) [Pubmed]
  7. Cold-adapted beta-galactosidase from the Antarctic psychrophile Pseudoalteromonas haloplanktis. Hoyoux, A., Jennes, I., Dubois, P., Genicot, S., Dubail, F., François, J.M., Baise, E., Feller, G., Gerday, C. Appl. Environ. Microbiol. (2001) [Pubmed]
  8. Cycloprodigiosin hydrocloride suppresses tumor necrosis factor (TNF) alpha-induced transcriptional activation by NF-kappaB. Kamata, K., Okamoto, S., Oka, S., Kamata, H., Yagisawa, H., Hirata, H. FEBS Lett. (2001) [Pubmed]
  9. Involvement of an extracellular protease in algicidal activity of the marine bacterium Pseudoalteromonas sp. strain A28. Lee, S.O., Kato, J., Takiguchi, N., Kuroda, A., Ikeda, T., Mitsutani, A., Ohtake, H. Appl. Environ. Microbiol. (2000) [Pubmed]
  10. Assignment of Alteromonas elyakovii KMM 162T and five strains isolated from spot-wounded fronds of Laminaria japonica to Pseudoalteromonas elyakovii comb. nov. and the extended description of the species. Sawabe, T., Tanaka, R., Iqbal, M.M., Tajima, K., Ezura, Y., Ivanova, E.P., Christen, R. Int. J. Syst. Evol. Microbiol. (2000) [Pubmed]
  11. Pseudoalteromonas maricaloris sp. nov., isolated from an Australian sponge, and reclassification of [Pseudoalteromonas aurantia] NCIMB 2033 as Pseudoalteromonas flavipulchra sp. nov. Ivanova, E.P., Shevchenko, L.S., Sawabe, T., Lysenko, A.M., Svetashev, V.I., Gorshkova, N.M., Satomi, M., Christen, R., Mikhailov, V.V. Int. J. Syst. Evol. Microbiol. (2002) [Pubmed]
  12. Inhibition of bacterial attachment by pulsed Nd:YAG laser irradiations: an in vitro study using marine biofilm-forming bacterium Pseudoalteromonas carrageenovora. Nandakumar, K., Obika, H., Shinozaki, T., Ooie, T., Utsumi, A., Yano, T. Biotechnol. Bioeng. (2002) [Pubmed]
  13. Optimization of glycosidases production by Pseudoalteromonas issachenkonii KMM 3549(T). Alexeeva, Y.V., Ivanova, E.P., Bakunina, I.Y., Zvaygintseva, T.N., Mikhailov, V.V. Lett. Appl. Microbiol. (2002) [Pubmed]
  14. A DNA ligase from the psychrophile Pseudoalteromonas haloplanktis gives insights into the adaptation of proteins to low temperatures. Georlette, D., Jónsson, Z.O., Van Petegem, F., Chessa, J., Van Beeumen, J., Hübscher, U., Gerday, C. Eur. J. Biochem. (2000) [Pubmed]
  15. Kinetic and structural optimization to catalysis at low temperatures in a psychrophilic cellulase from the Antarctic bacterium Pseudoalteromonas haloplanktis. Garsoux, G., Lamotte, J., Gerday, C., Feller, G. Biochem. J. (2004) [Pubmed]
  16. The precursor of a psychrophilic alpha-amylase: structural characterization and insights into cold adaptation. Claverie, P., Vigano, C., Ruysschaert, J.M., Gerday, C., Feller, G. Biochim. Biophys. Acta (2003) [Pubmed]
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