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PubMed1961

Taxonomic relationships among the pseudomonads.

Colwell, R. R. (University of Washington, Seattle), and J. Liston. Taxonomic relationships among the pseudomonads. J. Bacteriol. 82:1-14. 1961.-An electronic computer technique, utilizing the Adansonian principle that every feature should have equal weight, was applied in an effort to derive a taxonomy of the Pseudomonas-Achromobacter group of gram-negative, asporogenous, rodlike bacteria. The validity of the general method was tested by an analysis of 40 well defined strains, principally derived from type culture collections and representative of different genera and families of the Pseudomonadales and the Eubacteriales. The analysis clearly separated groups which are recognized to be taxonomically distinct. Aerogenic Aeromonas were most similar to the Enterobacteriaceae and taxonomically distinct from the anaerogenic Aeromonas formicans which was more similar to the Pseudomonas group. Oxidative Vibrio species grouped with Pseudomonas and probably should be renamed Pseudomonas. Fermentative Vibrio species showed affinities with A. formicans.Fifty-four Pseudomonas strains out of 58 tested in an analysis of 80 bacterial cultures, clustered into four large groups: group 1, a marine group within which appeared a psychrophilic, nonproteolytic species subgroup related to Vibrio beijerinckii and a subgeneric subgroup which included Pseudomonas elongata; group 2, a subgeneric mesophilic group including Vibrio percolans and associated with Pseudomonas fragi; group 3, a fluorescent pigment-producing group, including three subgroups, a psychrophilic aeruginosa-like species group, a mesophilic Pseudomonas aeruginosa species group, and a heterogeneous subgeneric group containing Vibrio cuneatus and related to Pseudomonas fluorescens and Pseudomonas pavonacea; group 4, a subgeneric nonpigment-producing, mesophilic group, which included Vibrio tyrogenus, Pseudomonas ovalis, and Pseudomonas denitrificans.

Achromobacter↗
PubMed2003

Pathophysiology and management of pulmonary infections in cystic fibrosis.

This comprehensive State of the Art review summarizes the current published knowledge base regarding the pathophysiology and microbiology of pulmonary disease in cystic fibrosis (CF). The molecular basis of CF lung disease including the impact of defective cystic fibrosis transmembrane regulator (CFTR) protein function on airway physiology, mucociliary clearance, and establishment of Pseudomonas aeruginosa infection is described. An extensive review of the microbiology of CF lung disease with particular reference to infection with P. aeruginosa is provided. Other pathogens commonly associated with CF lung disease including Staphylococcal aureus, Burkholderia cepacia, Stenotrophomonas maltophilia, Achromobacter xylosoxidans and atypical mycobacteria are also described. Clinical presentation and assessment of CF lung disease including diagnostic microbiology and other measures of pulmonary health are reviewed. Current recommendations for management of CF lung disease are provided. An extensive review of antipseudomonal therapies in the settings of treatment for early P. aeruginosa infection, maintenance for patients with chronic P. aeruginosa infection, and treatment of exacerbation in pulmonary symptoms, as well as antibiotic therapies for other CF respiratory pathogens, are included. In addition, the article discusses infection control policies, therapies to optimize airway clearance and reduce inflammation, and potential future therapies.

Achromobacter↗
PubMed1997

Domon L, an immunopotentiating agent, acts as an NF-kappaB activator.

Domon L, a heat-treated component of gram-negative bacterium Achromobacter stenohalis, is used for the treatment of infectious diseases of animals. Here, we investigated the immunopotentiating potential of Domon L. In vitro studies showed that Domon L enhanced nitric oxide (NO) formation from murine macrophage RAW264.7 cells in concert with interferon (IFN)-gamma. The effect of Domon L on NF-kappaB activation was investigated, in order to understand the molecular mechanisms of enhanced NO formation by Domon L. Domon L induced translocation of NF-kappaB to the nucleus in RAW264.7 cells. Induction of NF-kappaB dependent gene expression by Domon L was further confirmed using a transfectant containing an NF-kappaB-luciferase reporter gene. In vivo injection of Domon L elevated both serum IL-6 and mucoprotein, whose gene expression is partly under the control of NF-kappaB. The spleen cells of rats treated with Domon L produced much more NO when stimulated with LPS + IFN gamma than spleen cells of untreated rats. These results suggest that Domon L acts as an anti-infectious agent via NF-kappaB activation.

Achromobacter↗
PubMedDate not supplied

[Biotransformation of organic substances by an immobilized associative bacterial culture].

Bacterial strains were screened to transform to end-products (carbon monoxide and water) elevated concentrations of acetone, acidic acid, and ethanol in a biocatalyst with an immobilized bacterial association cultivated on solid foam polyvinyl acetate (FPVA). The innocuous association amalgamated Paracoccus denitrificans VKM V-1324, Pseudomonas esterophilus VKM V-1736D and Achromobacter parvulus VKM V-1541D. The biocatalyst was tested with the help of classic methods and equipment for microbes cultivation. Microbial growth was assessed in the optical density units. Comparative evaluation of the biocatalytic activity was performed on gas-chromatographer Pue Unicam-104. Based on test results, specific rates of oxidation of acidic acid, ethanol and acetone per one g of FPVA were 0.75, 0.72, and 0.67 mg/hr, respectively.

Acetic Acid↗
PubMed1999

Reactivity of Lys(NH2)-containing peptides toward endopeptidases.

Lys(NH2)-containing peptides were subjected to various proteolytic enzymes which were selected for their well-documented specificity for arginyl and/or lysyl peptide bonds. Lys(NH2)-containing peptides were cleaved more rapidly by clostripain than the corresponding lysyl peptides. On the other hand, they proved to be resistant to Achromobacter protease I hydrolysis. The modified peptides synthesized in this study were more stable than the arginyl and lysyl analogues when incubated with trypsin or thrombin. The same tendency was observed when Lys(NH2)-containing peptides were incubated in diluted human serum, suggesting that the replacement of Arg or Lys by Lys(NH2) could be used to increase the stability of peptides in vivo.

Alcaligenes↗
PubMed2000

Profiling of Caenorhabditis elegans proteins using two-dimensional gel electrophoresis and matrix assisted laser desorption/ionization-time of flight-mass spectrometry.

The nematode Caenorhabditis elegans (C. elegans) is the first animal whose whole 97 Mb genome sequence, encoding ca. 19000 open reading frames (ORF's), has been essentially determined. We tried to establish a 2-DE map of the nematode proteome by means of two-dimensional polyacrylamide gel electrophoresis (2-D PAGE). A soluble protein fraction of mixed stages of the worm, wild-type strain N2, was applied to 2-D PAGE. After Coomassie Brilliant Blue (CBB) staining, 1200 spots were detected and 140 major spots were excised from the gel and subjected to in-gel digestion with Achromobacter protease I (lysyl endopeptidase). Resulting peptides were analyzed by matrix assisted laser desorption/ionization-time of flight-mass spectrometry (MALDI-TOF-MS) followed by peptide mass fingerprinting for protein identification. With this approach we have obtained a two-dimensional electrophoresis (2-DE) protein map in which 69 spots were localized as landmarks for comparison of expression profiles to elucidate the basis of various biological events.

Animals↗
PubMed2006

Plant growth promoting potential of free-living diazotrophs and other rhizobacteria isolated from Northern Indian soil.

The viable count of free-living diazotrophic bacteria in different crop rhizospheres varied from 1.11 x 10(4) to 8.5 x 10(5) CFU/g of soil. The majority of the diazotrophs phenotypically belong to either Azotobacter chroococcum, non-A. chroococcum type and to a heterogenous group tentatively named putative nitrogen-fixing (PNF) bacteria. In this study, 25 isolates of the PNF group were screened for their multiple plant growth-promoting (PGP) traits and grouped into 5 PGP types. An isolate, PNF(11) showed promising PGP potential in vitro and was characterized as a species of Achromobacter by 16S rRNA analysis. The isolate PNF(11) along with three other previously isolated PGP bacteria, Azotobacter sp. (AZS(3)), fluorescent pseudomonas (Ps(5)), Bacillus sp. (Bc(1)) were selected for crop inoculation response in green house experiment on Vigna radiata var.T44. Plants from inoculated and control pots were sampled and analyzed at 30, 45 and 60 days after sowing for various vegetative, nodule-related data and yield parameters. The findings indicated that selected isolate of PNF bacteria, and other PGP isolates with multiple activities significantly improve the plant growth parameters, yield parameters of Vigna radiata T44 over control and also show good compatibility with Bradyrhizobium inoculation.

Fabaceae↗
PubMed1991

Proton and tritium NMR relaxation studies of peptide inhibitor binding to bacterial collagenase: conformation and dynamics.

The interaction of succinyl-Pro-Ala, a competitive inhibitor of Achromobacter iophagus collagenase, with the enzyme was studied by longitudinal proton and tritium relaxation. Specific deuterium and tritium labeling of the succinyl part at vicinal positions allowed the measurement of the cross-relaxation rates of individual proton or tritium spin pairs in the inhibitor-enzyme complex as well as in the free inhibitor. Overall correlation times, internuclear distances, and qualitative information on the internal mobility in Suc1 (as provided by the generalized order parameter S2) could be deduced by the comparison of proton and tritium cross-relaxation of spin pairs at complementary positions in the -CH2- CH2- moiety as analyzed in terms of the model-free approach by Lipari and Szabo. The conformational and motional parameters of the inhibitor in the free and enzyme-bound state were directly compared by this method. The measurement of proton cross-relaxation in the Ala residue provided additional information on the inhibitor binding. The determination of the order parameter in different parts of the inhibitor molecule in the bound state indicates that the succinyl and alanyl residues are primarily involved in the interaction with the enzyme activity site. The succinyl moiety, characterized in solution by the conformational equilibrium among the three staggered rotamers--i.e., trans: 50%; g+: 20%; g-: 30%--adopted in the bound state the unique trans conformation.

Alcaligenes↗
PubMed2006

Transient performance of two-phase partitioning bioreactors treating a toluene contaminated gas stream.

Two-phase partitioning bioreactors (TPPBs) consist of a cell-containing aqueous phase and an immiscible organic phase that sequesters and delivers toxic substrates to cells based on equilibrium partitioning. The immiscible organic phase, which acts as a buffer for inhibitory substrate loadings, makes it possible for TPPBs to handle high volatile organic compound (VOC) loadings, and in this study the performance of liquid n-hexadecane and solid styrene butadiene (SB) polymer beads used as partitioning phases were compared to a single aqueous phase system while treating transient loadings of a toluene contaminated air stream by Achromobacter xylosoxidans Y234. The TPPBs operated as well-mixed stirred tanks, with total working volumes of 3 L (3 L aqueous for the single-phase system, 2 L aqueous and 1 L n-hexadecane for the solvent system, and 2.518 L aqueous volume and 500 g of SB beads for the polymer system). Two 60-min step changes (7 and 17 times the nominal loading rates, termed "small" and "large" steps, respectively) were imposed on the systems and the performance was characterized by the overall removal efficiencies, instantaneous removal efficiency recovery times (above 95% removal), and dissolved oxygen recovery times. For the small steps, with a nominal loading of 343 g/m3/h increasing to 2,400 g/m3/h, the TPPB system using n-hexadecane as the second phase performed best, removing 97% of the toluene fed to the system compared with 90% for the polymer beads system and only 69% for the single-phase system. The imposed large transient gave similar results, although the impact of the presence of a second sequestering phase was more pronounced, with the n-hexadecane system maintaining much reduced aqueous toluene concentrations leading to significantly improved performance. This investigation also showed that the presence of both n-hexadecane and SB beads improved the oxygen transfer within the systems.

Air Pollution↗
PubMed1977

Bacteriolysis by immobilized enzymes.

Bacteriolytic enzymes produced by Achromobacter lunatus were immobilized in collagen membrane. Intact bacteria such as Pseudomonas solanacearum, Xanthomonas oryzae, Staphylococcus aureus, and Pseudomonas aeruginosa were lyzed with the bacteriolytic enzyme-collagen membrane. Relative activity of the bacteriolytic enzyme-collagen membrane against Pseu. solanacearum was about 2% of that of native bacteriolytic enzymes. No difference in the optimum pH was observed between immobilized enzymes and native enzymes. The bacteriolytic enzymes in the collagen membrane were stable against sodium chloride which was an inhibitor of the native bacteriolytic enzymes. Xanthomonas oryzae and Pseu. aeruginosa were continuously lyzed by a reactor containing the rolled bacteriolytic enzyme-collagen membrane.

Alcaligenes↗
PubMed1990

Numerical analysis of sodium dodecyl sulphate-polyacrylamide gel electrophoretic protein patterns for the classification, identification and typing of medically important bacteria.

A numerical analysis of one-dimensional sodium dodecyl sulphate polyacrylamide gel electrophoretic protein patterns of three separate bacterial groups is described. Similarity between patterns was estimated using a correlation coefficient and is represented diagramatically by the unweighted pair-group with arithmetic averages method of clustering. Protein patterns were scanned using a laser densitometer interfaced directly to a microcomputer, where calculations were performed semi-automatically with specially written software. A method for the normalization of patterns from different gels is utilized. Whole cell protein patterns clearly distinguished strains representing various groups of Achromobacter. Similarly the two biovars of the Group EF-4 bacteria could be separated after analysis of partial "background patterns" as could the different species of Providencia. In addition, whole patterns could be used to type the various strains of P. rettgeri. These examples serve to illustrate the power, versatility and potential of the technique when applied to problems of classification, identification and typing of bacteria of medical interest. Its advantages and disadvantages, when compared to other available electrophoretic methodologies, are discussed, as is the future application of such technology to the hospital laboratory.

Bacteria↗
PubMed1996

S-pyridylethylation of intact polyacrylamide gels and in situ digestion of electrophoretically separated proteins: a rapid mass spectrometric method for identifying cysteine-containing peptides.

In-gel proteolytic digestion of acrylamide-gel separated proteins is a method widely used for generating peptide fragments for the purpose of identifying proteins by Edman degratation, tandem mass spectrometry, and peptide-mass fingerprinting. However, it is well recognised for disulfide-bonded proteins electrophoresed under reducing conditions that if no precautions are taken to minimise disulfide bond formation during protein digestion or peptide isolation, complex peptide maps can result. Here, we describe an improved method for in-gel protein digestion. It consists of first reducing and S-pyridylethylating Coomassie Brilliant Blue R-250-stained proteins immobilised in the whole gel slab with dithiothreitol and 4-vinylpyridine, excising the individual stained and alkylated proteins, and then digesting them in situ in the gel matrix with trypsin or Achromobacter lyticus protease I. Peptide fragments generated in this manner are extracted from the gel piece and purified to homogeneity by a rapid (< or = 12 min) reversed-phase high performance liquid chromatography (HPLC) procedure, based upon conventional silica supports. Recoveries of peptides are increased by S-pyridylethylation of acrylamide-immobilised proteins prior to in-gel digestion. Further, the levels of gel-related contaminants, which otherwise result in suppression of sample signals during electrosprayionisation mass spectrometry, are greatly reduced by the reduction/alkylation step. Additionally, we demonstrate that S-beta-(4-pyridylethyl)-cysteine containing peptides can be readily identified during reversed-phase HPLC by absorbance at 254 nm, and during electrospray ionisation tandem mass spectrometry by the appearance of a characteristic-pyridylethyl fragment ion of 106 Da. The position of cysteine residues in a sequence can be determined as phenylthiohydantoin S-beta-(4-pyridylethyl)-cysteine during Edman degradation, and by tandem mass spectrometry.

Acrylic Resins↗
PubMed2001

Purification and identification of monoubiquitin-phosphoglycerate mutase B complex from human colorectal cancer tissues.

Ubiquitin-conjugated proteins in human colorectal cancer tissues were analyzed by the immunoprecipitation with the antibody FK2 against conjugated ubiquitin followed with SDS-PAGE. In these immunoprecipitable proteins, a 38-kDa protein was abundant in the tumor regions but almost absent in the adjacent normal regions in 17/26 patients, thus we attempted to purify it. Using immunoaffinity chromatography with the antibody FK2 followed by gel filtration and SDS-PAGE, approximately 10 pmol of this protein was separated from 34 g of the pooled cancerous tissue and transferred onto a PVDF membrane. The 38-kDa protein was further digested with Achromobacter protease I, resulting in several peptide fragments. Amino acid sequences of these peptides showed complete sequence identity to those derived from either ubiquitin or phosphoglycerate mutase-B, suggesting that the 38-kDa protein is monoubiquitinated phosphoglycerate mutase-B, whose calculated mass is 37,369 Da. Western blot using an antibody against phosphoglycerate mutase-B revealed the presence of the 38-kDa protein in the anti-ubiquitin immunoprecipitates derived from the tumor regions, but not from normal counterparts. In addition, part of non-ubiquitinated phosphoglycerate mutase-B (29 kDa) was also found in the anti-ubiquitin immunoprecipitates, whose levels were higher in the tumor regions than in the adjacent normal regions. These results suggest that monoubiquitination of phosphoglycerate mutase-B as well as formation of a noncovalent complex containing ubiquitin and phosphoglycerate mutase-B increases in colorectal cancer and novel modification of phosphoglycerate mutase-B might have a pathophysiological role.

Aged↗
PubMedDate not supplied

Enzymatic semisynthesis of human insulin: an update.

Peptide bond formation can be enzymatically catalysed by the reverse reaction of proteases. Application is seen in the industrial production of human insulin. Human insulin derivative can be enzymatically prepared using either porcine insulin or the single chain B(1-29)-A(1-21) insulin precursor as the starting material. This is accomplished by either (1) digesting the starting material at Lys29 with Achromobacter lyticus protease I (Ach) and then coupling with Thr-X (X = blocking residue) (two-step reaction) or (2) subjecting Ala-B30 of porcine insulin or Gly-A1 of the single chain insulin precursor to transpeptidation with Thr-X (one-step reaction). Trypsin and Ach can be used for either type of reaction and, in the immobilized form, for the two-step reaction. Since the single chain insulin precursor can be produced by gene technology (yeast), use of immobilized trypsin or Ach and the two-step reaction using the single chain insulin precursor as the starting material ensures the continuous production of human insulin making it a feasible method for industrial manufacture.

Amino Acid Sequence↗
PubMed1997

Purification, characterization, and amino acid sequencing of DNase gamma from rat spleen.

An endonuclease named DNase gamma was purified to apparent homogeneity from rat splenocyte nuclei and its properties were characterized. We also determined the NH2-terminal and partial amino acid sequences of the proteolytic internal peptides. The molecular mass of gamma DNase was 33,000 daltons as determined by SDS-polyacrylamide gel electrophoresis. A native molecular mass of 30,000 was estimated by gel filtration. Purified DNase gamma is active in the presence of both Ca2+ and Mg2+ or Mn2+ alone and inhibited by Co2+, Ni2+, Cu2+, and especially Zn2+. Maximal activity was achieved at pH 7.2 in Mops-NaOH buffer. The sequence data on the NH2-terminal and seven internal peptides obtained by sequential digestions with Achromobacter protease I and endoproteinase Asp-N revealed that DNase gamma is a novel endonuclease that shows sequence homology with DNase I.

Amino Acid Sequence↗
PubMed1995

The complete amino acid sequence of a mannose-binding lectin from "Kidachi Aloe" (Aloe arborescens Miller var. natalensis Berger).

The complete amino acid sequence of a mannose-binding lectin purified from the leaf skin of "Kidachi Aloe" (Aloe arborescens Miller var. natalensis Berger) is presented. The 109-residue sequence of the subunit was determined by analysis of peptides of the intact or S-pyridylethylated protein generated by digestion with cyanogen bromide, BNPS-skatole, Achromobacter protease I, or trypsin. The subunit contains an intrachain disulfide bridge. The sequence is highly homologous to that of a mannose-binding lectin from snowdrop bulb.

Aloe↗
PubMed1997

Sulfated lipids as inhibitors of pancreatic trypsin and chymotrypsin in epithelium of the mammalian digestive tract.

Cholesterol sulfate and I3SO3-GalCer, which were commonly contained in the epithelia of mammalian digestive tracts, were found to inhibit the activities of typical digestive enzymes, pancreatic trypsin and chymotrypsin, but steroid sulfates, gangliosides and the other membrane constituents did not show any inhibitory activity. The preincubation of trypsin with I3SO3-GalCer at 37 degrees C for 10min was necessary to inhibit the activity of trypsin, but cholesterol sulfate showed its inhibitory activity without preincubation. Sulfated lipid-treated enzyme gave the same Km as and lower Vmax than those of the original enzymes. Also, both sulfated lipids inhibited pronase from Streptomyces griseus, but not lysyl endopeptidase from Achromobacter lyticus. These findings indicate that cholesterol sulfate and I3SO3-GalCer in the digestive tract function as epithelial inhibitors to prevent tissue injury by endogenous and exogenous proteases.

Animals↗
PubMed1999

Cloning, sequencing, and transcriptional studies of the gene encoding copper-containing nitrite reductase from Alcaligenes xylosoxidans NCIMB 11015.

Gene encoding of the blue copper-containing nitrite reductase (nir) from Alcaligenes xylosoxidans NCIMB 11015 has been cloned and characterized. The nir is translated into a polypeptide of 360 amino acid residues as a precursor, and the N-terminal 24 residues are subsequently removed upon transport into the periplasm as a mature protein. A specific transcription product of nir was detected only in the presence of nitrate. The aeration level of the culture medium did not show a significant effect on the transcriptional level. A varsigma54 binding sequence is identified upstream of the transcriptional initiation at 53 to 26 nucleotides. A putative fnr box has also been identified in the sequence of the upstream region. The mature polypeptide showed 70% sequence identity with those of the Achromobacter cycloclastes enzyme. The transcriptional start point has been determined at 92 nucleotides upstream of the initiation codon and is preceded by the binding sites for varsigma54 and the fnr box. These results suggest that gene expression depends on the presence of nitrate and is stimulated under an anaerobic environment.

5' Untranslated Regions↗