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PubMed1991

A novel lipopolysaccharide-binding hemagglutinin isolated from hemocytes of the solitary ascidian, Halocynthia roretzi: it can agglutinate bacteria.

A hemagglutinin was isolated from hemocytes of the ascidian, Halocynthia roretzi, by a procedure including extraction and ion-exchange chromatography on CM-cellulose. The molecular weight of the hemagglutinin was estimated to be 120,000 by gel filtration. It was resistant to acid treatment but sensitive to alkali or heat treatment. The hemagglutinating activity was inhibited by heparin, chondroitin sulfate, and lipopolysaccharide (LPS), but not by mono- and disaccharides such as N-acetyl-galactosamine, galactose, and melibiose. The hemagglutinin showed binding ability to heparin and LPS, as demonstrated by heparin-Sepharose chromatography and centrifugation experiments, respectively. It was also found that the hemagglutinin can bind to various bacteria such as Escherichia coli, Bacillus subtilis, Vibrio anguillarum, Pseudomonas perfectomarinus, Achromobacter aquamarinus, and Alteromonas putrefaciens, and can agglutinate all of them.

Animals↗
PubMed1982

Chemical modification of lysine residues in bacterial formate dehydrogenase.

Specific modification of 4.4 lysine residues per molecule of formate dehydrogenase, from the methylotrophic bacterium Achromobacter parvulus I by pyridoxal, results in complete inactivation of the enzyme. The concentration effect of the modifying agent and substrates on the inactivation of formate dehydrogenase has been studied. Coenzymes do not protect the enzyme from inactivation. Complete maintenance of enzyme activity was achieved in the presence of saturating concentrations of the formate and upon formation of the ternary complex, enzyme-NAD-azide. Formate specifically protects two lysine residues per dimer molecule of the enzyme from modification. The presence of one essential lysine residue in the substrate-binding region of the enzyme active site is assumed.

Alcaligenes↗
PubMed1987

Detergent inhibition of nitric-oxide reductase activity.

Gas chromatography revealed that exposure of extracts of the denitrifiers 'Achromobacter cycloclastes', Paracoccus denitrificans, Pseudomonas aeruginosa and Pseudomonas perfectomarina to Triton X-100 inhibited reduction of NO to N2O, and thus concomitantly inhibited reduction of NO2- to N2O. After exposure of extracts to Triton X-100, the ratio of H+ consumed to NO2- added decreased from approx. 2.0 (for untreated extracts) to approx. 1.5, which indicated that NO2- was reduced to NO by the treated extracts. Addition of a CHAPS-soluble extract (devoid of nitrite reductase activity but rich in nitric-oxide reductase activity) to the Triton X-100-treated extract of P. denitrificans restored capacity for reduction of NO2- on to N2O. Exposure to either the NO that accumulated from reduction of NO2- or to enthetic NO transiently inhibited rates of NO2- reduction in Triton X-100-treated extracts. Use of an Oxides of Nitrogen analyzer indicated that only 5-33% of NO2- reduced by untreated extracts appeared in the stripping gas as NO, whereas 80-95% of NO2- reduced by Triton X-100-treated extracts was recovered as NO.

Alcaligenes↗
PubMed1992

Proteolytic processing of human lysosomal arylsulfatase A.

Arylsulfatase A purified from human placenta contained an unreported component with an apparent molecular mass of 7 kDa in addition to the two known components with apparent molecular masses of 58 and 50 kDa. The detailed relationship between the 58 kDa component and the 50 kDa component is as yet unknown. The present study was undertaken to define the structure of the subunits of the sulfatase. The N-terminal sequence of the 50 kDa component was identical to that of the 58 kDa component. Furthermore, the peptide maps of the 50 kDa component, which was separately digested with trypsin and Achromobacter proteinase I, were quite similar to those of the 58 kDa one. Through sequence analysis of the incompatible peaks in the peptide maps, the 50 kDa component was found to lack a sequence from Val-445 to the C-terminus. On the other hand, the N-terminal sequence of the 7 kDa component began with Ala-448, though there was a minor sequence commencing with Thr-449. These observations suggest that the 50 and 7 kDa components were produced by limited proteolysis near the C-terminus of the 58 kDa component. Through analysis using unreducing SDS-PAGE, the 58 and the 7 kDa components were found to be linked by disulphide bonds. Arylsulfatase A purified from human liver was also composed of the same subunits as the placental one. This finding suggests that human arylsulfatase A undergoes similar proteolytic processing regardless of the tissue involved.

Amidohydrolases↗
PubMed1993

Pro-major basic protein has three types of sugar chains at the pro-portion.

The amino-acid sequence of purified recombinant pro-major basic protein from Chinese hamster kidney cells was determined to verify the primary structure and glycosylation sites. Reduced and S-carboxamidemethylated protein was first digested with Achromobacter proteinase I. Each peptide was characterized by amino-acid analysis and amino-acid sequence analysis. We could identify all the peptides which were expected from the pro-major basic protein cDNA sequence. Sequence analysis and deglycosylation study revealed that Ser-8, Thr-9, Ser-46 and Asn-70 were glycosylated. The results indicated that proMBP has three types of sugar chains, O-glycoside, N-glycoside and glycosaminoglycan, in the pro-portion.

Amino Acid Sequence↗
PubMed1996

The 30 kDa protein co-purified with chick liver glutathione S-transferases is a carbonyl reductase.

An unidentified 30 kDa protein was co-purified with chick liver glutathione S-transferases from S-hexylglutathione affinity column. The protein was isolated to apparent homogeneity with chromatofocusing. The molecular mass of the protein was determined to be 30 277 +/- 3 dalton by mass spectrometry. The protein was digested with Achromobacter proteinase I. Amino-acid sequence analyses of the resulting peptides show a high degree of identity with those of human carbonyl reductase. The protein is active with menadione as substrate. Thus, it is identified as chick liver carbonyl reductase.

Alcohol Oxidoreductases↗
PubMed1990

Absence of role for plasmids in resistance to multiple disinfectants in three strains of bacteria.

Three chlorhexidine-resistant strains, two of Achromobacter xylosoxidans, one of Pseudomonas cepacia, were isolated from clinical sources. The three strains showed cross-resistance to benzethonium chloride, benzalkonium chloride and alkyldiaminoethylglycine. Resistance persisted after treatment of the strains with acridine orange (12.5 mg-25 mg l-1). Conjugation to appropriate recipients of Escherichia coli was unsuccessful and plasmid DNA could not be detected. These results suggest that plasmids do not play a role in resistance to multiple disinfectants in the strains of bacteria studied.

Alcaligenes↗
PubMed1994

Handwashing machines, handwashing compliance, and potential for cross-contamination.

Although handwashing is considered an important factor in the prevention of nosocomial infections, the optimal technique has not been determined and compliance is often difficult to obtain. Handwashing compliance is particularly important in intensive care areas of the hospital. In an effort to improve HW compliance, the surgical intensive care unit in our hospital purchased three handwashing machines. Four months after installation of the handwashing machines, an outbreak of methicillin-resistant Staphylococcus aureus occurred in the intensive care unit. As part of evaluating the outbreak, we cultured the handwashing machines, including the portholes and the paper towel dispenser. Cultures were positive for methicillin-resistant Staphylococcus epidermidis, Achromobacter species, and Streptococcus viridans. The design of the handwashing machines made contamination of sleeves and already-washed hands possible. An observational study revealed that handwashing compliance was poor but improved from 22% to 38% when the handwashing machines were in use. Nurses preferred handwashing at the sink and physicians preferred the handwashing machine. Handwashing machines may increase handwashing compliance because of their novelty, but they may also result in novel problems.

Cooperative Behavior↗
PubMed1981

Improvement in the persistence of microbial asparaginase and glutaminase in the circulation of the rat by chemical modifications.

Three enzymes used in cancer chemotherapy (asparaginases from Escherichia coli and Erwinia carotovora and glutaminase from Achromobacter) were each reacted with four amino specific reagents (ethyl acetimidate, O-methylisourea, succinic anhydride, and formaldehyde/sodium borohydride). The half-lives of the modified enzymes measured in the blood of rats showed that guanidation, acetimidation and reductive alkylation were more likely to increase the persistence of the native enzymes than succinylation. However, the improvement in the persistence of any one enzyme after any one modification could not be predicted from the results with the others. It was concluded that changes in persistence caused by each modification were due to the different effects on the tertiary structure of each native enzyme. The advantages of chemical modification for increasing the persistence of enzymes over other methods such as encapsulation or aggregation are discussed.

Alcaligenes↗
PubMed1989

Extracellular product of Nocardia amarae induces bacterial cell flocculation.

The fact that Nocardia amarae YK1 produced a bacterial flocculation-inducing substance (designated as FIX) was discovered. FIX had a function of flocculating proliferous cells. FIX-induced flocculation was inhibited by making cells resting, but not completely by adding chloramphenicol. FIX worked widely on Gram-positive to -negative bacteria. In the presence of FIX, Achromobacter cycloclastus IAM1013, Acinetobacter calcoaceticus IAM1517, Bacillus subtilis IAM1069, Escherichia coli C600-1, E. coli IAM1239, Flavobacterium lutescens IAM1667, Klebsiella pneumoniae IAM1102, Micrococcus luteus IAM1313 and Pseudomonas putida IAM1002 formed flocs. B. cereus IAM1029, however, exhibited no flocculation.

Agglutination↗
PubMed1996

A removable spacer peptide in an alpha-factor-leader/insulin precursor fusion protein improves processing and concomitant yield of the insulin precursor in Saccharomyces cerevisiae.

An alpha-factor leader/insulin precursor fusion protein was produced in Saccharomyces cerevisiae and metabolically labeled in order to analyse the efficiency of maturation and secretion. A substantial fraction of the secreted material was found in a hyperglycosylated unprocessed form, indicating incomplete Kex2p endopeptidase maturation. Introduction of a spacer peptide (EAEAEAK) after the dibasic Kex2p site, creating a N-terminal extension of the insulin precursor, greatly increased the Kex2p catalytic efficiency and the fermentation yield of insulin precursor. The N-terminal extension features a Lys to allow subsequent proteolytic removal by trypsin or the Achromobacter lyticus Lys-specific protease. Dipeptidyl aminopeptidase A (DPAPA) activity removing Glu-Ala dipeptides from the extension was inhibited by adding a Glu N-terminally to the extension. Unexpectedly, this modified N-terminal extension (EEAEAEAK) was partially cleaved after the Lys during fermentation. This monobasic proteolytic activity was demonstrated to be associated with Yap3p. Yap3p cleavage could be prevented by insertion of a Pro before the Lys (EEAEAEAPK).

Amino Acid Sequence↗
PubMed1985

Occurrence and antimicrobial susceptibility of gram-negative nonfermentative bacilli in cystic fibrosis patients.

Isolation of nonfermentative gram-negative bacilli (other than Pseudomonas aeruginosa) from respiratory tract cultures of cystic fibrosis (CF) patients has increased in recent years. Species recovered include Pseudomonas cepacia, P. maltophilia, P. fluorescens/putida, P. alcaligenes, P. pseudoalcaligenes, P. stutzeri, Acinetobacter spp., Achromobacter xylosoxidans, Flavobacterium spp., and CDC groups IVe and Ve. Although colonization with most of these organisms is sporadic, P. cepacia (and to a lesser extent, P. maltophilia) is usually isolated consistently, and can be associated with significant clinical deterioration. Occurrence of P. cepacia in CF respiratory tract cultures obtained close to the time of death rose nearly ten-fold from 1979 to 1982. Strains representing all nonfermentative gram-negative species encountered were assayed for susceptibility to 17 newer antimicrobial agents. Ceftazidime, n-formimidoyl thienamycin, and aztreonam were most active; cefsulodin, ceforanide, and ceftriaxone were not active against these isolates.

Adolescent↗
PubMedDate not supplied

Antimicrobial activity of Ro 24-6778, a covalent bonding of desmethylfleroxacin and desacetylcefotaxime.

A new "dual action" cephalosporin (Ro 24-6778), representing an ester-linked desacetylcefotaxime and desmethylfleroxacin was tested against 287 aerobic bacteria. Ro 24-6778 was found to be very active (minimal inhibitory concentrations [MIC90], less than or equal to 0.5 micrograms/ml) against Enterobacteriaceae, Streptococcus spp., and Aeromonas hydrophila. Moderate Ro 24-6778 activity (MIC90, 1-8 micrograms/ml) was demonstrated against Bacillus spp., Staphylococcus spp. (including oxacillin-resistant strains), Flavobacterium spp., Enterococcus durans, and Acinetobacter anitratus. More Ro 24-6778-resistant strains (MIC90, 16- greater than 32 micrograms/ml) were usually found among the enterococci, Xanthomonas hydrophila, Pseudomonas spp., and Achromobacter xyloxidans isolates. These preliminary Ro 24-6778 MIC test results show a spectrum superior (93.4% of strains susceptible at less than or equal to 8 micrograms/ml) to the comparison drugs (cefotaxime or fleroxacin) and possible clinical utility for therapy of many fluoroquinolone- or cephalosporin-resistant strains.

Anti-Bacterial Agents↗
PubMed1988

Identity of molecular structure of Shiga-like toxin I (VT1) from Escherichia coli O157:H7 with that of Shiga toxin.

The primary structures of the A and B subunits of Shiga toxin and of Shiga-like toxin I (VT1), isolated from the culture supernatants of Shigella dysenteriae 1 and Escherichia coli O157:H7, respectively, were analyzed by Edman degradation of intact proteins and peptides in their digests with trypsin or Achromobacter protease I and also by fast atom bombardment mass spectrometry of the digests. The results indicated that the A and B subunits of Shiga toxin and Shiga-like toxin I have the same primary structures. The identity of their primary structures was confirmed by determining the nucleotide sequence of the gene encoding Shiga-like toxin I cloned from a Shiga-like toxin I converting phage. This nucleotide sequence was different from that reported by Jackson et al. (Microbial Pathogenesis 1987; 2: 147-153), by Calderwood et al. (Proc Natl Acad Sci USA 1987; 84: 4364-8) and by Grandis et al. (J Bacteriol 1987; 169: 4313-9) in one base at position 231, which was found to be adenine instead of thymine, which they reported. The amino acid residue at position 45 from the N-terminus of the A subunit of Shiga-like toxin I deduced from the nucleotide sequence determined in this study is threonine, which corresponds with that found by amino acid sequencing, whereas from previous reports by other investigators it is serine. Edman degradation of the intact A subunit of Shiga toxin indicated that the A subunit was nicked between Ala253 and Ser254 to form A1 and A2 fragments linked by a disulfide bond.

Amino Acid Sequence↗
PubMed2006

Cleavage with phospholipase of the lipid anchor in the cell adhesion molecule, csA, from Dictyostelium discoideum.

A cell adhesion molecule, 80-kDa csA, is involved in EDTA-resistant cell contact at the aggregation stage of Dictyostelium discoideum. A 31-kDa csA was isolated from the 80-kDa csA by treatment with Achromobacter protease I. Results from thin-layer chromatography and MALDI-TOF MS analysis indicated that the 31-kDa csA contains ceramide as a component of glycosylphosphatidyl-inositol (GPI). Comparison between the 80-kDa csA and the 31-kDa csA treated with phosphatidylinositol-specific phospholipase C (PI-PLC) or GPI-specific phospholipase D (GPI-PLD) was carried out. Our results indicated that the GPI-anchor of the 31-kDa csA was more sensitive to PI-PLC treatment than that of the 80-kDa csA, and that the anchor in both was easily cleaved by GPI-PLD treatment. They suggested that the resistance of 80-kDa csA to PI-PLC treatment was due to steric hindrance and myo-inositol modification. The results of the 80-kDa csA and the 31-kDa csA treated with sphingomyelinase were similar to those with PI-PLC treatment. In the presence of 1,10-phenanthroline, a GPI-PLD inhibitor, development of Dictyostelium was markedly inhibited, suggesting that GPI-PLD is functional in developmental regulation through cell adhesion.

Animals↗
PubMed2006

Growth in Stewart's medium is a simple, rapid and inexpensive screening tool for the identification of Burkholderia cepacia complex.

Ninety-one percent of Burkholderia cepacia complex reference strains (66 out of 72) displayed a yellow slope-green butt colour reaction after growth in Stewart's medium indicating the oxidation of glucose and the absence of an arginine dihydrolase system. This same colour reaction was observed for Burkholderia gladioli and several Ralstonia species, but not for Pseudomonas aeruginosa, Stenotrophomonas, Achromobacter, Pandoraea and several other Gram-negative non-fermenting bacilli. We therefore consider growth in Stewart's medium a useful, simple, rapid and inexpensive screening test to reduce the number of false positive isolates from B. cepacia complex selective media.

Bacterial Typing Techniques↗
PubMed2005

Antibiotic resistance and antibacterial activity in heterotrophic bacteria of mineral water origin.

Antibiotic resistance and antibacterial activity were determined on heterotrophic bacteria isolated from mineral waters. Of the 120 isolates Pseudomonas spp. (55.8%) was the predominant group followed by Acinetobacter spp. (14.17%), Flavobacterium spp. (10.83%), Achromobacter spp. (10%), Burkholderia cepacia (3.3%), Agrobacterium/radiobacter (2.5%), Moraxella spp. (1.7%), Aeromonas hydrophila (1.7%). Over 80% of the isolates were resistant to one or more antibiotics and the highest resistance was found for chloramphenicol, ampicillin, colistin and sulfamethizole (60%, 55%, 50% and 47.5%, respectively). Strains with multiple antibiotic resistance (MAR) represented 55% of isolates and the most resistant organism belonged to the genus Pseudomonas. Of 40 randomly selected strains, 27 (67.5%) had antibacterial activity towards one or more indicators. This activity, found in a high percentage in the genus Pseudomonas (92%), emerged mainly against closely related microorganisms. Several producers were active also against Escherichia coli, Salmonella, Listeria monocytogenes and Staphylococcus aureus. Forty-six percent of the isolates harboured 1 to 5 plasmids with molecular weights ranging from 2.1 to 41.5 MDa.

Anti-Bacterial Agents↗
PubMed2006

Analysis of denitrification genes and comparison of nosZ, cnorB and 16S rDNA from culturable denitrifying bacteria in potato cropping systems.

Bacterial denitrification in agricultural soils is a major source of nitrous oxide, a potent greenhouse gas. This study examined the culturable bacterial population of denitrifiers in arable field soils in potato (Solanum tuberosum L.) production and denitrification genes (nir, nor and nos) and 16S rDNA in those isolates. Enrichments for culturable denitrifiers yielded 31 diverse isolates that were then analysed for denitrification genes. The nitrous oxide reductase (nosZ) gene was found in all isolates. The majority of isolates ( approximately 90%) contained the cnorB nitric oxide reductase gene, with the remainder containing the qnorB gene. Nitrite reductase genes (nirS and nirK) were amplifiable from most of the isolates, and were segregated between species similar to previously isolated denitrifiers. Isolated strains were preliminarily identified using fatty acid methyl ester analysis and further identified using 16S rDNA sequencing. The majority of isolates (21) were classified as Pseudomonas sp., with smaller groups of isolates being most similar to Bosea spp. (4), Achromobacter spp. (4) and two isolates closely related to Sinorhizobium/Ensifer spp. Phylogenetic trees were compared among nosZ, cnorB and 16S rDNA genes for a subset of Pseudomonas strains. The trees were mostly congruent, but some Pseudomonas sp. isolates grouped differently depending on the gene analysed, indicating potential horizontal gene transfer of denitrification genes. Although Bosea spp. are known denitrifiers, to the best of our knowledge this is the first report of isolation and sequencing of denitrification genes from this bacterial genus.

Bacteria↗