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PubMed1997

Cell-surface hydrophobicity and scum formation of Rhodococcus rhodochrous strains with different colonial morphologies.

Rhodococcus rhodochrous has been reported to be one of the micro-organisms responsible for the formation of scum which is thick and viscous biological foam in activated sludge plants. The hydrophobicity of mycolic acids present on the cell surface and the long-branched shape of the hyphae have been thought to contribute to the scum formation. Cell surface hydrophobicity and scum formation of four R. rhodochrous strains with different colony morphologies were determined, and the results showed that the two rough strains had strong cell surface hydrophobicity and produced scum, whereas the weakly hydrophobic smooth strain and the hydrophilic mucoidal strain did not. All four strains displayed long, branched hyphae, and their electrophoretic mobilities were similar, between pH 4 and 9. These data suggest that changes in the cell surface hydrophobicity of the R. rhodochrous result in changes in the culture characteristics and the formation of scum.

Bacterial Adhesion↗
PubMed2005

Atrazine degradation by encapsulated Rhodococcus erythropolis NI86/21.

AIMS: To develop an encapsulation procedure for Rhodococcus erythropolis NI86/21 and demonstrate its use as a slow-release inoculant for reducing atrazine levels in aquatic and terrestrial environments. METHODS AND RESULTS: Alginate encapsulation procedures were developed for the atrazine-degrading bacteria R. erythropolis NI86/21. Several bead amendments, including bentonite, powdered activated carbon (PAC) and skimmed milk (SM), were evaluated for slow release of R. erythropolis NI86/21 and efficacy of atrazine degradation. All bead types demonstrated a capacity to degrade atrazine in basal minimal nutrient buffer whilst continually releasing viable bacterial cells. We found that the addition of bentonite hastened cell release whilst SM sustained cell viability in bead formulations. Reducing the percentage of SM to 1% (w/v) resulted in faster rates of atrazine degradation in both liquid and soil, and was found to prolong cell survival upon bead storage. Limited oxygen transfer affects the capacity of the encapsulated R. erythropolis cells to degrade atrazine. CONCLUSIONS: Degradation studies have demonstrated the efficacy of R. erythropolis encapsulated cells to degrade atrazine in amended liquid and soil. However, in their current formulation, the wet alginate-based beads are impractical for field application because of their poor cell viability during storage. SIGNIFICANCE AND IMPACT OF THE STUDY: R. erythropolis NI86/21-encapsulated cells have the potential to reduce atrazine residues in a number of soil and water environments, possibly ensuring the continued registration and use of atrazine in agriculture by minimizing or eliminating nontarget effects.

Alginates↗
PubMed2007

Enhancing cell survival of atrazine degrading Rhodococcus erythropolis NI86/21 cells encapsulated in alginate beads.

AIMS: To develop a method to produce beads with encapsulated Rhodococcus erythropolis NI86/21 with high cell density, extended shelf life, ease of handling and good atrazine degradation capabilities in both liquid and in agricultural soil. METHODS AND RESULTS: Our findings show that the supplementary recovery step in nutrient broth media shortly after cell encapsulation facilitates cell survival in both wet and dry beads upon extended storage at 4 degrees C. Air drying has little or no impact on encapsulated R. erythropolis cell's ability to degrade atrazine in liquid or soil. Bead storage for periods extending up to 12 months at 4 degrees C did not affect the capacity of R. erythropolis encapsulated cells to degrade atrazine in either BMN or nonsterile soil extracts. Bentonite-amended beads formulated with 1% skim milk and exposed to the supplementary growth step, outperformed all other bead formats. These beads provided adequate numbers of vigorous R. erythropolis cells in either liquid or soil media to degrade atrazine. CONCLUSIONS: Supplementary growth in nutrient broth media immediately following cell encapsulation greatly enhances R. erythropolis cells survival in both wet and dry beads upon extended storage at 4 degrees C. Wet and dried beads have similar capacity for atrazine degradation, and their usefulness and appeal in agronomic practise will only be known after bioassay evaluation and successful demonstration at field scale using incurred residues. SIGNIFICANCE AND IMPACT OF THE STUDY: R. erythropolis NI86/21 encapsulated cells have the potential to reduce residual atrazine in soil, thereby minimizing the likelihood of off-site transport to ground or river water and reduce the loss of crops because of phytotoxicity of residual herbicide. Owing to their ease of handling, storage and possible compatibilities with pre-existing mechanical equipment, dried bead formats are ideally suited for agricultural and remediational applications.

Alginates↗
PubMed2006

Pulmonary disposition of tilmicosin in foals and in vitro activity against Rhodococcus equi and other common equine bacterial pathogens.

The objectives of this study were to determine the serum and pulmonary disposition of tilmicosin in foals and to investigate the in vitro activity of the drug against Rhodococcus equi and other common bacterial pathogens of horses. A single dose of a new fatty acid salt formulation of tilmicosin (10 mg/kg of body weight) was administered to seven healthy 5- to 8-week-old foals by the intramuscular route. Concentrations of tilmicosin were measured in serum, lung tissue, pulmonary epithelial lining fluid (PELF), bronchoalveolar lavage (BAL) cells, and blood neutrophils. Mean peak tilmicosin concentrations were significantly different between sampling sites with highest concentrations measured in blood neutrophils (66.01+/-15.97 microg/mL) followed by BAL cells (20.1+/-5.1 microg/mL), PELF (2.91+/-1.15 microg/mL), lung tissue (1.90+/-0.65 microg/mL), and serum (0.19+/-0.09 microg/mL). Harmonic mean terminal half-life in lung tissue (193.3 h) was significantly longer than that of PELF (73.3 h), bronchoalveolar cells (62.2 h), neutrophils (47.9 h), and serum (18.4 h). The MIC90 of 56 R. equi isolates was 32 microg/mL. Tilmicosin was active in vitro against most streptococci, Staphylococcus spp., Actinobacillus spp., and Pasteurella spp. The drug was not active against Enterococcus spp., Pseudomonas spp., and Enterobacteriaceae.

Animals↗
PubMed1991

Illegitimate integration of non-replicative vectors in the genome of Rhodococcus fascians upon electrotransformation as an insertional mutagenesis system.

Electrotransformation of Rhodococcus fascians by non-replicating plasmids containing a suitable resistance marker resulted in stable transformants by integration of these constructs at various sites in the genome, thereby generating different mutations. Tagged genes could be isolated in Escherichia coli owing to the presence of a CoIE1 replicon and an ampicillin resistance gene in the inserted sequences. Southern analysis and nucleotide sequencing revealed that recombination can occur at defined locations in the plasmid, while no site preference for target sequences could be detected. Low homology between the recombining sequences indicates illegitimate recombination. The specificity of the plasmid sites could be explained by assuming a linear recombination intermediate, generated by cleavage of the transformed plasmid.

Base Sequence↗
PubMed1992

The plasmid-encoded chloramphenicol-resistance protein of Rhodococcus fascians is homologous to the transmembrane tetracycline efflux proteins.

The nucleotide sequence of the chloramphenicol-resistance gene (cmr) of Rhodococcus fascians NCPPB 1675 (located on the conjugative plasmid pRF2) allowed the identification of two possible open reading frames (ORFs), of which ORF1 was consistent with the mutational analysis. Biochemical analysis of cmr revealed that it does not encode an antibiotic-modifying enzyme. The amino acid sequence of ORF1 predicted a hydrophobic protein, with 12 putative membrane-spanning domains, homologous to proteins involved in the efflux of tetracycline across the plasma membrane. Expression of the cmr gene was induced by addition of chloramphenicol to the growth media. The promoter of this gene was restricted to 50 bp upstream from a 200 bp 5'-untranslated mRNA region, the latter containing two inverted repeats. At the amino acid level, the cmr gene is 52% identical to a previously identified chloramphenicol-resistance determinant in Streptomyces lividans, indicating a wider dispersion of this type of cmr gene among the actinomycetes.

Amino Acid Sequence↗
PubMed1989

Primary structure of nitrile hydratase deduced from the nucleotide sequence of a Rhodococcus species and its expression in Escherichia coli.

The nitrile hydratase (NHase) of Rhodococcus species N-774, which is composed of two subunits, alpha and beta, catalyzes the hydration of various nitrile compounds to the corresponding amides. The amino acid sequences of the NH2 termini and the fragments obtained by digesting each of the two subunits with lysyl endopeptidase were determined for preparation of synthetic oligonucleotides as hybridization probes. A 4.4-kb SphI fragment which contained DNA sequences hybridizing to several of the probes was cloned in pBR322 in Escherichia coli. The nucleotide sequences together with the determined amino acid sequences indicated that the alpha and beta subunits of NHase consisted of 207 amino acids (Mr, 22918) and 212 amino acids (Mr, 23428), respectively. The open reading frame for the alpha subunit includes that for the beta subunit with a short interval of only 26 base pairs; the two genes are probably translated in a polycistronic manner. Although large amounts of the alpha- and beta-subunit proteins were produced as insoluble forms in E. coli when the cloned genes were placed under the control of the lac promoter, no enzymatic activity was detected. The activity of the enzyme was restored, to some extent, by solubilization of the proteins with 8 M urea and subsequent dialysis for refolding at pH 10 in the presence of Fe2+ and pyrroloquinoline quinone.

Amino Acid Sequence↗
PubMed1989

Nitrilase of Rhodococcus rhodochrous J1. Purification and characterization.

Nitrilase was purified from an extract of isovaleronitrile-induced cells of Rhodococcus rhodochrous J1 in seven steps. In the last step, the enzyme was crystallized by adding ammonium sulfate. The crystallized enzyme appeared to be homogeneous by polyacrylamide electrophoresis, ampholyte electrofocusing and double immunodiffusion in agarose. The enzyme has a molecular mass of about 78 kDa and consists of two subunits identical in molecular mass. The purified enzyme exhibits a pH optimum of 7.6 and a temperature optimum of 45 degrees C. The enzyme catalyzed stoichiometrically the hydrolysis of benzonitrile to benzoic acid and ammonia, and no formation of amide was detected. The enzyme required thiol compounds such as dithiothreitol, L-cysteine or reduced glutathione to exhibit maximum activity. The enzyme was specific for nitrile groups attached to an aromatic or heteroaromatic ring, e.g. benzonitrile, 3-chlorobenzonitrile, 4-tolunitrile, 2-furonitrile and 2-thiophenecarbonitrile. The comparison of the properties of the enzyme with other nitrilases and nitrile hydratases has been also discussed.

Amino Acids↗
PubMed1991

Characterization of a new cobalt-containing nitrile hydratase purified from urea-induced cells of Rhodococcus rhodochrous J1.

A new cobalt-containing nitrile hydratase was purified from extracts of urea-induced cells from Rhodococcus rhodochrous J1 in seven steps. At the last step, the enzyme was crystallized by adding ammonium sulfate. Nitrile hydratase was a 500-530-kDa protein composed of two different subunits (alpha subunit 26 kDa, beta subunit 29 kDa). The enzyme contained approximately 11-12 mol cobalt/mol enzyme. A concentrated solution of highly purified nitrile hydratase exhibited a broad absorption spectrum in the visible range, with an absorption maxima at 410 nm. The enzyme had a wide substrate specificity. Aliphatic saturated or unsaturated nitriles as well as aromatic nitriles, were substrates for the enzyme. The optimum pH of the hydratase was pH 6.5-6.8. The enzyme was more stable than ferric nitrile hydratases. The amino-terminal sequence of each subunit of R. rhodochrous J1 enzyme was determined and compared with that of ferric nitrile hydratases. Prominent similarities were observed with the beta subunit. However, the amino acid sequence of the alpha subunit from R. rhodochrous J1 was quite different from that of the ferric enzymes.

Amino Acid Sequence↗
PubMed1993

Purification and characterization of cytochrome P450RR1 from Rhodococcus rhodochrous.

A soluble cytochrome P450 whose synthesis is induced by and that binds 2-ethoxyphenol was purified to apparent homogeneity from Rhodococcus rhodochrous strain 116. The enzyme had a subunit molecular mass of 44.5 kDa as determined by SDS/PAGE and a pI of 5.2. The electronic absorption spectrum indicates that the native cytochrome in the absence of substrate is predominantly in the low-spin state (13% high-spin state in 50 mM Mops, pH 7.0 25 degrees C). 2-Methoxyphenol binds to the cytochrome with a macroscopic dissociation constant of 0.53 +/- 0.03 microM (50 mM Mops, pH 7.0, 25 degrees C) and induces a 99.7% transition of the heme iron to the pentacoordinate high-spin form. Using a reconstituted in-vitro activity assay, it was demonstrated that P450RR1 catalyzed the O-dealkylation of 2-ethoxyphenol and 2-methoxyphenol to produce catechol. The cytochrome binds other ortho-substituted phenols, including 2-ethoxyphenol, 2-methylphenol (o-cresol) and 2-chlorophenol. The affinity of P450RR1 for these compounds is lower than that of 2-methoxyphenol and they are less effective than 2-methoxyphenol at inducing a transition in the heme iron to the high-spin state. Para-substituted and meta-substituted ether phenols did not induce a spin transition.

Amino Acid Sequence↗
PubMed1991

Typing of Rhodococcus equi isolated from submaxillary lymph nodes of pigs in Japan.

Isolation of Rhodococcus equi from the submaxillary lymph nodes of pigs, with or without caseous lymphadenitis, and typing of the isolates by two serological methods were carried out. The rate of isolation of the organisms from the lymph nodes of pigs was 5 times higher in the lymph nodes with caseous lymphadenitis than in those without the lesion. Of 219 isolates, 146 (66.7%) were typable by the method of Prescott, while all the 219 isolates (100%) were typable by the method of Nakazawa et al. The most frequently isolated were serotype 2 of Prescott (identical to serogroup 16 of Nakazawa et al.), and serogroup 3 of Nakazawa et al., which did not correspond with any serotypes of Prescott. Serotypes/serogroups of R. equi from pigs were thus first clarified in Japan.

Actinomycetales Infections↗
PubMed1991

Selective medium containing fosfomycin, nalidixic acid, and culture supernatant of Rhodococcus equi for isolation of Corynebacterium pseudotuberculosis.

FNR medium containing fosfomycin, nalidixic acid, bovine blood and culture supernatant of Rhodococcus equi was prepared by the present authors, and the medium did not inhibit growth of Corynebacterium pseudotuberculosis but completely hampered the growth of Bacillus subtilis, Staphylococcus aureus, and Escherichia coli. The culture supernatant of R. equi facilitated detection of suspected colonies of C. pseudotuberculosis due to synergistic hemolysis. Rate of isolation of the organisms (from the trachea, larynx and nasal cavity of 16 slaughtered sheep with caseous abscess in the lung) was higher with FNR, the selective medium, than with nonselective medium. The selective medium was thus found to be useful for isolation of C. pseudotuberculosis from sheep.

Animals↗
PubMed1994

Biochemical and serological characteristics of Rhodococcus equi isolates from animals and humans.

In the present study, 17 Rhodococcus equi isolates from animals and 13 R. equi isolates from humans were correctly identified by the use of the API Coryne-test system. The biochemical characteristics revealed no significant differences between isolates from animals and humans. Heat extractions at acid pH or autoclave extractions of the bacteria and the use of monospecific antisera against type antigens 1-7 allowed the serotyping of the bacteria. The majority of the R. equi isolates reacted with serotype 1 and serotype 2-specific antisera, extracts of two human isolates reacted with serotype 5 and serotype 6-specific antisera, respectively. The determination of biochemical and serological properties of R. equi might help to characterize individual cultures of this species. This might be useful in epidemiological studies.

Actinomycetales Infections↗
PubMed1996

Blastogenic response of lymphocytes from foals infected with Rhodococcus equi.

The blastogenic response of lymphocytes from 16 newborn foals naturally infected with Rhodococcus equi was investigated, in order to evaluate the relationship between R. equi infection and depressed host response. Naturally infected foals showed evidence of R. equi infection at 5-6 weeks of age, as determined by clinical, haematological, bacteriological and serological methods. The blastogenic response of lymphocytes against phytohaemagglutinin was significantly depressed (stimulation index < 1.80; P < 0.01, P < 0.05) in R. equi-infected foals at 5-6 weeks of age compared with those of control foals. Serum IgG concentration decreased rapidly after foals reached 1 week of age, and minimum levels of IgG were observed at 5-7 weeks of age in R. equi-infected foals. This study suggests that the onset of R. equi infection may be associated with the depressed immune function of naturally infected foals during the first 5-6 weeks after birth.

Actinomycetales Infections↗
PubMed1996

Relationship between haemagglutination and HeLa-cell adherence of Rhodococcus equi.

In this study, 45 Rhodococcus equi isolates from animals and humans were identified by the Api Coryne system, and serologically with monospecific antisera against capsular types 1-7, with serotypes 1 and 2 predominating. Regardless of serotype, 14 out of 31 isolates from animals and one of 14 isolates from humans expressed 15-17-kD virulence-associated proteins. In hexadecane adherence studies, serotype 2 isolates generally displayed hydrophobic surfaces. In addition, isolates of serotype 1 generally haemagglutinated erythrocytes from rabbits. Neither property appeared to be related to the occurrence of the virulence-associated proteins. By contrast, the haemagglutination reaction correlated significantly with the adherence of the bacteria to HeLa cells. This adhesion might serve as additional marker of virulence among isolates of R. equi and might be useful in epidemiological studies.

Alkanes↗
PubMed1997

Studies on the rod-coccus life cycle of Rhodococcus equi.

In the present study all 19 Rhodococcus equi cultures isolated from horses and 19 of 22 R. equi cultures isolated from human patients displayed a rod-coccus life cycle after cultivation under defined growth conditions. A bacillary growth could be observed after cultivation of the bacteria in fluid media for 4 h at 37 degrees C, a coccoid morphology after cultivation of the bacteria for 24 h either on sheep blood agar plates or in fluid media. The different morphological features did not significantly influence the typability of the bacteria or the expression of surface proteins including 15-17 kDa virulence proteins. Studies on further surface characteristics revealed a relation between haemagglutinating properties, the surface hydrophobicity and adherence properties of the bacteria to HeLa cells. These properties seemed to be influenced by the cultivation conditions but not by the different morphological forms of the bacteria. A haemagglutination reaction, a hydrophobic surface and an enhanced adherence to HeLa cells could be observed with coccoid bacteria after cultivation in fluid media for 24 h at 37 degrees C but not with coccoid bacteria harvested from sheep blood agar plates or with bacillary bacteria after 4 h growth in fluid media. This difference might possibly be caused by the degree of encapsulation of the bacteria after various cultivation conditions and a subsequent masking effect of the hydrophilic polysaccharide capsule of R. equi.

AIDS-Related Opportunistic Infections↗
PubMed2005

Recognition of a B-cell epitope of the VapA protein of Rhodococcus equi in newborn and experimentally infected foals.

The aim of this study was to evaluate the usefulness of the previously identified B-cell epitope TSLNLQKDEPNGRASDTAGQ of the VapA protein of Rhodococcus equi and its association with R. equi pneumonia. A modified peptide designated PN11-14 corresponding to the epitope was recognized by all sera from experimentally infected foals with virulent R. equi ATCC103+ containing the virulence plasmid but not by its plasmid-cured derivative ATCC103- strain. Marked levels of VapA-specific immunoglobulin (Ig)G were detected in all sera from the ATCC103+ infected foals at 2 weeks after the infection. One control animal had high titres as determined by the peptide enzyme-linked immunosorbent assay (ELISA), indicating the ELISA may not absolutely differentiate between foals with R. equi pneumonia and healthy exposed foals in farms where the prevalence of disease is high. However, numbers of animals used were small. Further evaluation of the peptide ELISA with field samples is necessary to determine whether the assay is diagnostically useful. This study showed that levels of passive transfer of maternal IgG antibodies to the epitope in newborn foals could be measured. Interestingly, the maternally derived antibodies were found to significantly (P<0.05 by Student's t-test) decline 2 weeks after birth. Seroconversion against naturally occurring VapA expressing R. equi could be detected in some foals at 4 weeks of age. Antibodies to the epitope peaked and were significantly (P<0.05) greater in foals aged between 6 and 8 weeks. These results indicated that the peptide ELISA could be used to monitor anti-VapA antibodies in foals, particularly those at the age of 4-6 weeks. It is possible that the ELISA may be of some use as a diagnostic test on farms where R. equi is non-endemic. Further studies using large number of field samples are needed to verify this assumption.

Actinomycetales Infections↗