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PubMed1991

[Identification of Mycobacterium avium, Mycobacterium intracellulare, and Mycobacterium tuberculosis complex by Gen-Probe Rapid Diagnostic System].

DNA probe testing for Mycobacterium avium, Mycobacterium intracellulare and Mycobacterium tuberculosis complex (MTC) was performed using Gen-Probe Rapid Diagnostic System (Gen-Probe Inc., San Diego, Calif., U.S.A.). By DNA probe test carried out blindfold for 48 mycobacterial strains with code numbers obtained from Kyoto University (Prof. F. Kuze), 13, 7, and 5 strains were identified as to be M. avium, M. intracellulare, and MTC, respectively. The diagnostic specificity and sensitivity of this testing were 100%. In this experiment, % hybridization of M. avium complex (MAC) and MTC were 25-55% and 45-52%, respectively. DNA probe test for 54 MTC strains including M. tuberculosis, M. bovis, M. africanum and M. microti revealed that 53 strains, except for one strain donated as a niacin-negative M. tuberculosis, reacted with MTC probe but not with MAC-probes. The one exceptional strain reacted with both the MTC- and M. avium-probes. However, when ten colonies randomly isolated from this strain on 7H11 agar plate were subjected to the DNA probe test again, all of these colonies reacted with M. avium probe, but not with MTC probe. Moreover, one representative colony was found to have alpha-antigen specific for the MAC.

DNA Probes↗
PubMed2000

Activity of rifapentine and its metabolite 25-O-desacetylrifapentine compared with rifampicin and rifabutin against Mycobacterium tuberculosis, Mycobacterium africanum, Mycobacterium bovis and M. bovis BCG.

The in vitro activity of rifapentine and its metabolite, 25-O:-desacetylrifapentine, as compared with that of rifampicin and rifabutin, was determined against Mycobacterium tuberculosis, Mycobacterium africanum, Mycobacterium bovis and M. bovis BCG. MICs were determined radiometrically and by the 1% proportional method using Middlebrook 7H11 agar. The bactericidal effect of the drugs was determined in parallel at selected concentrations. For drugsusceptible isolates of M. tuberculosis, the Bactec MICs of rifapentine and 25-O:-desacetylrifapentine were 0.03-0.06 mg/L and 0. 125-0.25 mg/L, respectively. Similar MICs were obtained for M. africanum (0.03-0.125 and 0.125-0.50 mg/L, respectively), and M. bovis (0.063-0.25 and 0.125-1.0 mg/L, respectively), but MICs were considerably lower for M. bovis BCG (0.008-0.063 mg/L for rifapentine and 0.016-0.125 mg/L for its metabolite). In general, MICs determined using 7H11 agar medium were usually one or two dilutions higher than those obtained using Bactec broth. When compared with rifampicin and rifabutin, the inhibitory activity of rifapentine for drug-susceptible isolates was roughly equal to that of rifabutin, and the inhibitory activity of 25-O:-desacetylrifapentine was comparable to that of rifampicin; however, rifapentine was somewhat more bactericidal than rifabutin at equal concentrations. Clinical isolates of M. tuberculosis with a high degree of resistance to rifampicin (MIC >/= 32 mg/L) were also highly resistant to rifabutin, rifapentine and 25-O:-desacetylrifapentine, although the MICs of rifabutin in this case were somewhat lower than the MICs of rifapentine.

Animals↗
PubMed1994

Structures of the glycopeptidolipid antigens of Mycobacterium abscessus and Mycobacterium chelonae and possible chemical basis of the serological cross-reactions in the Mycobacterium fortuitum complex.

Mycobacterium abscessus and Mycobacterium chelonae, two members of the Mycobacterium fortuitum complex, contain five major glycolipids. A combination of NMR spectroscopy, fast atom bombardment mass spectrometry and chemical degradation was used to elucidate their structures. All the compounds belong to the family of glycopeptidolipids. A 6-deoxy-alpha-L-talosyl unit, which may bear one or two acetyl groups, invariably occupies the site of glycosylation on the threonine residue in the various compounds. A 3,4-di-O-methyl- or 2,3,4-tri-O-methyl-alpha-L-rhamnosyl unit modifies the alaninol end of the diglycosylated molecules. Both species also contain a multiglycosylated compound consisting of alpha-L-rhamnosyl-(1-->2)-3,4-di-O-methyl-alpha-L-rhamnosyl linked to alaninol, which belongs to the class of new variants of glycopeptidolipids recently described. Using an ELISA, the latter glycolipid as well as the diglycosylated ones (not previously reported to be antigenic), were shown to react with the serum raised against the whole lipid antigens of M. chelonae. A comparative serologic study of the native and chemically modified glycopeptidolipid antigens allowed the identification of their epitope as the 3,4-di-O-methyl-alpha-L-rhamnosyl residue. Similar experiments conducted on the glycopeptidolipids isolated from the serologically cross-reacting species M. peregrinum led to the conclusion that the epitope identified in M. chelonae and M. abscessus was involved in the cross-reactions and demonstrated the existence of a second haptenic moiety in the glycolipids of M. peregrinum, the 3-O-methyl-alpha-L-rhamnosyl unit. In addition to this latter non-shared epitope, the recently described sulfated glycopeptidolipid antigen of M. peregrinum did not react with the M. chelonae serum, thus further explaining the difference in the seroreactivity within the complex.

Amino Acid Sequence↗
PubMed1987

Intrinsic catalase dot blot immunoassay for identification of Mycobacterium tuberculosis, Mycobacterium avium, and Mycobacterium intracellulare.

The heat-labile T class of mycobacterial catalase exhibits peroxidase activity with some substrates. Most species of mycobacteria produce T-catalase, which is serologically characterized by a combination of shared epitopes and unique, species-specific epitopes. Antibodies to T-catalases from Mycobacterium tuberculosis, Mycobacterium avium, and Mycobacterium intracellulare have been cross absorbed with T-catalases from heterologous species and applied as dots to nitrocellulose membranes. When these membranes were incubated with crude sonic extracts of 93 strains of mycobacteria that produce sufficient T-catalase, and were then exposed to 3,3'-diaminobenzidine peroxidase substrate, only those extracts made from one of the three species represented yielded a discrete brown dot at the site of the corresponding globulin. The sensitivity of the test was at least 96.5%, and the specificity was in excess of 99.5%.

Catalase↗
PubMed1992

Separation of Mycobacterium bovis BCG from Mycobacterium tuberculosis and Mycobacterium bovis by using high-performance liquid chromatography of mycolic acids.

Profile analysis of mycolic acid ester patterns of Mycobacterium tuberculosis, Mycobacterium bovis, and Mycobacterium bovis bacillus Calmette-Gúerin (BCG) using high-performance liquid chromatography indicated that separation of BCG from M. tuberculosis and M. bovis by elution and relative retention times is possible. Mycolic acid patterns of BCG eluted from the column 0.5 min before M. tuberculosis or M. bovis, resulting in relative retention times for two peaks not seen in the pattern of M. tuberculosis or M. bovis. Identification was confirmed by phage typing, which has been the standard procedure for confirmation of BCG strains. These results showed that high-performance liquid chromatographic analysis of mycolic acid esters can be used in the mycobacterial reference laboratory for separation of BCG from M. tuberculosis and M. bovis.

Bacteriophage Typing↗
PubMed2002

Characterization of an unusual Mycobacterium: a possible missing link between Mycobacterium marinum and Mycobacterium ulcerans.

In an attempt to characterize an unusual mycobacterial isolate from a 44-year-old patient living in France, we applied phenotypic characterizations and various previously described molecular methods for the taxonomic classification of mycobacteria. The results of the investigations were compared to those obtained in a previous study with a set of temporally and geographically diverse Mycobacterium ulcerans (n = 29) and Mycobacterium marinum (n = 29) isolates (K. Chemlal, G. Huys, P.-A. Fonteyne, V. Vincent, A. G. Lopez, L. Rigouts, J. Swings, W. M. Meyers, and F. Portaels, J. Clin. Microbiol. 39:3272-3278, 2001). The isolate, designated ITM 00-1026 (IPP 2000-372), is closely related to M. marinum according to its phenotypic properties, lipid pattern, and partial 16S rRNA sequence. Moreover, fingerprinting by amplified fragment length polymorphism (AFLP) analysis unequivocally classified this strain as a member of the species M. marinum, although it lacked two species-specific AFLP marker bands. However, PCR and restriction fragment length polymorphism analysis based on M. ulcerans-specific insertion sequence IS2404 showed the presence of this element in a low copy number in isolate ITM 00-1026. In conclusion, the designation of this isolate as a transitional species further supports the recent claim by Stinear et al. (T. Stinear, G. Jenkin, P. D. Johnson, and J. K. Davies, J. Bacteriol. 182:6322-6330, 2000) that M. ulcerans represents a relatively recent phylogenetic derivative of M. marinum resulting from the systematic acquisition of foreign DNA fragments.

Adult↗
PubMed1985

Equivalence of mycobactins from Mycobacterium senegalense, Mycobacterium farcinogenes and Mycobacterium fortuitum.

Mycobactins were isolated from five strains designated Mycobacterium farcinogenes and a similar number designated Mycobacterium senegalense following growth under conditions of iron-limitation. These lipid-soluble iron-chelating compounds were characterized by a combination of thin-layer and high-performance liquid chromatography. The mycobactins from both the slow-growing M. farcinogenes and the rapidly-growing M. senegalense strains proved impossible to differentiate both from each other and from those produced by strains of Mycobacterium fortuitum, indicating a close relationship between all three species. However, Nocardia farcinica, previously implicated with the bovine farcy strains, produced a different mycobactin which was easily distinguished by thin-layer chromatography alone.

Chromatography, High Pressure Liquid↗
PubMed1990

High-performance liquid chromatography patterns of mycolic acids as criteria for identification of Mycobacterium chelonae, Mycobacterium fortuitum, and Mycobacterium smegmatis.

Rapidly growing mycobacteria of clinical significance were identified by mycolic acids detected with high-performance liquid chromatography. Mycolic acids from whole cells were extracted, derivatized, and detected by a modified high-performance liquid chromatography procedure in less than 3 h. Use of an internal standard allowed differentiation of Mycobacterium chelonae and Mycobacterium fortuitum by comparison of relative retention times. Peak height ratios were used for subidentification of M. chelonae strains; however, M. fortuitum and Mycobacterium smegmatis could not be separated by this system.

Chromatography, High Pressure Liquid↗
PubMed1979

Phagosome-lysosome fusion and cyclic adenosine 3':5'-monophosphate in macrophages infected with Mycobacterium microti, Mycobacterium bovis BCG or Mycobacterium lepraemurium.

When ingested by mouse peritoneal macrophage monolayers, live Mycobacterium microti caused a sustained increase in monolayer cyclic AMP content and fusion of lysosomes with the bacterium-containing phagosomes was impaired. Ingested live M. bovis BCG caused a transient increase in cyclic AMP and the defect in phagolysosome formation was less pronounced. Dead mycobacteria and live M. lepraemurium neither enhanced monolayer cyclic AMP content nor inhibited phagolysosome formation. Mycobacterium microti and BCG exceeded M. lepraemurium in cyclic AMP-synthesizing activity in vitro but the question of whether bacterial cyclic AMP contributed substantially to the increments in infected macrophages was not resolved. Antibody-coated BCG retained the ability to synthesize cyclic AMP and to enhance monolayer cyclic AMP but lost the ability to inhibit phagolysosome formation in macrophages, The observations are discussed in terms of possible control of phagolysosome formation by cyclic nucleotides.

Cyclic AMP↗
PubMed1991

Gen-Probe Rapid Diagnostic System for the Mycobacterium avium complex does not distinguish between Mycobacterium avium and Mycobacterium paratuberculosis.

Three reference and 16 field strains of Mycobacterium paratuberculosis were tested with the Gen-Probe Mycobacterium avium complex DNA probe (Gen-Probe Inc., San Diego, Calif.). All reference strains and 12 of 16 field strains gave positive hybridization results with the probe. This study shows that the M. avium complex probe does not distinguish between M. avium and M. paratuberculosis and indicates heterogeneity in the 16S rRNA gene of M. paratuberculosis.

Animals↗
PubMed2002

Biochemical and genetic evidence for the transfer of Mycobacterium tuberculosis subsp. caprae Aranaz et al. 1999 to the species Mycobacterium bovis Karlson and Lessel 1970 (approved lists 1980) as Mycobacterium bovis subsp. caprae comb. nov.

We propose to replace the species designation Mycobacterium tuberculosis subsp. caprae (Aranaz et al. 1999) by Mycobacterium bovis subsp. caprae comb. nov., since isolates of this subspecies share their main growth, biochemical and genetic characteristics with M. bovis and not with M. tuberculosis. These include negative biochemical test results for niacin accumulation and nitrate reduction as well as genetic features like the presence of an M. bovis-specific mutation in the oxyR locus, absence of the mtp40 sequence and a specific mutation in the gyrB gene, all of which have been described as characteristics for the differentiation of M. bovis. The only obvious biochemical character that differentiates the caprae subtype from other M. bovis isolates is susceptibility to pyrazinamide (PZA), which is due to the lack of a single point mutation in the pncA gene. However, susceptibility to PZA among clinical isolates of M. bovis isolates has been reported previously and, thus, may now been explained by a PZA-susceptible subspecies of M. bovis. We conclude that the species designation M. tuberculosis subsp. caprae is misleading and not correct in light of the biochemical and genetic characteristics and propose that the accurate designation of isolates of this subtype is M. bovis subsp. caprae.

Amidohydrolases↗
PubMed1978

Ocular histopathology in animals experimentally infected with Mycobacterium leprae and M. lepraemurium. 1. Mycobacterium leprae and M. lepraemurium infections in the mouse. 2. Mycobacterium leprae infections in the 9-banded armadillo (Dasypus novemcinctus L.).

At varying periods of time following the successful establishment of systemic infections with Mycobacterium leprae or M. lepraemurium in the mouse and the nine-banded armadillo eyes were examined by light microscopy. Inoculation of bacilli was by the intravenous or intraperitoneal route or directly into the hind footpads; eyes were not directly inoculated in this study. During periods of up to 3 years under laboratory conditions no animal showed evidence of impaired vision or blindness, and the external appearance of both eyes was normal. The ocular histopathology and the sites of accumulation of bacilli are described. In immunologically normal mice infected with M. lepraemurium bacilli were much commoner in extraorbital tissues, but they were, nevertheless, found in various tissues within the orbit, including the ciliary body and sclera. In immunologically normal mice (and one rat) injected with M. leprae of human origin no bacilli were found in the eye, but in mice immunologically depressed by thymectomy and total body irradiation considerable numbers of bacilli were present in the iris and ciliary body and also in the limbal cornea. In the armadillo bacilli were found in large numbers in virtually all tissues except the lens, retina, optic nerve, and aqueous and vitreous humours, but the uveal tract was heavily involved. Findings are discussed in relation to the great frequency of ocular involvement and the importance of immune-complex disease in patients with lepromatous leprosy, and to factors wihch may favour the localisation and multiplication of Mycobacterium leprae in the eye.

Animals↗
PubMed1979

Comparison of proteins from Mycobacterium fortuitum, Mycobacterium nonchromogenicum and Mycobacterium terrae using flat bed electrophoresis.

Polyacrylamide gel electrophoresis of bacterial lysates in a flat bed gives a linear relationship between 1n mol. wt of the proteins and the square root of their migration distances, thereby allowing standardization of different electrophoresis runs and precise comparison between homologous bands. The results obtained with Mycobacterium fortuitum, M. terrae and M. nonchromogenicum strains were used in numerical analysis. Mycobacterium fortuitum and M. nonchromogenicum showed a greater internal similarity than M. terrae, while two strains of the latter clustered with M. nonchromogenicum. The method described allows the comparison of mycobacteria with different generation times and provides a large number of good characters for numerical taxonomy.

Bacterial Proteins↗
PubMed2000

Comparison of enhanced Mycobacterium tuberculosis amplified direct test with COBAS AMPLICOR Mycobacterium tuberculosis assay for direct detection of Mycobacterium tuberculosis complex in respiratory and extrapulmonary specimens.

The new Roche COBAS AMPLICOR Mycobacterium tuberculosis Assay was compared to the Gen-Probe enhanced Mycobacterium tuberculosis Amplified Direct Test (AMTDII). A total of 486 specimens (296 respiratory and 190 extrapulmonary) collected from 323 patients were tested in parallel with both assays. Results were compared with those of acid-fast staining and culture, setting the combination of culture and clinical diagnosis as the "gold standard." After resolution of discrepant results, the sensitivity, specificity, and positive and negative predictive values for AMTDII were 85.7, 100, 100, and 90.4% for respiratory specimens and 82.9, 100, 100, and 95. 5% for extrapulmonary specimens, respectively. The corresponding values for AMPLICOR were 94.2, 100, 100, and 96.6% for respiratory specimens and 85, 100, 100, and 96.1% for extrapulmonary specimens, respectively. No significant differences were observed between the results of both assays or, within each one, between respiratory and extrapulmonary specimens. The difference between AMTDII and AMPLICOR sensitivities was related to the presence of inhibitory samples, which the former assay, lacking an internal amplification control (IAC), could not detect. The overall inhibition rate for the AMPLICOR assay was 3.9% (19 specimens). It is concluded that, although both amplification assays proved to be rapid and specific for the detection of M. tuberculosis complex in clinical samples, AMPLICOR, by a completely automated amplification and detection procedure, was shown to be particularly feasible for a routine laboratory setting. Finally, AMTDII is potentially an excellent diagnostic technique for both respiratory and extrapulmonary specimens, provided that an IAC is included with the assay.

Biopsy↗
PubMed2003

Characterization of Mycobacterium montefiorense sp. nov., a novel pathogenic Mycobacterium from moray eels that is related to Mycobacterium triplex.

The characterization of a novel Mycobacterium sp. isolated from granulomatous skin lesions of moray eels is reported. Analysis of the hsp65 gene, small-subunit rRNA gene, rRNA spacer region, and phenotypic characteristics demonstrate that this organism is distinct from its closest genetic match, Mycobacterium triplex, and it has been named M. montefiorense sp. nov.

Animals↗
PubMed1981

Structure of the specific oligosaccharides from the glycopeptidolipid antigens of serovars in the Mycobacterium avium-Mycobacterium intracellulare-Mycobacterium scrofulaceum complex.

The specific oligosaccharide units of the C-mycosidic glycopeptidolipid antigens from serovarieties in the Myobacterium avium-Mycobacterium intracellulare-Mycobacterium scrofulaceum complex were liberated as oligosaccharide alditols by treatment of the glycopeptidolipids with alkaline borohydride. The complete structures of the oligosaccharide alditols have been derived from their 1H-NMR spectra or those of their permethylated (or pertrideuteriomethylated) derivatives, the mass spectra of the methylated derivatives, and from methylation fragmentation analysis. Periodate oxidation was also used to confirm the position of the link between the ultimate and penultimate sugars. The following structures are proposed (with some extrapolation of enantiomeric configurations where evidence for assignment is not yet complete) for the oligosaccharide alditols: Serovar 9 2,3-Me2-alpha-L-Fucp-(1 leads to 4)-2,3-Me2-alpha-L-Fucp-(1 leads to 3)-alpha-L-Rhap-(1 leads to 2)-6-deoxy-L-Talol Serovar 25 2-Me-alpha-L-Fucp-(1 leads to 4)-2-Me-alpha-L-Fucp-(1 leads to 3)-alpha-L-Rhap-(1 leads to 2)-6-deoxy-L-talol Serovar 8 4,6-(1'-carboxyethylidene)-3-Me-beta-D-Glcp-(1 leads to 3)-alpha-L-Rhap-(1 leads to 2)-6-deoxy-L-Talol Thus, 6-deoxytalitol (6-deoxytalose in the original glycopeptidolipid) invariably occupies the reducing terminus. Rhamnose is invariably the penultimate sugar, and the link between rhamnose and 6-deoxytalose is invariably alpha 1 leads to 2. Moreover, the results point to the outer one or two appendages for the provision of individually distinctive features required for antigen specificity. The abbreviations used are: serovar, serologically distinct varieties; Me, methyl; Fucp, fucopyranose; Rhap, rhamnopyranose; Talol, talitol.

Antigens, Bacterial↗
PubMed1994

Comparison of the 23S ribosomal RNA genes and the spacer region between the 16S and 23S rRNA genes of the closely related Mycobacterium avium and Mycobacterium paratuberculosis and the fast-growing Mycobacterium phlei.

The 23S rDNA sequences of Mycobacterium paratuberculosis, M. avium and M. phlei and the sequences of the spacer regions between the 16S and 23S rRNA genes were determined. The overall 23S rDNA sequence identity between M. paratuberculosis and M. avium was 99.7% (nine mismatches), showing the very close relatedness of these mycobacteria. Evolutionary distances between the five known mycobacterial 23S rRNA/rDNA sequences and those of other Gram-positive G + C-rich bacteria were determined. The 23S rDNA sequences of mycobacteria showed two inserted regions compared to the other bacteria. A mycobacterial unique region contained one mismatch between M. paratuberculosis and M. avium. An Actinomycetales-specific insertion, consisting of 111 nucleotides, was completely identical for M. paratuberculosis and M. avium. The sequence of the intergenic spacer region between 16S and 23S rDNA had a length of 278 bp for M. paratuberculosis and M. avium with only two mismatches. The spacer region of the fast-growing M. phlei was 85 bp longer. No tRNA-encoding region was found in the spacer region.

Actinomycetales↗
PubMed2000

Aminoglycoside resistance in Mycobacterium kansasii, Mycobacterium avium-M. intracellulare, and Mycobacterium fortuitum: are aminoglycoside-modifying enzymes responsible?

Aminoglycoside acetyltransferase was detected in Mycobacterium kansasii and M. fortuitum but not in M. avium-M. intracellulare when they were screened by a radioassay. Aminoglycoside phosphotransferase and nucleotidyltransferase activities were absent from all three species tested. Acetyltransferases from both M. kansasii and M. fortuitum displayed relatively high K(m)s, all at the millimolar level, for substrates including tobramycin, neomycin, and kanamycin A. The K(m) of each substrate was well above the corresponding maximum achievable level in serum. The low affinities of these enzymes for their substrates suggested that drug modification in vivo was very unlikely. Among the various substrates tested, no apparent positive correlation was found between substrate affinity and resistance level. The presence of aminoglycoside-modifying enzymes in these mycobacterial species was therefore not shown to confer resistance to aminoglycosides.

Acetyltransferases↗