Alkaline Phosphatases from Mycobacterium smegmatis

David, Hugo L.

doi:10.1099/00221287-101-1-99

Cited by 13 publications

(6 citation statements)

References 3 publications

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“…The period of treatment with the above spheroplast-inducing substances was 54 to 60 h (corresponding to three cell divisions) instead of the 18 h for M. aurum. After incubation, the cells were harvested by centrifugation, and our method was followed as reported earlier (42 (35), arylsulfatase (63), fl-glucosidase (13), acid phosphatase (26), alkaline phosphatase (10), penicillinase (15), and trehalase (15).…”

Section: Methodsmentioning

confidence: 99%

Multiple drug resistance in Mycobacterium avium: is the wall architecture responsible for exclusion of antimicrobial agents?

Rastogi¹,

Fréhel²,

Ryter³

et al. 1981

Antimicrob Agents Chemother

196

129

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Whole cells of Mycobacterium avium, characterized by their negative response in the nine biochemical tests used for mycobacterial identification in our laboratory, turned positive for nitrate reductase, Tween-80 hydrolysis, beta-glucosidase, acid phosphatase, alkaline phosphatase, penicillinase, and trehalase after their wall portion was removed to yield spheroplasts. This suggested that the negative results in most of the biochemical procedures were caused by the exclusion mechanism at the wall level. Preliminary transmission and scanning electron microscopic studies showed differences at wall level between laboratory-maintained opaque, dome-shaped (SmD) and host-recycled smooth, transparent (SmT) colony type variants of M. avium and suggested the presence of an outer regularly structured layer in SmT variants. Comparative ultrastructural studies utilizing different polysaccharide coloration methods confirmed the presence of an outer polysaccharide layer in SmT variants which was probably related to their enhanced pathogenicity for experimental animals and drug resistance as compared to that of SmD variants. These findings are discussed with respect to multiple drug resistance, virulence, and gene expression of M. avium.

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Section: Methodsmentioning

confidence: 99%

Multiple drug resistance in Mycobacterium avium: is the wall architecture responsible for exclusion of antimicrobial agents?

Rastogi¹,

Fréhel²,

Ryter³

et al. 1981

Antimicrob Agents Chemother

196

129

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“…The tests shown in Table 2 have been described previously (14)(15)(16); when necessary, some of these tests were performed on media supplemented with mycobactin. Stimulation by pyruvate (4.1 g/liter) and resistance to NaCl were tested on Middlebrook 7H10 medium; the ability to grow at pH 5.5 was determined on Middlebrook 7Hll medium.…”

Section: Mycobacterial Strainsmentioning

confidence: 99%

Numerical Taxonomy of Mycobactin-Dependent Mycobacteria, Emended Description of Mycobacterium avium, and Description of Mycobacterium avium subsp. avium subsp. nov., Mycobacterium avium subsp. paratuberculosis subsp. nov., and Mycobacterium avium subsp. silvaticum subsp. nov.

Thorel

Krichevsky

Lévy-Frébault

1990

International Journal of Systematic Bacteriology

349

195

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“…The two forms of the enzyme differ in their regulatory sensitivities; the dimer is sensitive in vitro to inhibition by ATP, whereas the multimeric form is inhibited by NADH and 2-oxoglutarate. The amino acid sequences of citrate synthase either have been determined directly from the protein or have been inferred from DNA sequences for members of the domain Eukarya (including pig [9], Tetrahymena thermophila [30], Arabidopsis thaliana [50], and Saccharomyces cerevisiae [46], for members of the domain Bacteria (including Escherichia coli [28], Acinetobacter anitratum [ 141, R. prowazekii [62], Coxiella bumetii [21], Bartonella henselae [29], Pseudomonas aeruginosa [ 151, Corynebacterium glutamicum [ 161, Bacillus coagulans [43], and Mycobacterium smegmatis [12]), and for a representative of the domain Archaea, Thermoplasma acidophilum (47). Multiple alignments of these protein sequences have revealed significant levels of similarity between intradomain Eukarya sequences (46 to 92%) and between intraphylum Proteobacteria sequences (56 to 75%); however, the interdomain levels of similarity are far lower (20 to 26%) (47).…”

mentioning

confidence: 99%

Citrate Synthase Gene Comparison, a New Tool for Phylogenetic Analysis, and Its Application for the Rickettsiae

Roux

Rydkina

Eremeeva

et al. 1997

International Journal of Systematic Bacteriology

498

366

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Using PCR and an automated laser fluorescent DNA sequencer, we amplified and sequenced a 1,234-bp fragment of the citrate synthase-encoding gene ( g U ) of 28 bacteria belonging to the genus Rickettsia. Comparative sequence analysis showed that most of the spotted fever group (SFG) rickettsiae belonged to one of two subgroups. The first subgroup included Rickettsia massiliae, strain Bar 29, Rickettsia rhipicephali, "Rickettsia aeschlimanni," and Rickettsia montana, which have been isolated only from ticks. The second subgroup was larger and included the majority of the human pathogens and also rickettsiae isolated only from ticks; the members of this subgroup were strain S, Rickettsia apicae, "Rickettsia mongolotimonae," Rickettsia sibirica, Rickettsia parkeri, Rickettsia conorii, Rickettsia rickettsii, the Thai tick typhus rickettsia, the Israeli tick typhus rickettsia, the Astrakhan fever rickettsia, "Rickettsia slovaca," and Rickettsia japonica. The sequence analysis also showed that the tick-borne organisms Rickettsia helvetica and Rickettsia australis and the mite-borne organism Rickettsia akari were associated with the SFG cluster; that Rickettsia prowazekii and Rickettsia typhi, two representatives of the typhus group, clustered together; and that Rickettsia Canada, Rickettsia bellii, and the AB bacterium probably represent three new groups. We compared the phylogenetic trees inferred from citrate synthase gene sequences and from 16s ribosomal DNA (rDNA) sequences. For rickettsial phylogeny, the citrate synthase approach was more suitable, as demonstrated by significant bootstrap values for all of the nodes except those in the larger subgroup defined above. We also compared phylogenetic analysis results obtained in a comparison of the sequences of both genes for all of the representatives of the domain Bacteria for which the gZtA sequence was determined. We believe that comparison of glL4 sequences could be a complementary approach to 16s rDNA sequencing for inferring bacterial evolution, especially when unstable phylogenetic models are obtained from ribosomal sequences because of high levels of sequence similarity between the bacteria studied.Rickettsiae belong to the order Rickettsiales, whose members were described as obligately intracellular gram-negative microorganisms (55). Several species cause disease in humans or in other vertebrate and invertebrate hosts and have a worldwide distribution. Recently, on the basis of 16s rRNA sequence similarity, Rickettsia tsutsugamushi was removed from the genus Rickettsia and was renamed Orientia tsutsugarnushi (48). The genus Rickettsia is presently divided into two groups: the typhus group (TG), which includes three species (Rickettsia prowazekii, the agent of the epidemic typhus, Rickettsia typhi, which causes murine typhus, and Rickettsia Canada, which has been isolated only from ticks), and the spotted fever group (SFG). The number of recognized members of the SFG increased following the development of an improved cell culture isolation technique (the shell...

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Alkaline Phosphatases from Mycobacterium smegmatis

Cited by 13 publications

References 3 publications

Multiple drug resistance in Mycobacterium avium: is the wall architecture responsible for exclusion of antimicrobial agents?

Multiple drug resistance in Mycobacterium avium: is the wall architecture responsible for exclusion of antimicrobial agents?

Numerical Taxonomy of Mycobactin-Dependent Mycobacteria, Emended Description of Mycobacterium avium, and Description of Mycobacterium avium subsp. avium subsp. nov., Mycobacterium avium subsp. paratuberculosis subsp. nov., and Mycobacterium avium subsp. silvaticum subsp. nov.

Citrate Synthase Gene Comparison, a New Tool for Phylogenetic Analysis, and Its Application for the Rickettsiae

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