Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: DrugBank:APRD00216 (ABC)
 8,859 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Female C3H/He mice aged 14 weeks with transplanted MM46 tumor were used to investigate the effect of an immunomodulator, Z-100 (an arabinomannan lipid extracted from Mycobacterium tuberculosis strain Aoyama B) combined with local irradiation of 30 Gy (3,000 rad). Daily doses of 5 micrograms, 50 micrograms and 500 micrograms/kg of Z-100 were injected intramuscularly for 14 consecutive days after irradiation, and 2 times a week for 6 weeks thereafter. The antitumor effect was evaluated by the changes in tumor volume and survival curves. In groups administered 50 micrograms and 500 micrograms/kg of Z-100, tumor growth decreased significantly compared with the control group (radiotherapy group). Concerning survival rates of each group of mice, there were no marked differences between Z-100 administered groups and the control group. To clarify the mechanisms of action of Z-100, the changes in the lymphocyte subsets infiltrated into tumor tissue after Z-100 treatment were analysed immunohistochemically using monoclonal antibodies, anti-Thy 1.2, anti-Lyt-1, anti-Lyt-2, anti-L3T4, MAS034b and MAS053c and avidin-biotin-peroxidase complex method (ABC method). In the findings of immunohistochemical studies, differences were hardly observed between groups administered Z-100 and groups treated with radiation only. From these results, it was concluded that immunological effects of Z-100 resembled that of radiotherapy on the topical tumor tissue.
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PMID:[Experimental study of the antitumor effect of Z-100 in the treatment of MM46 tumor transplanted in C3H/He mice. 2. Effect of the combination therapy of radiation and long term administration of Z-100]. 273 40

The avidin-biotin complex peroxidase (ABC-P) method was used to detect Mycobacterium bovis, and the results were compared with those obtained by the Ziehl-Neelsen (ZN) technique. Lesions were examined from 18 cows and 24 goats with tuberculosis. All animals showed pulmonary lesions, which in the cattle were mainly minor (i.e. primary complex) but in the goats were sometimes minor and sometimes severe. Microscopically, typical granulomas were seen in the lungs and lymph nodes, with central necrosis and the cellular components of chronic inflammation, but mycobacteria were either seen in small numbers or were not detectable. The ABC-P technique was more sensitive than the ZN method, as shown by the number of positive animals detected, the intensity of staining, and the successful use of low magnification. Caprine lesions, although more severe than bovine lesions, appeared to contain fewer organisms.
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PMID:Comparison of Ziehl-Neelsen staining and immunohistochemistry for the detection of Mycobacterium bovis in bovine and caprine tuberculous lesions. 750 54

The nucleotide sequence of cosmid B1790, carrying the Rif-Str regions of the Mycobacterium leprae chromosome, has been determined. Twelve open reading frames were identified in the 36716bp sequence, representing 40% of the coding capacity. Five ribosomal proteins, two elongation factors and the beta and beta' subunits of RNA polymerase have been characterized and two novel genes were found. One of these encodes a member of the so-called ABC family of ATP-binding proteins while the other appears to encode an enzyme involved in repairing genomic lesions caused by free radicals. This finding may well be significant as M. leprae, an intracellular pathogen, lives within macrophages.
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PMID:Nucleotide sequence of the first cosmid from the Mycobacterium leprae genome project: structure and function of the Rif-Str regions. 844 28

Immunohistochemical studies were performed to determine the presence and distribution of polypeptide transforming growth factor (TGF)-beta 1, a cytokine with macrophage-suppressing activity, in skin biopsies from 41 patients with different clinical forms of leprosy. We used an anti-TGF-beta 1 polyclonal antibody and the avidinbiotin-peroxidase (ABC complex) method. The results demonstrated that the lesions of the lepromatous and borderline lepromatous forms presented intense cytoplasm staining for TGF-beta 1 in the cells of the dermal infiltrate. A reaction of moderate intensity was observed in the cells of granulomas from borderline borderline cases, whereas no detectable immunoreaction was observed in granuloma cells from the tuberculoid and borderline tuberculoid forms. Considering that in the lepromatous leprosy form Mycobacterium leprae multiplies in the cytoplasm of macrophages and the lesions are diffuse and consist of poorly differentiated young macrophages, we believe that these alternations may be explained at least in part by the presence of TGF-beta 1 in the dermal infiltrate. Production of the cytokine may be induced by the presence of the bacillus itself and of its constituents, causing a mechanism of parasite evasion. Similarly, the absence of TGF-beta 1 in tuberculoid leprosy, which progresses with a specific immune response to M. leprae, may explain the intense differentiation of macrophage cells with the formation of well defined epithelioid granulomas capable of eliminating most of the bacilli.
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PMID:Detection of transforming growth factor-beta 1 in dermal lesions of different clinical forms of leprosy. 877 45

The DNA sequence has been determined upstream of the amiE structural gene in the amidase operon of Rhodococcus sp. R312 and a new ORF (amiS2) identified. The amiS2 gene encodes a potential 206 amino acid (aa) protein containing a high proportion of hydrophobic residues. The AmiS2 protein possesses high homology to the ORFP3, amiS and ureI gene products from the Mycobacterium smegmatis (Ms) acetamidase operon, Pseudomonas aeruginosa (Pa) amidase operon and Helicobacter pylori (Hp) urease operon, respectively. Hydropathic analysis and secondary structure prediction of AmiS2 suggested the presence of seven potential transmembrane (TM) alpha-helices. Sequence analysis of the amiB2 gene, located downstream of the Rhodococcus sp. R312 amiE gene, showed that it encoded a 351-aa protein containing a potential ATP-binding motif. AmiB2 showed significant homology with the ATP-binding subunit of the bacterial Clp protease and high homology with the amiB product located within the Pa amidase operon. AmiB2 and AmiS2 appear to be two components of a recently identified novel family of ABC transporters (Wilson et al., 1995) and might be responsible for the adsorption of amidase substrates or release of their hydrolysis products.
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PMID:Amide metabolism: a putative ABC transporter in Rhodococcus sp. R312. 898 91

A gene encoding a protein homologous to the periplasmic ABC phosphate binding receptor PstS from Escherichia coli was cloned and sequenced from a lambda gt11 library of Mycobacterium tuberculosis by screening with monoclonal antibody 2A1-2. Its degree of similarity to the E. coli PstS is comparable to those of the previously described M. tuberculosis phosphate binding protein pab (Ag78, Ag5, or 38-kDa protein) and another M. tuberculosis protein which we identified recently. We suggest that the three M. tuberculosis proteins share a similar function and could be named PstS-1, PstS-2, and PstS-3, respectively. Molecular modeling of their three-dimensional structures using the structure of the E. coli PstS as a template and their inducibility by phosphate starvation support this view. Recombinant PstS-2 and PstS-3 were produced and purified by affinity chromatography. With PstS-1, these proteins were used to demonstrate the specificity of three groups of monoclonal antibodies. Using these antibodies in flow cytometry and immunoblotting analyses, we demonstrate that the three genes are expressed and their protein products are present and accessible at the mycobacterial surface as well as in its culture filtrate. Together with the M. tuberculosis genes encoding homologs of the PstA, PstB, and PstC components we cloned before, the present data suggest that at least one, and possibly several, related and functional ABC phosphate transporters exist in mycobacteria. It is hypothesized that the mycobacterial gene duplications presented here may be a subtle adaptation of intracellular pathogens to phosphate starvation in their alternating growth environments.
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PMID:Three different putative phosphate transport receptors are encoded by the Mycobacterium tuberculosis genome and are present at the surface of Mycobacterium bovis BCG. 913 6

We describe here the PCR amplification of a DNA fragment (mtp1) from Mycobacterium smegmatis using primers derived from consensus sequences of the ABC family of transporters. The fragment encodes amino acid sequences that exhibited significant homology with different ABC transporters. Amino acid sequence alignment of the full length gene with other transporters identified the ABC protein as the B-subunit of the phosphate specific transporter. Strikingly, a M. smegmatis colony which exhibited a high level of ciprofloxacin resistance showed mRNA level overexpression of mtp1. Thus this is the first report in any prokaryote indicating differential expression of an ABC transporter in a fluoroquinolone resistant colony.
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PMID:Identification of an ABC transporter gene that exhibits mRNA level overexpression in fluoroquinolone-resistant Mycobacterium smegmatis. 954 Oct 26

A secretion reporter system based on Staphylococcus aureus nuclease (nuc) was developed for use in mycobacteria. Fusion of secretion signals to the reporter cloned in a shuttle vector, pBPnuc1, resulted in halo formation around colonies of Mycobacterium smegmatis and Mycobacterium tuberculosis grown on DNase agar plates containing Methyl Green indicator dye. This in-situ detection system was used to identify secreted proteins by screening a pBPnuc1::H37Rv nuc gene fusion library in M. smegmatis. The clones identified in this screen all formed colony halos when present in M. tuberculosis grown on indicator media. The proteins corresponded to DesA2, a stearoyl-acyl carrier protein desaturase, PepA, a putative serine protease and the Apa antigen, which is the ATP-binding subunit of an ABC transport system. Of these proteins, only PepA and Apa contained recognizable leader peptides.
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PMID:Staphylococcus aureus nuclease is a useful secretion reporter for mycobacteria. 1054 30

Phosphate specific transporter (Pst) in bacteria is involved in phosphate transport. Pst is a multisubunit system which belongs to the ABC family of transporters. The import function of this transporter is known to be operative at media phosphate concentrations below the millimolar range. However, we found amplification of this transporter in a laboratory generated ciprofloxacin resistant Mycobacterium smegmatis colony (CIPr) which was grown in a condition when phosphate scavenging function of this operon was inoperative. Our results therefore argue the role of this ABC importer in conferring high level of fluoroquinolone resistance in CIPr.
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PMID:Role of an ABC importer in mycobacterial drug resistance. 1058 94

Oxygen starvation triggers an adaptive stationary-phase response in Mycobacterium smegmatis. During this anaerobic stationary phase, RNA synthesis continues at a low but significant level. Employing a modified expressed-sequence-tag (EST) approach, in combination with the M. tuberculosis genome data and comparative Northern analysis, we have identified the first genes that show an increase in transcription in M. smegmatis cells that have entered anaerobic stationary phase. One gene encodes the counterpart of the M. tuberculosis NifS-like protein Rv1464. Two genes are homologues of M. tuberculosis Rv1460 and Rv3368c, of unknown function. Strikingly, several genes induced by oxygen starvation encode putative stress protection proteins (counterparts of M. tuberculosis DnaK, Rv0350; betaine-aldehyde dehydrogenase, Rv0768; thioredoxin reductase, Rv3913) and ABC transporters (counterparts of M. tuberculosis Rv1463, Rv1473, Rv3197). We conclude that development of general stress resistance and certain active transport processes might play a role in the survival of oxygen-starved M. smegmatis.
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PMID:Upregulation of stress response genes and ABC transporters in anaerobic stationary-phase Mycobacterium smegmatis. 1062 50


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