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| Michelim,Lessandra; Muller,Gabriela; Zacaria,Jucimar; Delamare,Ana Paula Longaray; Costa,Sérgio Olavo Pinto da; Echeverrigaray,Sergio. |
| Proteus mirabilis is one of the most important pathogens associated with complicated urinary tract infections (acute pyelonephritis, bladder infections, kidney stones) and bacteremia, affecting patients with anatomical abnormalities, immunodeficiency, and long-term urinary catheterization. For epidemiological purposes, various molecular typing methods, such as pulse-field gel electrophoresis (PFGE) or ribotyping, have been developed for this pathogen. However, these methods are labor intensive and time-consuming. We evaluated the discriminatory power of several PCR-based fingerprinting methods (RAPD, ISSR, ERIC-PCR, BOX-PCR and rep-PCR) for P. mirabilis clinical isolates. Typing patterns and clustering analysis indicated that RAPD, BOX-PCR and ERIC-PCR... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Proteus mirabilis; Molecular markers; Fingerprinting; PCR. |
| Ano: 2008 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1413-86702008000500014 |
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| Fernandes,B.L.; Anéas,M.A.F.; Juliano,L.; Palma,M.S.; Lebrun,I.; Portaro,F.C.V.. |
| The protease ZapA, secreted by Proteus mirabilis, has been considered to be a virulence factor of this opportunistic bacterium. The control of its expression requires the use of an appropriate methodology, which until now has not been developed. The present study focused on the replacement of azocasein with fluorogenic substrates, and on the definition of enzyme specificity. Eight fluorogenic substrates were tested, and the peptide Abz-Ala-Phe-Arg-Ser-Ala-Ala-Gln-EDDnp was found to be the most convenient for use as an operational substrate for ZapA. A single peptide bond (Arg-Ser) was cleaved with a Km of 4.6 µM, a k cat of 1.73 s-1, and a catalytic efficiency of 376 (mM s)-1. Another good substrate for ZapA was peptide 6... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Metalloprotease; Substrate specificity; Quenched fluorescence peptides; Proteus mirabilis. |
| Ano: 2000 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2000000700006 |
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| The inducible tetracycline resistance determinant isolated from Proteus mirabilis cloned into the plasmid pACYC177 was mutagenized by insertion of a mini-Mu-lac phage in order to define the regions in the cloned sequences encoding the structural and regulatory proteins. Three different types of mutants were obtained: one lost the resistance phenotype and became Lac+; another expressed the resistance at lower levels and constitutively; the third was still dependent on induction but showed a lower minimal inhibitory concentration. The mutant phenotypes and the locations of the insertions indicate that the determinant is composed of a repressor gene and a structural gene which are not transcribed divergently as are other known tetracycline determinants... |
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Palavras-chave: Tetracycline; Mutation; LacZ-fusion; Proteus mirabilis; Bacteriophage Mu. |
| Ano: 1997 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1997000300009 |
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| Anéas,M.A.F.; Portaro,F.C.V.; Lebrun,I.; Juliano,L.; Palma,M.S.; Fernandes,B.L.. |
| The opportunistic bacterium Proteus mirabilis secretes a metalloprotease, ZapA, considered to be one of its virulence factors due to its IgA-degrading activity. However, the substrate specificity of this enzyme has not yet been fully characterized. In the present study we used fluorescent peptides derived from bioactive peptides and the oxidized ß-chain of insulin to determine the enzyme specificity. The bradykinin- and dynorphin-derived peptides were cleaved at the single bonds Phe-Ser and Phe-Leu, with catalytic efficiencies of 291 and 13 mM/s, respectively. Besides confirming already published cleavage sites, a novel cleavage site was determined for the ß-chain of insulin (Val-Asn). Both the natural and the recombinant enzyme displayed the same broad... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Proteus mirabilis; Metalloprotease; Substrate specificity; Fluorogenic peptides; IgA; Insulin ß-chain. |
| Ano: 2001 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2001001100004 |
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