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Tigecycline - A New Antibiotic in Infections Treatment

100%

Stefaniuk E., Hryniewicz W.

Polish Journal of Surgery

2007

vol. 79

issue 9

587-593

Tigecycline, a member of a new class of antimicrobials (glycylcyclines), was shown to have expanded broad spectrum activity against most commonly encountered species responsible for community and hospital acquired infections, including Gram-positive and Gram-negative multidrug resistant bacterial strains.The aim of the study was to evaluate the activity of tigecycline against resistant bacterial strains commonly associated with nosocomial infections, including skin structure, subcutaneous layer and intra-abdominal infections.Material and methods. Ten general hospitals from different regions of Poland participated in the study. Antimicrobial susceptibility tests were carried for 539 isolates of different genus/species of bacterial strains isolated from patients hospitalized in hospitals throughout Poland. Minimal inhibitory concentrations (MICs) of tigecycline were determined using the broth dilution method.Results. Ten strains of 50 S. aureus isolates, i.e. 20%, were methicillin-resistant (MRSA). The lowest MIC90 values observed for tigecycline were (0.25 μg/ml); they were similar to the MIC50 for MSSA and MRSA.S. pneumoniae varied with respect to their susceptibility to penicillin. Twenty two percent of isolates (n=11) had decreased susceptibility to penicillin. However, all 50 strains of this species were susceptible to levofloxacin, vancomycin and linezolid. Tigecycline exhibited high activity against S. pneumoniae strains. Tigecycline MIC90 values for this group of strains were lower than MIC90 of the remaining antibiotics. One hundred percent of collected S. agalactiae strains were susceptible to all investigated antibiotics.Conclusion. The presented data indicate that tigecycline exhibits excellent inhibitory activity against nosocomial and community pathogens regardless of resistance patterns.

A novel member of the thermolysin family, cloning and biochemical characterization of metalloprotease from Staphylococcus pseudintermedius

61%

Wladyka B., Bista M., Sabat A. J., Bonar E., Grzeszczuk S., Hryniewicz W., Dubin A.

2008

vol. 55

issue 3

525-536

Thermolysins constitute a family of secreted bacterial metalloproteases expressed, among others, by several pathogens. Strains of Staphylococcus pseudintermedius isolated from diseased dogs and judged as protease-positive, by skim milk agar plate culture, were investigated for protease content. No proteolytic activity was detected when the bacteria were grown in regular liquid media. Unexpectedly, supplementation of the medium with calcium ions resulted in expression of a metalloprotease and profound changes in the profile of extracellular proteins. On the basis of homology to other staphylococcal metalloproteases, the nucleotide sequence of the gene encoding this protease (Pst) and its flanking regions was determined. The full-length pst codes for a protein with an open reading frame of 505 amino acids. The internal region contains the HEXXH catalytic domain that is conserved in members of the thermolysin family. Regardless of the presence of calcium in the medium, the expression of the protease gene was of the same intensity. This suggests that regulation of the metalloprotease production by calcium ions is at a post-transcriptional level. Isolates of S. pseudintermedius exhibit a proteolytic phenotype due to the metalloprotease expression, however only in presence of calcium ions, which most probably stabilize the structure of the protease.

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1 Acta Biochimica Polonica

1 Polish Journal of Surgery

1 2008

1 2007

2 Hryniewicz W.

1 Bista M.

1 Bonar E.

1 Dubin A.

1 Grzeszczuk S.

1 Sabat A. J.

1 Stefaniuk E.

1 Wladyka B.

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Tigecycline - A New Antibiotic in Infections Treatment

A novel member of the thermolysin family, cloning and biochemical characterization of metalloprotease from Staphylococcus pseudintermedius