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Anti-staphylococcal activities of lysostaphin and LytM catalytic domain » Isaúde
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BMC microbiology [electronic resource]
2012-06-07 03:35:04

Anti-staphylococcal activities of lysostaphin and LytM catalytic domain

Descrição: Background:Lysostaphin and the catalytic domain of LytM cleave pentaglycine crossbridges ofStaphylococcus aureus peptidoglycan. The bacteriocin lysostaphin is secreted byStaphylococcus simulans biovar staphylolyticus and directed against the cell walls ofcompeting S. aureus. LytM is produced by S. aureus as a latent autolysin and can beactivated in vitro by the removal of an N-terminal domain and occluding region.Results:We compared the efficacies of the lysostaphin and LytM catalytic domains using a newlydeveloped model of chronic S. aureus infected eczema. Lysostaphin was effective, like inother models. In contrast, LytM was not significantly better than control. The differenttreatment outcomes could be correlated with in vitro properties of the proteins, including proteolytic stability, affinity to cell wall components other than peptidoglycan, and sensitivityto the ionic milieu.Conclusions:Although lysostaphin and LytM cleave the same peptide bond in the peptidoglycan, the twoenzymes have very different environmental requirements what is reflected in their contrastingperformance in mouse eczema model.

Identificador: doi:10.1186/1471-2180-12-97
Volume: 0
Página: 9 a


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