Human eosinophil peroxidase induces surface alteration, killing, and lysis of Mycobacterium tuberculosis.
The antimycobacterial role of eosinophil peroxidase (EPO), one of the most abundant granule proteins in human eosinophils, was investigated. Our data indicate that purified EPO shows significant inhibitory activity towards Mycobacterium tuberculosis H37Rv. On a molar basis, this activity was similar to that exhibited by neutrophil myeloperoxidase (MPO) and was both dose and time dependent. In contrast to the activity of MPO, which requires H(2)O(2), EPO also exhibited anti-M. tuberculosis activity in the absence of exogenously added peroxide. Morphological evidence confirmed that the mechanism of action of EPO against mycobacteria differs from that of MPO. While MPO kills M. tuberculosis H37Rv exclusively in the presence of hydrogen peroxide, it does not induce morphological changes in the pathogen. In contrast, EPO-treated bacteria frequently had cell wall lesions and eventually underwent lysis, either in the presence or in the absence of H(2)O(2).
Borelli
Violetta
V
Dipartimento di Fisiologia e Patologia, Università di Trieste, Italy.
Vita
Francesca
F
Shankar
Sandeep
S
Soranzo
Maria Rosa
MR
Banfi
Elena
E
Scialino
Giuditta
G
Brochetta
Cristiana
C
Zabucchi
Giuliano
G
D001433:Bacteriolysis; D047209:Eosinophil Peroxidase; D004804:Eosinophils / Q000201:enzymology; D006801:Humans; D006861:Hydrogen Peroxide / Q000378:metabolism / Q000494:pharmacology; D008854:Microscopy, Electron; D008855:Microscopy, Electron, Scanning; D009169:Mycobacterium tuberculosis / Q000187:drug effects / Q000502:physiology* / Q000648:ultrastructure; D009195:Peroxidase / Q000378:metabolism / Q000494:pharmacology; D010544:Peroxidases / Q000378:metabolism* / Q000494:pharmacology
D006861:Hydrogen Peroxide; D047209:Eosinophil Peroxidase; D010544:Peroxidases; D009195:Peroxidase