Previous Article | Next Article ![]()
Infection and Immunity, February 2003, p. 605-613, Vol. 71, No. 2
0019-9567/03/$08.00+0 DOI: 10.1128/IAI.71.2.605-613.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.
Maria Rosa Soranzo,1 Elena Banfi,3 Giuditta Scialino,3 Cristiana Brochetta,1 and Giuliano Zabucchi1*
Dipartimento di Fisiologia e Patologia,1 Dipartimento di Scienze Biomediche, Università di Trieste, 34127 Trieste, Italy,3 Department of Microbiology, Colorado State University, Fort Collins, Colorado 805232
Received 25 June 2002/ Accepted 16 September 2002
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 H2O2, 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 H2O2.
Present address: Zenith Conoco, Inc., Littleton, CO 80121.
This article has been cited by other articles:
Copyright © 2009 by the American Society for Microbiology. For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»