Inactivation of Mycobacterium avium complex by UV irradiation.

The effectiveness of two major UV technologies against a highly prevalent species of Mycobacterium avium complex was investigated. Our study indicates that M. avium is much more resistant to UV irradiation than most waterborne pathogens and that it is one of the rare microorganisms that are highly resistant to both chemical and UV disinfection in water.

Assessing the effectiveness of low-pressure ultraviolet light for inactivating Mycobacterium avium complex (MAC) micro-organisms.

AIMS: To assess low-pressure ultraviolet light (LP-UV) inactivation kinetics of Mycobacterium avium complex (MAC) strains in a water matrix using collimated beam apparatus. METHODS AND RESULTS: Strains of M. avium (n = 3) and Mycobacterium intracellulare (n = 2) were exposed to LP-UV, and log(10) inactivation and inactivation kinetics were evaluated. All strains exhibited greater than 4 log(10) inactivation at fluences of less than 20 mJ cm(-2). Repair potential was evaluated using one M. avium strain. Light repair was evaluated by simultaneous exposure using visible and LP-UV irradiation. Dark repair was evaluated by incubating UV-exposed organisms in the dark for 4 h. The isolate did not exhibit light or dark repair activity. CONCLUSIONS: Results indicate that MAC organisms are readily inactivated at UV fluences typically used in drinking water treatment. Differences in activation kinetics were small but statistically significant between some tested isolates. SIGNIFICANCE AND IMPACT OF THE STUDY: Results provide LP-UV inactivation kinetics for isolates from the relatively resistant MAC. Although UV inactivation of Mycobacterium species have been reported previously, data collected in this effort are comparable with recent UV inactivation research efforts performed in a similar manner. Data were assessed using a rigorous statistical approach and were useful towards modelling efforts.

Involvement of the N- and C-terminal domains of Mycobacterium tuberculosis KatG in the protection of mutant Escherichia coli against DNA-damaging agents.

The Mycobacterium tuberculosis KatG enzyme, like most hydroperoxidase I (HPI)-type catalases, consists of two related domains, each with strong similarity to the yeast cytochrome c peroxidase. The catalase-peroxidase activity is associated with the amino-terminal domain but currently no definite function has been assigned to the carboxy-terminal domain, although it may play a role in substrate binding. This paper reports another possible function of the KatG protein involving protection of the host cell against DNA-damaging agents. The M. tuberculosis katG gene, the 5' domain and the 3' domain were cloned separately, in-frame with the maltose-binding protein, into the vector pMAL-c2. These constructs were introduced into four DNA-repair mutants of Escherichia coli, DK1 (recA), AB1884 (uvrC), AB1885 (uvrB) and AB1886 (uvrA), which were then tested for their ability to survive treatment with UV light (254 nm), hydrogen peroxide (1.6 mg ml-1) and mitomycin C (6 micrograms ml-1). All three constructs conferred resistance to UV upon the recA E. coli cells, whereas resistance to mitomycin C was found in all repair mutants tested. Protection against hydrogen peroxide damage was less pronounced and predominantly found in the recA host. These results indicated that the M. tuberculosis katG gene can enhance DNA repair in E. coli, and that the 5' and 3' domains can function separately. UV sensitivity tests on Mycobacterium intracellulare and M. tuberculosis strains mutant in katG revealed that the katG gene product does not play an additive role in the survival of mycobacterial cells after exposure to short-wavelength UV irradiation, in repair-competent cells.