%0 Journal Article %A Kroll, J. Simon %A Langford, Paul R. %A Wilks, Kathryn E. %A Keil, Anthony D. %T Bacterial [Cu,Zn]-superoxide dismutase: phylogenetically distinct from the eukaryotic enzyme, and not so rare after all! %D 1995 %J Microbiology, %V 141 %N 9 %P 2271-2279 %@ 1465-2080 %R https://doi.org/10.1099/13500872-141-9-2271 %K [Cu,Zn]-superoxide dismutase %K Haemopbilus-Actinobacillus-Pasteurella %K Neisseria %K bacterial pathogenicity %K phylogenetic tree %I Microbiology Society, %X Copper- and zinc-containing superoxide dismutases ([Cu,Zn]-SODs) are generally considered almost exclusively eukaryotic enzymes, protecting the cytosol and extracellular compartments of higher organisms from damage by oxygen free-radicals. The recent description of a few examples of bacterial forms of the enzyme, located in the periplasm of different Gram-negative micro-organisms, prompted a re-evaluation of this general perception. A PCR-based approach has been developed and used successfully to identify bacterial genes encoding [Cu,Zn]-SOD in a wide range of important human and animal pathogens - members of the Haemophilus, Actinobacillus and Pasteurella (HAP) group, and Neisseria meningitidis. Comparison of [Cu,Zn]-SOD peptide sequences found in Haemophilus ducreyi, Actinobacillus pleuropneumoniae, Actinobacillus actinomycetemcomitans, Pasteurella multocida, and N. meningitidis with previously described bacterial proteins and examples of eukaryotic [Cu,Zn]-SOD has shown that the bacterial proteins constitute a distinct family apparently widely separated in evolutionary terms from the eukaryotic examples. The widespread occurrence of [Cu,Zn]-SOD in the periplasm of bacterial pathogens, appropriately located to dismute exogenously derived superoxide radical anions, suggests that this enzyme may play a role in the interactive biology of organisms with their hosts and so contribute to their capacity to cause disease. %U https://www.microbiologyresearch.org/content/journal/micro/10.1099/13500872-141-9-2271