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Haemophilus ducreyi is the etiologic agent of the sexually transmitted disease chancroid, an ulcerative condition implicated in increased HIV transmission. There is increasing evidence for the roles of oxidative stress proteins including superoxide dismutase enzymes in the survival and persistence of pathogenic organisms within the host. The sodA gene of Haemophilus ducreyi was isolated from a genomic plasmid library on the basis of its ability to rescue the hydrogen peroxide hypersensitivity of an Escherichia coli sodA sodB strain. The H. ducreyi SodA protein also complemented the aerobic growth defect of the E. coli sodA sodB strain in minimal medium. The deduced amino-acid sequence of the H. ducreyi sodA gene product is 74 and 70% identical to the Mn-SODs of Haemophilus influenzae and E. coli, respectively. However, unlike Mn-SODs, the H ducreyi SodA protein was inhibited by hydrogen peroxide in native gels stained for SOD activity.

The sodC gene of Haemophilus ducreyi was cloned and sequenced. The deduced amino acid sequence of this protein exhibited 71.6% identity and 81.8% similarity to the H. influenzae and H. parainfluenzae copper (Cu), zinc (Zn)-superoxide dismutase (SOD) enzymes. This gene was localized to a 2.2-kb H. ducreyi chromosomal DNA insert in plasmid pHdSOD. SOD activity was expressed in cell-free extracts of Escherichia coli containing the recombinant plasmid pHdSOD and was localized to the periplasmic space. The Cu,Zn-SOD produced by the H. ducreyi sodC gene did not complement the aerobic growth defect of an E. coli SOD-deficient mutant.