Identification of a secreted superoxide dismutase in Mycobacterium avium ssp. paratuberculosis

Xiaofei Liu, Zhengyu Feng, N. Beth Harris, Jeffrey D. Cirillo, Herve Bercovier, Raúl G. Barletta

Research output: Contribution to journalArticlepeer-review

34 Scopus citations


Mycobacterium avium ssp. paratuberculosis (M. paratuberculosis), the causative agent of Johne's disease, is an important animal pathogen that has also been implicated in human disease. The major proteins expressed by M. paratuberculosis were analyzed by two-dimensional gel electrophoresis, and a superoxide dismutase (Sod) was identified from this protein profile. The M. paratuberculosis Sod has a molecular mass of 23 kDa and an isoelectric point of 6.1. Sequence analysis of the corresponding sodA gene from M. paratuberculosis indicates that this protein is a manganese-dependent enzyme. We show that the M. paratuberculosis Sod is actively secreted, suggesting that it may elicit a protective cellular immune response in the host during infection.

Original languageEnglish (US)
Pages (from-to)233-238
Number of pages6
JournalFEMS Microbiology Letters
Issue number2
StatePublished - Aug 21 2001


  • Johne's disease
  • Mycobacterium avium ssp. paratuberculosis
  • Superoxide dismutase

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology
  • Genetics


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