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*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

35 Scopus citations

Abstract

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
Pages (from-to)233-238
Number of pages6
JournalFEMS Microbiology Letters
Volume202
Issue number2
DOIs
StatePublished - 21 Aug 2001

Keywords

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

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