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

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.

authors

• Cirillo, Jeffrey

published proceedings

• FEMS Microbiol Lett

author list (cited authors)

• Liu, X., Feng, Z., Harris, N. B., Cirillo, J. D., Bercovier, H., & Barletta, R. G.

citation count

• 34

complete list of authors

• Liu, X||Feng, Z||Harris, NB||Cirillo, JD||Bercovier, H||Barletta, RG

publication date

• August 2001

publisher

• Oxford University Press (OUP)  Publisher

published in

• FEMS Microbiology Letters  Journal

keywords

• Amino Acid Sequence
• Animals
• Base Sequence
• Blotting, Western
• Cloning, Molecular
• Electrophoresis, Gel, Two-Dimensional
• Genes, Bacterial
• Humans
• Molecular Sequence Data
• Mycobacterium Avium
• Mycobacterium Avium Subsp. Paratuberculosis
• Paratuberculosis
• Sequence Homology, Amino Acid
• Subcellular Fractions
• Superoxide Dismutase
• Tuberculosis

PubMed Central ID

• 11520620

Digital Object Identifier (DOI)

• 10.1111/j.1574-6968.2001.tb10809.x

start page

• 233

end page

• 238

volume

• 202

issue

• 2

URL

• http://dx.doi.org/10.1111/j.1574-6968.2001.tb10809.x