Cloning and molecular characterization of Cu,Zn superoxide dismutase from Actinobacillus pleuropneumoniae.

Infection and Immunity
P R LangfordJ S Kroll

Abstract

Copper-zinc superoxide dismutases (Cu,Zn SODs), until recently considered very unusual in bacteria, are now being found in a wide range of gram-negative bacterial species. Here we report the cloning and characterization of sodC, encoding Cu,Zn SOD in Actinobacillus pleuropneumoniae, a major pathogen of pigs and the causative organism of porcine pleuropneumonia. sodC was shown to lie on a monocistronic operon, at the chromosomal locus between the genes asd (encoding aspartate semialdehyde dehydrogenase) and recF. The primary gene product was shown to have an N-terminal peptide extension functioning as a leader peptide, so that the mature Actinobacillus enzyme, like other bacterial examples, is directed to the periplasm, where it is appropriately located to dismutate exogenously generated superoxide. While the role of these secreted bacterial SODs is unknown, we speculate that in A. pleuropneumoniae the enzyme may confer survival advantage by accelerating dismutation of superoxide derived from neutrophils, a central host defense response in the course of porcine infection.

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Citations

Aug 12, 2009·Applied and Environmental Microbiology·Janine T BosséPaul R Langford
Jul 20, 2007·Infection and Immunity·Nataliya V BalashovaScott C Kachlany
Oct 19, 2013·Journal of Basic Microbiology·Hye Jung ChoiWoo Hong Joo
Oct 15, 1998·Proceedings of the National Academy of Sciences of the United States of America·J S KrollP R Langford
Feb 27, 2001·Journal of Bacteriology·S M Doree, M H Mulks
Nov 17, 2020·Frontiers in Veterinary Science·Berenice Plasencia-MuñozAlma L Guerrero-Barrera
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Apr 27, 2002·Science·Dirk Roos, Christine C Winterbourn
Nov 17, 2009·Biochimica Et Biophysica Acta·J J P PerryJ A Tainer
Nov 23, 2011·Journal of Inorganic Biochemistry·Dávid ArusTamás Gajda

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