Title: AN EXTRACELLULAR CU ZN SUPEROXIDE DISMUTASE FROM LYSIPHLEBUS TESTACEIPES Authors
|Weathersbee Iii, Albert|
Submitted to: Florida Entomological Society Annual Meeting
Publication Type: Abstract Only
Publication Acceptance Date: May 27, 2005
Publication Date: July 24, 2005
Citation: Weathersbee III, A.A., Boykin, L.M. 2005. An extracellular cu zn superoxide dismutase from Lsiphlebus Testaceipes. Florida Entomological Society Annual Meeting. Paper No. DSP 19. Technical Abstract: A cDNA encoding an extracellular copper/zinc superoxide dismutase (SOD) was cloned and sequenced from the parasitoid Lysiphlebus testaceipes. Evidence for extracellular Cu Zn SODs in insects was first reported in 2004. The protein precursor for L. testaceipes SOD is 172 aa long and contains a 16 aa secretory signal that is cleaved to yield the mature protein. The SODs are antioxidant enzymes that act as catalysts in the conversion of free oxygen radicals to hydrogen peroxide and molecular oxygen. These enzymes protect cellular components from the damaging effects of reactive oxygen species (ROS) and thus may play a role in the ageing process. For parasites such as L. testaceipes, SODs can provide additional protection against oxygen-mediated defense mechanisms of its aphid host; and therefore, may be considered virulence factors. We provide a homology model of the enzyme from L. testaceipes that indicates the structure of extracellular Cu Zn SOD is highly conserved among eukaryotes.