Wednesday, 29 October 2003
D0483

This presentation is part of : Display Presentations, Section B. Physiology, Biochemistry, Toxicology, and Molecular Biology

Proteomic analysis Spodoptera frugiperda peritrophic matrix proteins

Tibor Pechan and Dawn S. Luthe. Mississippi State University, Biochemistry and Molecular Biology, Box 9650, Mississippi State, MS

We have shown that the peritrophic matrix (PM) of Spodoptera frugiperda (fall armyworm) larvae fed on insect resistant corn lines, or cell culture lines expressing a unique 33-kD cysteine protease appears to be cracked and torn. To determine if this damage is due to degradation of all, or a few PM proteins, we have undertaken the proteomic analysis of PMs dissected from larvae fed on resistant or susceptible plants, and artificial diet. The initial 2-D electrophoresis analysis of PM proteins from larvae fed on artificial diet indicated that approximately 30 proteins were visible on Commassie Blue-stained gels. Four proteins were selected for identification by MALDI-TOF-MS analysis. Tentative matches for two spots were found in the Drosophila genome. One spot (TrMBL Q9VV46) was most similar to insect cuticle chitin-binding proteins and the other spot (TrMBL Q9VRJ9) shared some similarity with an OTU (ovarian tumor)-like cysteine proteinase. Changes in the PM proteome in response to insect diet will be investigated.



Species 1: Lepidoptera Noctuidae Spodoptera frugiperda (fall armyworm)
Keywords: peritrophic matrix, proteomics

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