Sequence similarity-based proteomics in insects: characterization of the larvae venom of the Brazilian moth Cerodirphia speciosa.
Using a combination of tandem mass spectrometric sequencing and sequence similarity searches, we characterized the larvae venom of the moth Cerodirphia speciosa, which belongs to the Saturniidae family of the Lepidoptera order. Despite the paucity of available database sequence resources, the approach enabled us to identify 48 out of 58 attempted spots on its two-dimensional gel electrophoresis map, which represented 37 unique proteins, whereas it was only possible to identify 13 proteins by conventional non-error tolerant database searching methods. The majority of cross-species hits were made to proteins from the phylogenetically related Lepidoptera organism, the silk worm Bombyx mori. The protein composition of the venom suggested that envenoming by C. speciosa toxins might proceed through the contact with its hemolymph, similarly to another toxic Lepidoptera organism, Lonomia obliqua.
Shevchenko
Anna
A
Max Planck Institute of Molecular Cell Biology and Genetics, Pfotenhauerstrasse 108, 01307 Dresden, Germany.
de Sousa
Mirta Mittelstedt Leal
MM
Waridel
Patrice
P
Bittencourt
Silvia Tolfo
ST
de Sousa
Marcelo Valle
MV
Shevchenko
Andrej
A
D000818:Animals; D001180:Arthropod Venoms / Q000737:chemistry*; D019295:Computational Biology; D015180:Electrophoresis, Gel, Two-Dimensional; D019476:Insect Proteins / Q000032:analysis*; D007814:Larva; D009036:Moths; D010802:Phylogeny; D040901:Proteomics / Q000379:methods*; D017386:Sequence Homology, Amino Acid
D001180:Arthropod Venoms; D019476:Insect Proteins