Project description:Spiders have distinct capture prey behaviors selected along Araneae´s evolutive history, but mainly based on the use of venom for prey paralysis. Uloboridae spiders lost the venom glands secondarily in evolution. Due to that they extensively wrap prey with silk to paralyze and begin digestion. During the extra-oral digestion, the digestive fluid very efficiently performs the liquefaction of both the prey and the AcSp2 spidroins from the web fibers. Despite the efficiency of this process, the cocktail of enzymes involved in digestion in Uloboridae spiders is unknown. In this study, we evaluated the protein content in the midgut of Uloborus sp. using enzymatic, proteomic, and phylogenetic analysis approaches. Hydrolases as peptidases (endo and exopeptidases: cysteine, serine and metallopeptidases), carbohydrases (alpha-amylase, chitinase, alpha-mannosidase), and lipases were biochemically assayed; 50 proteins, annotated as enzymes, structural proteins, and toxins, were identified. This is the first characterization of the molecules involved in the digestive process and the midgut protein content of a nonvenomous spider.
Project description:The venom proteomes of three medically important Nigerian Elapidae snakes Naja haje, Naja katiensis and Naja nigricollis was studied using Hydrophilic Interaction Liquid Chromatography (HILIC) coupled with LC-MS/MS analysis. Peptides/Proteins were identified and characterised using the SEQUEST and X!Tandem algorithms incorporated on to the Scaffold proteome software version 4.10.0. The Nigerian elapid species studied displayed about 70% similarity in composition of their venoms.
Project description:True cobras of the genus Naja are venomous snakes with particular medical importance in Africa and Asia. The Cape cobra Naja nivea is one of the most toxic of the African true cobras, but the composition of its venom has rarely been investigated using proteomics methods.
Project description:Venoms of Naja mossambica and Naja nigricincta nigricincta were analysed in order to identify the proteins. Samples were run on SDS-PAGE gel or analysed without digestion.