Proteomic characterization of the multiple forms of the PLAs from the venom of the social wasp Polybia paulista

Abstract

The phospholipases A(1) (PLA(1) s) from the venom of the social wasp Polybia paulista occur as a mixture of different molecular forms. To characterize the molecular origin of these structural differences, an experimental strategy was planned combining the isolation of the pool of PLAs from the wasp venom with proteomic approaches by using 2-D, MALDI-TOF-TOF MS and classical protocols of protein chemistry, which included N- and C-terminal sequencing. The existence of an intact form of PLA(1) and seven truncated forms was identified, apparently originating from controlled proteolysis of the intact protein; in addition to this, four of these truncated forms also presented carbohydrates attached to their molecules. Some of these forms are immunoreactive to specific-IgE, while others are not. These observations permit to raise the hypothesis that naturally occurring proteolysis of PLA(1) , combined with protein glycosylation may create a series of different molecular forms of these proteins, with different levels of allergenicity. Two forms of PLA(2) s, apparently related to each other, were also identified; however, it was not possible to determine the molecular origin of the differences between both forms, except that one of them was glycosylated. None of these forms were immunoreactive to human specific IgE.

Proteomic analysis of the venom of the predatory ant Pachycondyla striata (Hymenoptera: Formicidae)

“…In the venom of P. striata , two different PLs are present: basic PLA2 vurtoxin and venom PLA1 2. The PLA1 and PLA2 catalyze the specific hydrolysis of ester bonds of 1,2‐diacyl‐3‐sn glycerophospholipids in the positions sn‐1 and sn‐2, respectively, converting these substrates into their corresponding lyso‐associated compounds with the release of fatty acids (Santos et al., )…”

“…PLA2 is among the most common PL found in ant venom (Touchard et al., ), and has been described in the venom of different species (Pinto et al., ; Santos et al., ; Schmidt & Blum, ; Touchard et al., ), whereas PLA1 has been described in several Hymenoptera venoms (Hoffman, ; King, Lu, Gonzalez, Qian, & Soldatova, ; Pinto et al., ). Venom PL from various animals have been described as a potent venom allergen (Lima & Brochetto‐Braga, ) with neurotoxic, platelet activation, hemolysis, and tissue damage effects (Pinto et al., ; Touchard et al., ).…”

“…However, ant venoms remain almost unexplored in comparison with other animals (Aili et al., ; Rifflet et al., ; Touchard et al., ). The species of ants with the most well‐characterized venoms are the fire ant Solenopsis invicta and Solenopsis saevissima and Myrmecia pilosula (Santos et al., ; Touchard et al., ).…”

Brown Recluse Spider Venom: Proteomic Analysis and Proposal of a Putative Mechanism of Action

“…Thus, we identified a superoxide dismutase (access code Q9Z5W5), catalase (access code Q65974), a series of proteases inhibitors (access codes P01070, P07385, P20907 and O24383) and the HSP 60-like protein (access code O02649). Superoxide dismutase (SOD) is an antioxidant enzyme that converts superoxide molecules to hydrogen peroxide, which is then degraded to water and oxygen by catalase [61]. Apparently, these enzymes seem to play a critical role in protecting the stored venom from oxidative stresses and/or the redox environment of venom in a more general way.…”

Profiling the short, linear, non-disulfide bond-containing peptidome from the venom of the scorpion Tityus obscurus

“…A detailed characterization of animal venom based on the profiling of proteomics and peptidomics has been performed using mass spectrometric analysis. The use of LC-MS and MS/MS has been crucial for detection, sequencing, and identification of the rich composition of peptides/proteins from animal venom, contributing to the assignment of the global proteopeptidomic profiles of various Arthropod venoms such as social wasps [11,[26][27][28][29], ants [30], honeybees [31], and spiders [32,33]. The assignment of the proteome complement from scorpion venom has also benefited from the use of mass spectrometric analysis; a detailed analysis of Tityus spp.…”