Novel acidic phospholipase A2 from Porthidium hyoprora causes inflammation with mast cell rich infiltrate

Abstract

Phospholipases A2 (PLA2) are a group of enzymes that hydrolyze phospholipids at the sn-2 position, being present in all nature. In venomous animals, these proteins assume a special role, being able to exert diverse pharmacological effects. In this work, authors identified a new isoform of PLA2 in the venom of Porthidium hyoprora, which was isolated through sequential chromatographic steps and named PhTX-III. The enzyme was characterized biochemically and structurally. Structural studies using mass spectrometry confirmed an acidic secretory PLA2, family IIA, with molecular mass of 13,620.9 Da and identification of 86% of its primary sequence. PhTX-III did not exhibit myotoxic, anticoagulant or antibacterial effects, often present in this class of enzymes. Although, it was capable of initiate inflammatory response, with local edema and release of cytokines IL-1α, IL-6 and TNF-α, probably due to mast cell degranulation.

Proteomic Investigations of Two Pakistani Naja Snake Venoms Species Unravel the Venom Complexity, Posttranslational Modifications, and Presence of Extracellular Vesicles

“…Despite the fact that acidic PLA 2 s are found abundantly in the snake venom, their role is poorly understood [ 81 ]. In spite of having high catalytic activity as compared to basic PLA 2 s, they do not induce toxicity [ 82 ]. Studies have suggested acidic PLA 2 s to participate in prey digestion [ 83 ].…”

ACP-TX-I and ACP-TX-II, Two Novel Phospholipases A2 Isolated from Trans-Pecos Copperhead Agkistrodon contortrix pictigaster Venom: Biochemical and Functional Characterization

“…Using this purification method, several other PLA 2 (Bp13 PLA 2 , PhTX-I, -II,-III, Bleu-PLA 2 , Bbil-TX, BbTX-II, -III, etc.) from different venoms have been purified, showing that it is rapid and efficient for the purification of these proteins in one step [6,7,8,35,36,37,38].…”

Analysis of Protein Composition and Bioactivity of Neoponera villosa Venom (Hymenoptera: Formicidae)

“…A phospholipase A2 was identified from spot 123. This enzyme, widely distributed in several venoms, destroys phospholipids in biological membranes, leading to the formation of pores, cell lysis and tissue damage [ 33 ], inducing inflammation [ 54 ], and inhibiting the activity of macrophages [ 55 ]. The presence of the enzyme in the venom can be related to hemolytic activity and to inhibition of NO formation by macrophages.…”