Composition and Acute Inflammatory Response from Tetraponera rufonigra Venom on RAW 264.7 Macrophage Cells

• Published in: Toxins Vol. 13; no. 4; p. 257
• Main Authors: Naephrai, Suwatjanee, Khacha-Ananda, Supakit, Pitchakarn, Pornsiri, Jaikang, Churdsak
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 03.04.2021; MDPI
• Subjects: Acids; Allergens; Aminopeptidase; Anaphylaxis; Cell cycle; Composition; COX-2/mPGES-1 pathway; Cyclooxygenase-2; Cytotoxicity; Endopeptidases; Enzymes; hymenoptera; Inflammation; Inflammatory response; Macrophages; Nucleotidase; Phospholipase A2; Prolyl oligopeptidase; Prostaglandin E2; Prostaglandin-E synthase; Protein composition; Proteins; Tetraponera rufonigra; Trypsin; Venom; Thailand; inflammation; hymenoptera; COX-2/mPGES-1 pathway
• ISSN: 2072-6651; 2072-6651
• DOI: 10.3390/toxins13040257

(Arboreal Bicoloured Ant) venom induces pain, inflammation, and anaphylaxis in people and has an increased incident in Southeast Asia regions. The bioactive components and mechanism of action of the ant venom are still limited. The aim of this research was to identify the protein composition and inflammatory process of the ant venom by using RAW 264.7 macrophage cells. The major venom proteins are composed of 5' nucleotidase, prolyl endopeptidase-like, aminopeptidase N, trypsin-3, venom protein, and phospholipase A (PLA ). The venom showed PLA activity and represented 0.46 μg of PLA bee venom equivalent/μg crude venom protein. The venom induced cytotoxic in a dose- and time-dependent manner with IC approximately at 4.01 µg/mL. The increased levels of COX-2 and PGE were observed after 1 h of treatment correlating with an upregulation of expression. Moreover, the level of expression was obviously increased after 12 h of venom induction. Hence, our results suggested that the induction of pathway could be a direct pathway for the ant venom-induced inflammation.