Hyperalgesic and edematogenic effects of peptides isolated from the venoms of honeybee (Apis mellifera) and neotropical social wasps (Polybia paulista and Protonectarina sylveirae)
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Stings by bees and wasps, including Brazilian species, are a severe public health problem. The local reactions observed after the envenoming includes typical inflammatory response and pain. Several studies have been performed to identify the substances, including peptides that are responsible for such phenomena. The aim of the present study is to characterize the possible nociceptive (hyperalgesic) and edematogenic effects of some peptides isolated from the venoms of the honeybee (Apis mellifera) and the social wasps Polybia paulista and Protonectarina sylveirae, in addition to characterize some of the mechanisms involved in these phenomena. For this purpose, different doses of the peptides mellitin (Apis mellifera), Polybia-MP-I, N-2-Polybia-MP-I (Polybia paulista), Protonectarina-MP-NH2 and Protonectarina-MP-OH (Protonectarina sylveirae) were injected into the hind paw of mice. Hyperalgesia and edema were determined after peptide application, by using an electronic von Frey apparatus and a paquimeter. Carrageenin and saline were used as controls. Results showed that melittin, Polybia-MP-I, N-2-Polybia-MP-I, Protonectarina-MP-NH2 and Protonectarina-MP-OH peptides produced a dose- and time-related hyperalgesic and edematogenic responses. Both phenomena are detected 2 h after melittin, Polybia-MP-I, N-2-Polybia-MP-I injection; their effects lasted until 8 h. In order to evaluate the role of prostanoids and the involvement of lipidic mediators in hyperalgesia induced by the peptides, indomethacin and zileuton were used. Results showed that zileuton blocked peptide-induced hyperalgesia and induced a decrease of the edematogenic response. On the other hand, indomethacin did not interfere with these phenomena. These results indicate that melittin, Polybia-MP-I, N-2-Polybia-MP-I, Protonectarina-MP-NH2, and Protonectarina-MP-OH peptides could contribute to inflammation and pain induced by insect venoms.
KeywordsHyperalgesia Inflammation Apis mellifera Polybia paulista Protonectarina sylveirae Peptides
This research is supported by grants from FAPESP (BIOprospecTA Proc. 04/07942-2, 06/57122-6), CNPq, Instituto Nacional de Ciência e Tecnologia em Imunologia (INCT/CNPq-MCT) and Coordenação de Aperfeiçoamento de Nível Superior—Projeto NanoBiotec (CAPES). MSP and YC are researchers for the Brazilian Council for Scientific and Technological Development (CNPq).
- Castro FFM, Palma MS (2009) Alergia a venenos de insetos. Manole, BrasilGoogle Scholar
- Chan WC, White PD (2004) Fmoc solid phase peptide synthesis: a practical approach. Oxford University Press, CambridgeGoogle Scholar
- Hirai Y, Yasuhara T, Yoshida H, Nakajima T, Fujino M, Kitada C (1979) A new mast cell degranulating peptide “mastoparan” in the venom of Vespula lewisii. Chem Pharm Bull (Tokyo) 27:1942–1944Google Scholar
- Horizoe T, Nagakura N, Chiba K, Shirota H, Shinoda M, Kobayashi N, Numata H, Okamoto Y, Kobayashi S (1998) ER-34122, a novel dual 5-lipoxygenase/cyclooxygenase inhibitor with potent anti-inflammatory activity in an arachidonic acid-induced ear inflammation model. Inflamm Res 47:375–383CrossRefPubMedGoogle Scholar
- Konno K, Hisada M, Fontana R, Lorenzi CC, Naoki H, Itagaki Y, Miwa A, Kawai N, Nakata Y, Yasuhara T, Ruggiero Neto J, de Azevedo WF Jr, Palma, Nakajima T (2001) Anoplin, a novel antimicrobial peptide from the venom of the solitary wasp Anoplius samariensis. Biochim Biophys Acta 1550:70–80PubMedGoogle Scholar
- Maguire (1998) Ectoparasite infestations and arthropod bites and stings. In: Fauci AS (ed) Harrison’s principles of internal medicine. McGraw Hill Health Professions Divisions, New York, pp 2548–2554Google Scholar
- Nakajima T (1986) Pharmacological biochemistry of vespid venoms. In: Piek T (ed) Venom of Hymenoptera Academic Press, London, pp 309–327Google Scholar
- Son DJ, Kang J, Kim TJ, Song HS, Sung KJ, Yun do Y, Hong JT (2007) Melittin, a major bioactive component of bee venom toxin, inhibits PDGF receptor beta-tyrosine phosphorylation and downstream intracellular signal transduction in rat aortic vascular smooth muscle cells. J Toxicol Environ Health A 70:1350–1355CrossRefPubMedGoogle Scholar