Phospholipase A1-based cross-reactivity among venoms of clinically relevant Hymenoptera from Neotropical and temperate regions

Author(s):Show less -

Perez-Riverol, Amilcar ^[1] ; Romani Fernandes, Luis Gustavo ^[2] ; Musacchio Lasa, Alexis ^[3] ; Aparecido dos Santos-Pinto, Jose Roberto ^[4] ; Abram, Debora Moitinho ^[2] ; Izuka Moraes, Gabriel Hideki ^[1] ; Jabs, Frederic ^[5] ; Miehe, Michaela ^[5] ; Seismman, Henning ^[6] ; Palma, Mario Sergio ; de Lima Zollner, Ricardo ; Spillner, Edzard ^[5] ; Brochetto-Braga, Marcia Regina ^{[1, 7]}

Affiliation

^[1] Univ Estadual Paulista, LBMA IBRC UNESP, Av 24-A, 1515, BR-13506900 Rio Claro, SP - Brazil

^[2] Univ Estadual Campinas, Lab Imunol Translac, FCM, UNICAMP, Rua Vital Brasil 300, Cidade Univ Zeferino Vaz, BR-13083887 Campinas, SP - Brazil

^[3] Ctr Genet Engn & Biotechnol, Biomed Res Div, Syst Biol Dept, Ave 31, E-158 & 190, POB 6162, Havana 10600 - Cuba

^[4] Univ Estadual Paulista, CEIS IBRC UNESP, Av 24-A, 1515, BR-13506900 Rio Claro, SP - Brazil

^[5] Aarhus Univ, Dept Engn, Immunol Engn, Gustav Wieds Vej 10, DK-8000 Aarhus C - Denmark

^[6] Euroimmun AG, Seekamp 21, Lubeck - Germany

^[7] Univ Estadual Paulista, CEVAP, Rua Jose Barbosa de Barros 1780, BR-18610307 Botucatu, SP - Brazil

• Document type: Journal article
• Source: Molecular Immunology; v. 93, p. 87-93, JAN 2018.
• Web of Science Citations: 6

Abstract

Molecular cross-reactivity caused by allergen homology or cross-reactive carbohydrate determinants (CCDs) is a major challenge for diagnosis and immunotherapy of insect venom allergy. Venom phospholipases A1 (PLA1s) are classical, mostly non-glycosylated wasp and ant allergens that provide diagnostic benefit for differentiation of genuine sensitizations from cross-reactivity. As CCD-free molecules, venom PLA1s are not causative for CCD-based cross-reactivity. Little is known however about the protein-based cross-reactivity of PLA1 within vespid species. Here, we address PLA1-based cross-reactivity among ten clinically relevant Hymenoptera venoms from Neotropical and temperate regions including Polybia paulista (paulistinha) venom and Vespula vulgaris (yellow jacket) venom. In order to evaluate cross-reactivity, sera of mice sensitized with recombinant PLA1 (rPoly p 1) from P. paulista wasp venom were used. Pronounced IgE and IgG based cross-reactivity was detected for wasp venoms regardless the geographical region of origin. The cross-reactivity correlated well with the identity of the primary sequence and 3-D models of PLA1 proteins. In contrast, these mice sera showed no reaction with honeybee (HBV) and fire ant venom. Furthermore, sera from patients monosensitized to HBV and fire ants did not recognize the rPoly p 1 in immunoblotting. Our findings reveal the presence of conserved epitopes in the PLA1s from several clinically relevant wasps as major cause of PLA1-based in vitro cross-reactivity. These findings emphasize the limitations but also the potential of PLA1-based HVA diagnostics. (AU)

• FAPESP's process: 13/26451-9 - Bioprospecting and Structural Analysis of the Silk Proteins of Arthropods by a Proteomics Approach Using nanoLC-ESI-CID/ETD System
• Grantee: José Roberto Aparecido dos Santos-Pinto
• Support Opportunities: Scholarships in Brazil - Post-Doctoral
• FAPESP's process: 14/13936-7 - Allergens from venom of the social wasp Polybia paulista (Hymenoptera, Vespidae): recombinant expression in yeast for improved diagnosis and specific immunotherapy to Hymenoptera venom allergy
• Grantee: Márcia Regina Brochetto Braga
• Support Opportunities: Regular Research Grants
• FAPESP's process: 11/51684-1 - System biology as experimental strategy for discovery of novel natural products in the fauna of venomous arthropods from São Paulo State
• Grantee: Mario Sergio Palma
• Support Opportunities: BIOTA-FAPESP Program - Thematic Grants