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pmid:37999519

Structural Similarities, in Relation with the Cross-Reactivity, of Hymenoptera Allergenic Dipeptidyl Peptidases IV-An Overall Comparison Including a New Dipeptidyl Peptidase IV Sequence from Vespa velutina.

Rafael I Monsalve · Manuel Lombardero · Lars H Christensen · Beatriz Núñez-Acevedo · David González-de-Olano · Miriam Sobrino-García · Rosita M Castillo-Loja · Susana B Bravo · Manuela Alonso-Sampedro · Carmen Vidal

Toxins · 2023 doi:10.3390/toxins15110656

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Structural Similarities, in Relation with the Cross-Reactivity, of Hymenoptera Allergenic Dipeptidyl Peptidases IV-An Overall Comparison Including a New Dipeptidyl Peptidase IV Sequence from Vespa velutina.
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Rafael I Monsalve
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Manuel Lombardero
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Lars H Christensen
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Beatriz Núñez-Acevedo
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David González-de-Olano
[5]
Miriam Sobrino-García
[6]
Rosita M Castillo-Loja
[7]
Susana B Bravo
[8]
Manuela Alonso-Sampedro
[9]
Carmen Vidal
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Toxins
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2023
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(1) Background: Dipeptidyl Peptidases IV (DPPIVs), present in many organisms, are minor components in the venoms of Hymenoptera, where they have been identified as cross-reactive allergenic molecules. Considering that the structure of homologous DPPIVs is well characterized, we aimed to explain which regions have higher similarity among these proteins and present a comparison among them, including a new Vespa velutina DPPIV sequence. Moreover, two cases of sensitization to DPPIVs in wasp- and honeybee-sensitized patients are presented. (2) Methods: Proteomic analyses have been performed on the venom of the Asian hornet Vespa velutina to demonstrate the sequence of its DPPIV (allergen named Vesp v 3, with sequence accession number P0DRB8, and with the proteomic data available via ProteomeXchange with the identifier PXD046030). A comparison performed through their alignments and analysis of the three-dimensional structure showed a region with higher similarity among Hymenoptera DPPIVs. Additionally, ImmunoCAP™ determinations (including specific inhibition experiments), as well as IgE immunoblotting, are performed to demonstrate the allergenicity of Api m 5 and Ves v 3. (3) Results and Conclusions: The data presented demonstrate that the similarities among Hymenoptera DPPIVs are most likely localized at the C-terminal region of these enzymes. In addition, a higher similarity of the Vespa/Vespula DPPIVs is shown. The clinical cases analyzed demonstrated the allergenicity of Api m 5 and Ves v 3 in the sera of the allergic patients, as well as the presence of this minor component in the preparations used in venom immunotherapy.
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Structural Similarities on Hymenoptera Allergenic Dipeptidyl Peptidases IV (DPPIVs). Overall comparison also including a new DPPIV sequence from Vespa velutina.
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