[Molecular mimicry between the major allergen of the centipede (Scolopendra subspinipes) Sco M 5 and proteins from allergenic sources. In silico analysis.]

Objective: To evaluate, through in silico analysis, the cross-reactivity between Sco m 5 and arthropod proteins and to identify potential IgE-binding epitopes.

Methods: The homology between Sco m 5 and 15 arthropod allergens (Vespula, Polistes, Polybia, Solenopsis, Brachyponera, Phoneutria, and Dermatophagoides) was assessed using the ALLERMATCH server for pairwise alignments and PRALINE for multiple alignments. Phylogenetic trees were constructed using Molecular Evo-lutionary Genetics Analysis (MEGA). Epitope prediction was performed with the Ellipro server. Protein visualization was carried out through PyMOL.

Results: The multiple alignment showed 50% identity, and the pairwise alignments between Sco m 5 and arthropod proteins revealed diverse homology. Two linear epitopes and one conformational epitope were identified in Sco m 5, which were highly conserved in the studied arthropod proteins, such as bees, wasps, and ants.

Conclusion: The high homology between Sco m 5 and allergens from other arthropods supports the potential for cross-reactivity. The identification of potential epitopes in conserved regions reinforces this idea and could serve as important targets for therapeutic interventions in allergies triggered by arthropod venoms, especially Scolopendra spp. Further in vitro and in vivo studies are needed to confirm these findings.