[Molecular mimicry between human thyroid peroxidase, thyroglobulin, cosinophil peroxidase, IL-24 and microorganisms antigens].
Autor: | Sánchez A; Faculty of Health, Medical Research Group (GINUMED), Rafael Nuñez University Corporation, Cartagena, Colombia.; Group of Clinical and Experimental Allergy (GACE), IPS Universitaria, University of Antioquia, Medellín, Colombia. andres.sanchez@curnvirtual.edu.co., García V; Faculty of Health, Medical Research Group (GINUMED), Rafael Nuñez University Corporation, Cartagena, Colombia., Emiliani-Navarro YM; Faculty of Health, Medical Research Group (GINUMED), Rafael Nuñez University Corporation, Cartagena, Colombia., Sánchez J; Group of Clinical and Experimental Allergy (GACE), IPS Universitaria, University of Antioquia, Medellín, Colombia., Ramos-Gomez JC; Faculty of Health, Medical Research Group (GINUMED), Rafael Nuñez University Corporation, Cartagena, Colombia., González-Rangel SK; Faculty of Health, Medical Research Group (GINUMED), Rafael Nuñez University Corporation, Cartagena, Colombia., Munera-Gomez M; Faculty of Health, Medical Research Group (GINUMED), Rafael Nuñez University Corporation, Cartagena, Colombia. |
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Jazyk: | Spanish; Castilian |
Zdroj: | Revista alergia Mexico (Tecamachalco, Puebla, Mexico : 1993) [Rev Alerg Mex] 2024 Feb 01; Vol. 71 (1), pp. 57. Date of Electronic Publication: 2024 Feb 01. |
DOI: | 10.29262/ram.v71i1.1376 |
Abstrakt: | Objective: Identify molecular mimicry between TPO, eosinophil peroxidase (EPX), thyroglobulin and IL24 and microorganism antigens. Methods: Through in silico analysis, we performed local alignments between human and microorganism antigens with PSI-BLAST. Proteins that did not present a 3D structure were modeled by homology through the Swiss Modeller server and epitope prediction was performed through Ellipro. Epitopes were located in the 3D models using PYMOL software. Results: A total of 38 microorganism antigens (parasites, bacteria) had identities between 30% and 45%, being the highest with Anisakis simplex. The alignment between 2 candidate proteins from A. simplex and EPX presented significant values, with identities of 43 and 44%. In bacteria, Campylobacter jejuni presented the highest identity with thyroglobulin (35%). 220 linear and conformational epitopes of microorganism antigens were predicted. Peroxidasin-like proteins from Toxocara canis and Trichinella pseudospiralis presented 10 epitopes similar to TPO and EPX, as possible molecules triggering cross-reactivity. No virus presented identity with the human proteins studied. Conclusion: TPO and EPX antigens shared potential cross-reactive epitopes with bacterial and nematode proteins, suggesting that molecular mimicry could be a mechanism that explains the relationship between infections and urticaria/hypothyroidism. In vitro work is needed to demonstrate the results obtained in the in silico analysis. |
Databáze: | MEDLINE |
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