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. 2021 May 28;7(6):423.
doi: 10.3390/jof7060423.

Prospecting Biomarkers for Diagnostic and Therapeutic Approaches in Pythiosis

Jéssica Luana Chechi  1 , Tiwa Rotchanapreeda  2 , Giselle Souza da Paz  3 , Ana Carolina Prado  1 , Alana Lucena Oliveira  3 , José Cavalcante Souza Vieira  1 , Marília Afonso Rabelo Buzalaf  4 , Anderson Messias Rodrigues  5 , Lucilene Delazari Dos Santos  6   7 , Theerapong Krajaejun  2 , Sandra de Moraes Gimenes Bosco  1   3
Affiliations

Prospecting Biomarkers for Diagnostic and Therapeutic Approaches in Pythiosis

Jéssica Luana Chechi et al. J Fungi (Basel). .

Abstract

Pythiosis, whose etiological agent is the oomycete Pythium insidiosum, is a life-threatening disease that occurs mainly in tropical and subtropical countries, affecting several animal species. It is frequently found in horses in Brazil and humans in Thailand. The disease is difficult to diagnose because the pathogen's hyphae are often misdiagnosed as mucoromycete fungi in histological sections. Additionally, there is no specific antigen to use for rapid diagnosis, the availability of which could improve the prognosis in different animal species. In this scenario, we investigated which P. insidiosum antigens are recognized by circulating antibodies in horses and humans with pythiosis from Brazil and Thailand, respectively, using 2D immunoblotting followed by mass spectrometry for the identification of antigens. We identified 23 protein spots, 14 recognized by pooled serum from horses and humans. Seven antigens were commonly recognized by both species, such as the heat-shock cognate 70 KDa protein, the heat-shock 70 KDa protein, glucan 1,3-beta-glucosidase, fructose-bisphosphate aldolase, serine/threonine-protein phosphatase, aconitate hydratase, and 14-3-3 protein epsilon. These results demonstrate that there are common antigens recognized by the immune responses of horses and humans, and these antigens may be studied as biomarkers for improving diagnosis and treatment.

Keywords: Pythium insidiosum; antigens; diagnosis; immunoproteomics; pythiosis; therapy.

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Conflict of interest statement

The authors declare no conflict of interest. The funders had no role in the design of the study; in the collection, analyses, or interpretation of data; in the writing of the manuscript, or in the decision to publish the results.

Figures

Figure 1
Figure 1
The 2D protein profile of the Eq-10 isolate of Pythium insidiosum (A,C). Identification of immunoreactive proteins from P. insidiosum by 2D Western blot analysis in pooled horse sera (B) and pooled human sera (D). The numbers of the spots refer to the identification used in Table 1 and Table 2. The experiments were run in triplicate.
Figure 2
Figure 2
STRING analysis of the Pythium insidiosum immunoproteome. (A) The STRING protein–protein interaction network for the 16 immunogenic proteins in human and equine pythiosis. The proteins shared between the two immunoproteomes are marked with an asterisk. Colored lines between the proteins indicate the various types of interaction evidence. (B) Classification of proteins based on the KEGG pathways. The protein–protein interactions’ enrichment p-value = 3.47 × 10−6.
Figure 3
Figure 3
Prediction of the six antigens (A–F) of higher antigenic propensity scores. According to the algorithm COBEpro, the antigenic propensity scores are plotted against position along the amino acid sequence. The higher the antigenic propensity scores, the more likely there is to be antigenic activity for the respective region.
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