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Updated: May 27, 2026

Cercarial Transformation and in vitro Cultivation of Schistosoma mansoni Schistosomules
Published on: August 16, 2011
Evolutionary histories of expanded peptidase families in Schistosoma mansoni
Larissa Lopes Silva1, Marina Marcet-Houben, Adhemar Zerlotini
1Grupo de Genômica e Biologia Computacional, Instituto Nacional de Ciência e Tecnologia em Doenças Tropicais, Belo Horizonte, MG, Brasil.
Abstract:
Schistosoma mansoni is one of the three main causative agents of human schistosomiasis, a major health problem with a vast socio-economic impact. Recent advances in the proteomic analysis of schistosomes have revealed that peptidases are the main virulence factors involved in the pathogenesis of this disease. In this context, evolutionary studies can be applied to identify peptidase families that have been expanded in genomes over time in response to different selection pressures. Using a phylogenomic approach, we searched for expanded endopeptidase families in the S. mansoni predicted proteome with the aim of contributing to the knowledge of such enzymes as potential therapeutic targets. We found three endopeptidase families that comprise leishmanolysins (metallopeptidase M8 family), cercarial elastases (serine peptidase S1 family) and cathepsin D proteins (aspartic peptidase A1 family). Our results suggest that the Schistosoma members of these families originated from successive gene duplication events in the parasite lineage after its diversification from other metazoans. Overall, critical residues are conserved among the duplicated genes/proteins. Furthermore, each protein family displays a distinct evolutionary history. Altogether, this work provides an evolutionary view of three S. mansoni peptidase families, which allows for a deeper understanding of the genomic complexity and lineage-specific adaptations potentially related to the parasitic lifestyle.
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