Comparative genomic analysis of aspartic proteases in eight parasitic platyhelminths: Insights into functions and evolution

• Some evidence implied gene loss events in family A01 along the class Cestoda.
• Members in family A22 were evolutionarily highly conserved among the parasites.
• One retroviral-like AP has potential to be inhibited by HIV protease inhibitors.
• Retrotransposon-associated APs were extensively expanded across the parasites.

We performed genome-wide identifications and comparative genomic analyses of the predicted aspartic proteases (APs) from eight parasitic flatworms, focusing on their evolution, potentials as drug targets and expression patterns. The results revealed that: i) More members of family A01 were identified from the schistosomes than from the cestodes; some evidence implied gene loss events along the class Cestoda, which may be related to the different ways to ingest host nutrition; ii) members in family A22 were evolutionarily highly conserved among all the parasites; iii) one retroviral-like AP in family A28 shared a highly similar predicted 3D structure with the HIV protease, implying its potential to be inhibited by HIV inhibitor-like molecules; and iiii) retrotransposon-associated APs were extensively expanded among these parasites. These results implied that the evolutionary histories of some APs in these parasites might relate to adaptations to their parasitism and some APs might have potential serving as intervention targets.