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A comparison of homologous genes encoding aminopeptidases among bird and human Encephalitozoon hellem isolates and a
Paulette F Waters1, Karen F Snowden, Patricia J Holman
1Department of Veterinary Pathobiology, The Texas Veterinary Medical Center, Texas A&M University, College Station, TX 77843-4467, USA.
Abstract:
Encephalitozoon cuniculi and E. hellem are often recognized as the agents of human microsporidiosis, but less than optimal therapy is available for treatment. The identification of enzymes critical to the parasitic life cycle is an important step in finding targets for potential drug development. Aminopeptidase gene sequences were obtained from cDNA and gDNA from avian and human E. hellem isolates and from a rabbit E. cuniculi isolate. At the amino acid level, the aminopeptidase sequences from the E. hellem human and bird isolates share >99% identity and are nearly 70% identical with the E. cuniculi sequence. Conserved HEXXH and GAMEN motifs classify the predicted aminopeptidase in the MA clan of the M1 family. The obtained aminopeptidase gene sequences are likely homologous to the previously reported E. cuniculi glutamyl aminopeptidase. The conservation of this aminopeptidase between species and divergence from mammalian aminopeptidases indicate that this enzyme may be a valid target for drug therapy.
Insights
Encephalitozoon species cause human microsporidiosis with limited treatment options. Researchers identified a conserved aminopeptidase enzyme in these parasites, suggesting it as a potential drug target for developing new therapies.
Area of Science:
- Parasitology
- Drug Discovery
- Molecular Biology
Background:
- Human microsporidiosis is caused by Encephalitozoon species, notably Encephalitozoon cuniculi and Encephalitozoon hellem.
- Current therapeutic options for microsporidiosis are suboptimal, necessitating the development of novel treatment strategies.
Purpose of the Study:
- To identify and characterize enzymes crucial for the parasitic life cycle of Encephalitozoon species.
- To evaluate potential parasitic enzymes as drug targets for treating human microsporidiosis.
Main Methods:
- Acquisition of aminopeptidase gene sequences from cDNA and genomic DNA of Encephalitozoon hellem (avian and human isolates) and Encephalitozoon cuniculi (rabbit isolate).
- Bioinformatic analysis of amino acid sequences to identify conserved motifs and classify the enzyme.
- Comparison of parasitic aminopeptidase sequences with mammalian counterparts.
Main Results:
- High amino acid identity (>99%) was observed between Encephalitozoon hellem isolates and approximately 70% identity with Encephalitozoon cuniculi.
- The identified aminopeptidase contains conserved HEXXH and GAMEN motifs, classifying it within the M1 family (MA clan).
- The enzyme is likely homologous to Encephalitozoon cuniculi glutamyl aminopeptidase and shows significant divergence from mammalian aminopeptidases.
Conclusions:
- The conserved aminopeptidase across Encephalitozoon species represents a promising candidate for antiparasitic drug development.
- Targeting this enzyme could lead to novel therapeutic interventions for human microsporidiosis.
