Characterizes NDR domain protein in Strongyloides ratti, indicating its potential role in parasite survival.
Introduction: using touchdown reverse transcription polymerase chain reaction (RT-PCR). Materials & Methods: was amplified using Touchdown RT-PCR. Results: SrNDR were grouped together with a strong bootstrap score of 87. Domain search analysis showed an e-value of 1.05e-100 for the conserved NDR1 domain within the a/b hydrolase superfamily protein (pfam03096), spanning amino acid residues 9 to 287. The core domain of SrNDR is folded into 12 alpha-helices surrounded by eight antiparallel b-strands. The three-dimensional structure model of SrNDR (residues 31-319) showed 100% identity to the human protein NDRG1 across 248 amino acids, with 77% sequence coverage. Conclusion: By using this program, we found a prediction of predominantly a-helical (44.86%), Strand (1.08%) and random coil (54.05%) content for the coding sequence of SrNDR. Based on the alignment of this protein with homologous sequences from related nematodes, it may play a vital role in parasite survival within host cells.
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Jolodar Abbas (2025) studied this question.
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