Analysis of structure, function and epitopes of Spirometra erinaceieuropaei casein kinase I

ABSTRACT

Spirometra erinaceieuropaei casein kinase I (SeCKI) was analyzed using bioinformatical methods to predict its structure and function based on the deduced amino acid sequence from full length cDNA sequence of SeCKI gene with online sites and software programs. The longest open reading frame contains 448 amino acids, 50 kDa and theoretical pI of 4.73, with a complete tubulin domain, a SMART tubulin_C domain and a low complexity region. SeCKI has no signal sequence and no transmembrane domain, but is predicted to be located extracellularly. The secondary structure of SeCKI contains 12 α-helixes, 11 β-strands and 22 coils. SeCKI had 19 potential antigenic epitopes and 25 HLA-I restricted epitopes. Based on phylogenetic analysis of SeCKI sequence, S. erinaceieuropaei has the closest evolutionary status with Hymenolepis microstoma. Information from this study could provide important insights into the identification of diagnostic antigens and molecular targets of antisparganum drugs.