Analysis of structure, function and epitopes of Spirometra erinaceieuropaei casein kinase I
- Author:
Liu, L.N
;
Wang, Z.Q
;
Zhang, X
;
Jiang, P
;
Zhang, Z.F
;
Zhang, G.Y
;
Cui, J.
- Publication Type:Journal Article
- From:Tropical Biomedicine
2015;32(1):167-175
- CountryMalaysia
- Language:English
-
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.
- Full text:W020150520329430934365.pdf
