Analysis of Structures, Functions, and Epitopes of Aminopeptidase from Trichinella spiralis
- Author:
Zhang, Y.L., , Zhang, H.W., Zhang, X., Liu, L.N., Liu, R.D., Xu, B.L., Wang, Z.Q., Cui, J.
- Publication Type:Journal Article
- From:Tropical Biomedicine
2015;32(4):776-782
- CountryMalaysia
- Language:English
-
Abstract:
We have previously reported that the recombinant T. spiralis aminopeptidase
(rTsAP) could induce a partial protective immunity against T. spiralis infection in mice. The
aim of this study was to predict the structures and functions of TsAP protein by using the full
length cDNA sequence of TsAP gene. TsAP sequence was 1515 bp length with a 1515 bp
biggest ORF encoding 504-amino acid protein. The molecular weight and isoelectric point of
TsAP were 54.7 kDa and 6.69, respectively. TsAP structure domains contained a
Peptidase_M17_N and a Peptidase_M17 domain, which has the function of catalysis of the
hydrolysis of N-terminal amino acid residues. TsAP had no signal peptide site and transmembrane
domain, and located in cytoplasm. The secondary structure of TsAP contained 16 α-helix, 14
β-strand and 29 coils. The TsAP had 11 and 21 potential antigenic epitopes of T cell and B cell,
respectively. Based on the phylogenetic analyses of TsAP, T. spiralis have the closest
relationship with Plasmodium falciparum. TsAP was a kind of proteolytic enzyme with a
variety of biological functions and its antigenic epitopes could provide important insights on
the diagnostic antigens and target molecular of anti-Trichinella drugs
- Full text:W020160112365964819383.pdf
