Analysis of structures, functions, and epitopes of cysteine protease from Spirometra erinaceieuropaei Spargana.

ABSTRACT: Spirometra erinaceieuropaei cysteine protease (SeCP) in sparganum ES proteins recognized by early infection sera was identified by MALDI-TOF/TOF-MS. The aim of this study was to predict the structures and functions of SeCP protein by using the full length cDNA sequence of SeCP gene with online sites and software programs. The SeCP gene sequence was of 1 053 bp length with a 1011 bp biggest ORF encoding 336-amino acid protein with a complete cathepsin propeptide inhibitor domain and a peptidase C1A conserved domain. The predicted molecular weight and isoelectric point of SeCP were 37.87 kDa and 6.47, respectively. The SeCP has a signal peptide site and no transmembrane domain, located outside the membrane. The secondary structure of SeCP contained 8 α -helixes, 7 β -strands, and 20 coils. T

SUBMITTER: Liu LN 

PROVIDER: S-EPMC3874363 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature