In silico design of a novel chimeric shigella IpaB fused to C terminal of clostridium perfringens enterotoxin as a vaccine candidate.

ABSTRACT: This study aimed to design a novel chimeric protein in silico to serve as a serotype-independent vaccine candidate against Shigella. The chimera contains amino acid residues 240-460 of Shigella invasion plasmid antigen B (IpaB) and the C-terminus of Clostridium perfringens enterotoxin (C-CPE). Amino acid sequences of 537 peptide linkers were obtained from two protein linker databases. 3D structures of IpaB-CPE_290-319, IpaB-CPE_184-319, IpaB-CPE_194-319 and 537 newly designed IpaB-linker-CPE_290-319 constructs with varying linker regions were predicted. These predicted 3D structures were merged with the 3D structures of native IpaB_240-460, CPE_194-319, CPE_184-319 and CPE_290-319 to select the structure most s

SUBMITTER: Arabshahi S 

PROVIDER: S-EPMC5972921 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature