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Today, transference of recombinant protein on the outer surface of bacteria is deemed as a valuable process for various applications in biotechnology including preparation of vaccines. In this study, Lpp-OmpA structure was used to present outer membrane protein E of  Haemophilus influenzae  on  E. coli  outer membrane. Also, a structure was designed according to Lpp-OmpA based on non-classical secretion pathway using bioinformatics software such as MEMSAT-SVM, ScrotumP and SignalP where it lacked any signal peptide at its N-terminal. Potential of this structure in the presentation of protein E on the surface of  E. coli  through non-classical pathway was indicated by western blotting, SDS page and fluorescent microscopy techniques, similarly its effectiveness was compared with Lpp-OmpA system. The results of the current study showed that the new structure had higher efficiency than Lpp-OmpA, and it could transport protein E on outer membrane well. This study is the first report in the presentation of  H. influenzae  PE onto the surface of  E. coli  by Lpp-OmpA, and the structure originated from Lpp-OmpA, according to the non-classical secretion pathway. Our results suggest that non-classical secretion pathway may be exploited as a new secretory pathway on the outer surface of the cell for recombinant proteins.   Electronic supplementary material  The online version of this article (doi:10.1186/s13568-017-0350-0) contains supplementary material, which is available to authorized users.

Designing novel construction for cell surface display of protein E on Escherichia coli using non-classical pathway based on Lpp-OmpA