Characterization of Salmonella typhi OmpC and OmpF porins engineered with HIV-gp41 epitope on the surface loops.

Thulasingam, M .; Damodharan, S .; Vigneshwari, G.M .; Pandaranayaka, E.P .; Hanna, L.E . Usha, R .; Krishnaswamy, S.

Proteins; 2017; 85; 657-664.

Abstract: Porins form trimers in the outer membrane and help transport nutrients and waste products across the bacterial cell membrane. Porin loops are suitable candidates as display systems due to their high immunogenicity and presentation at the bacterial cell surface. In this study, Salmonella typhi porins (OmpC and OmpF) engineered with the Kennedy peptide from gp41 of HIV were characterised. The chimeric OmpC carrying the Kennedy peptide in loop7 did not trimerise, whereas the chimeric OmpF with the epitope in loop5 formed trimers and also was recognised by the antibodies in the HIV patient serum. The results suggest that chimeric S. typhi OmpF may be taken further as a potential candidate to develop as an epitope display system.

Keywords: Display system; Kennedy peptide; membrane protein; chimeric protein; trimer.

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