1. Characterization of Salmonella typhi OmpC and OmpF porins engineered with HIV-gp41 epitope on the surface loops.
- Author
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Thulasingam M, Damodharan S, Madhana Vigneshwari G, P J Pandaranayaka E, Elizabeth Hanna L, Usha R, and Krishnaswamy S
- Subjects
- Amino Acid Sequence, Bacterial Proteins genetics, Bacterial Proteins immunology, Binding Sites, Cloning, Molecular, Epitopes genetics, Epitopes immunology, Escherichia coli genetics, Escherichia coli metabolism, Gene Expression, HIV genetics, HIV immunology, HIV Envelope Protein gp41 genetics, HIV Envelope Protein gp41 immunology, HIV Infections immunology, HIV Infections virology, Humans, Immune Sera chemistry, Peptide Library, Porins genetics, Porins immunology, Protein Binding, Protein Conformation, beta-Strand, Protein Engineering, Protein Interaction Domains and Motifs, Protein Multimerization, Recombinant Fusion Proteins chemistry, Recombinant Fusion Proteins genetics, Recombinant Fusion Proteins immunology, Salmonella typhi metabolism, Sequence Alignment, Bacterial Proteins chemistry, Epitopes chemistry, HIV Envelope Protein gp41 chemistry, Porins chemistry, Salmonella typhi genetics
- 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. Proteins 2017; 85:657-664. © 2016 Wiley Periodicals, Inc., (© 2017 Wiley Periodicals, Inc.)
- Published
- 2017
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