title: Characterization of Salmonella typhi OmpC and OmpF porins engineered with HIV-gp41 epitope on the surface loops.
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.
authors.affiliation: School of Biotechnology, Madurai Kamaraj University, Madurai, 625021, India.
authors.forename: Madhuranayaki
authors.initials: M
authors.lastname: Thulasingam
authors.affiliation: School of Biotechnology, Madurai Kamaraj University, Madurai, 625021, India.
authors.forename: Subha
authors.initials: S
authors.lastname: Damodharan
authors.affiliation: School of Biotechnology, Madurai Kamaraj University, Madurai, 625021, India.
authors.forename: Gopal
authors.initials: G
authors.lastname: Madhana Vigneshwari
authors.affiliation: School of Biotechnology, Madurai Kamaraj University, Madurai, 625021, India.
authors.forename: Eswari
authors.initials: E
authors.lastname: P J Pandaranayaka
authors.affiliation: National Institute for Research in Tuberculosis, Indian Council of Medical Research, Chennai, 600031, India.
authors.forename: Luke
authors.initials: L
authors.lastname: Elizabeth Hanna
authors.affiliation: School of Biotechnology, Madurai Kamaraj University, Madurai, 625021, India.
authors.forename: Ramakrishnan
authors.initials: R
authors.lastname: Usha
authors.affiliation: School of Biotechnology, Madurai Kamaraj University, Madurai, 625021, India.|Institute of Mathematical Sciences, Chennai, 600113, India.
authors.forename: Sankaran
authors.initials: S
authors.lastname: Krishnaswamy
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000276:immunology; D001665:Binding Sites; D003001:Cloning, Molecular; D000939:Epitopes / Q000737:chemistry* / Q000235:genetics / Q000276:immunology; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D015870:Gene Expression; D006678:HIV / Q000235:genetics / Q000276:immunology; D015700:HIV Envelope Protein gp41 / Q000737:chemistry* / Q000235:genetics / Q000276:immunology; D015658:HIV Infections / Q000276:immunology / Q000821:virology; D006801:Humans; D007106:Immune Sera / Q000737:chemistry; D019151:Peptide Library; D018272:Porins / Q000737:chemistry* / Q000235:genetics / Q000276:immunology; D011485:Protein Binding; D000072757:Protein Conformation, beta-Strand; D015202:Protein Engineering; D054730:Protein Interaction Domains and Motifs; D055503:Protein Multimerization; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000276:immunology; D012485:Salmonella typhi / Q000235:genetics* / Q000378:metabolism; D016415:Sequence Alignment
chemical_list: D001426:Bacterial Proteins; D000939:Epitopes; D015700:HIV Envelope Protein gp41; D007106:Immune Sera; C113724:OmpC protein; C109237:OmpF protein; D019151:Peptide Library; D018272:Porins; D011993:Recombinant Fusion Proteins
keywords: Kennedy peptide; chimeric protein; display system; membrane protein; trimer