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Outer membrane protein size and LPS O-antigen define protective antibody targeting to the Salmonella surface

Author

Listed:
  • C. Coral Domínguez-Medina

    (University of Birmingham
    University of Birmingham)

  • Marisol Pérez-Toledo

    (University of Birmingham
    University of Birmingham
    Specialties Hospital, National Medical Centre “Siglo XXI” Mexican Institute for Social Security)

  • Anna E. Schager

    (University of Birmingham
    University of Birmingham)

  • Jennifer L. Marshall

    (University of Birmingham)

  • Charlotte N. Cook

    (University of Birmingham
    University of Birmingham)

  • Saeeda Bobat

    (University of Birmingham
    University of Birmingham)

  • Hyea Hwang

    (Georgia Institute of Technology)

  • Byeong Jae Chun

    (Georgia Institute of Technology)

  • Erin Logan

    (University of Cape Town)

  • Jack A. Bryant

    (University of Birmingham)

  • Will M. Channell

    (University of Birmingham)

  • Faye C. Morris

    (University of Birmingham)

  • Sian E. Jossi

    (University of Birmingham)

  • Areej Alshayea

    (University of Birmingham)

  • Amanda E. Rossiter

    (University of Birmingham)

  • Paul A. Barrow

    (University of Nottingham)

  • William G. Horsnell

    (University of Cape Town)

  • Calman A. MacLennan

    (University of Oxford)

  • Ian R. Henderson

    (University of Birmingham)

  • Jeremy H. Lakey

    (University of Newcastle)

  • James C. Gumbart

    (Georgia Institute of Technology)

  • Constantino López-Macías

    (Specialties Hospital, National Medical Centre “Siglo XXI” Mexican Institute for Social Security)

  • Vassiliy N. Bavro

    (University of Essex, Wivenhoe Park)

  • Adam F. Cunningham

    (University of Birmingham
    University of Birmingham)

Abstract

Lipopolysaccharide (LPS) O-antigen (O-Ag) is known to limit antibody binding to surface antigens, although the relationship between antibody, O-Ag and other outer-membrane antigens is poorly understood. Here we report, immunization with the trimeric porin OmpD from Salmonella Typhimurium (STmOmpD) protects against infection. Atomistic molecular dynamics simulations indicate this is because OmpD trimers generate footprints within the O-Ag layer sufficiently sized for a single IgG Fab to access. While STmOmpD differs from its orthologue in S. Enteritidis (SEn) by a single amino-acid residue, immunization with STmOmpD confers minimal protection to SEn. This is due to the OmpD-O-Ag interplay restricting IgG binding, with the pairing of OmpD with its native O-Ag being essential for optimal protection after immunization. Thus, both the chemical and physical structure of O-Ag are key for the presentation of specific epitopes within proteinaceous surface-antigens. This enhances combinatorial antigenic diversity in Gram-negative bacteria, while reducing associated fitness costs.

Suggested Citation

  • C. Coral Domínguez-Medina & Marisol Pérez-Toledo & Anna E. Schager & Jennifer L. Marshall & Charlotte N. Cook & Saeeda Bobat & Hyea Hwang & Byeong Jae Chun & Erin Logan & Jack A. Bryant & Will M. Chan, 2020. "Outer membrane protein size and LPS O-antigen define protective antibody targeting to the Salmonella surface," Nature Communications, Nature, vol. 11(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-14655-9
    DOI: 10.1038/s41467-020-14655-9
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