Epitope mapping of antibodies induced with a conserved rhinovirus protein generating protective anti-rhinovirus immunity.

Authors:
Nicholas Glanville
Nicholas Glanville
Imperial College London
United Kingdom
Christine M Nunn
Christine M Nunn
University College London
Katarzyna Niespodziana
Katarzyna Niespodziana
Medical University of Vienna
Austria
Rudolf Valenta
Rudolf Valenta
Medical University of Vienna
Austria
Sebastian L Johnston
Sebastian L Johnston
National Heart and Lung Institute
United Kingdom
Gary R McLean
Gary R McLean
University of British Columbia
Canada

Vaccine 2019 May 16;37(21):2805-2813. Epub 2019 Apr 16.

Cellular and Molecular Immunology Research Centre, School of Human Sciences, London Metropolitan University, London, UK; Airway Disease Section, National Heart and Lung Institute, Imperial College London, London, UK. Electronic address:

Human rhinovirus (RV) infections are the principle cause of common colds and precipitate asthma and chronic obstructive pulmonary disease (COPD) exacerbations. Currently there is no vaccine for RV which is largely due to the existence of ∼160 serotypes/strains. We demonstrated previously that immunising mice with highly conserved VP4 and VP2 regions of the RV polyprotein (RV-A16 VP0) generated cross-reactive immunity to RV in vivo. The current study investigated and mapped the epitopes of RV-A16 VP0 that are targets for antibodies in serum samples from VP0 immunisation and RV challenge studies in mice. Recombinant capsid proteins, peptide pools and individual peptides spanning the immunogen sequence (RV-A16 VP0) were assessed for IgG binding sites to identify epitopes. We found that peptide pools covering the C-terminus of VP4, the N-terminus of VP2 and the neutralising NIm-II site within VP2 were bound by serum IgG from immunised mice. The NIm-II site peptide pool blocked IgG binding to the immunogen RV-A16 VP0 and individual peptides within the pool binding IgG were further mapped. Thus, we have identified immunodominant epitopes of RV vaccine candidate RV-A16 VP0, noting that strong IgG binding antibodies were observed that target a key neutralising epitope that is highly variable amongst RV serotypes.

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Source
https://linkinghub.elsevier.com/retrieve/pii/S0264410X193045
Publisher Site
http://dx.doi.org/10.1016/j.vaccine.2019.04.018DOI Listing
May 2019
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