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Targeting antigenic site on RSV F protein associated with virus neutralization for vaccine design
5th Asia Pacific Global Summit and Expo on Vaccines & Vaccination
July 27-29, 2015 Brisbane, Australia
Noushin Jaberolansar, Keith Chappell, Sharareh Eskandari, Daniel Watterson, Mariusz Skwarczynski, Paul Young and Istvan Toth
Posters-Accepted Abstracts: J Vaccines Vaccin
Abstract:
Respiratory syncytial virus (RSV) is a leading cause of lower respiratory tract infection in infants and young children. RSV also causes serious illness in the elderly, immuno-compromised and persons with cardiopulmonary diseases.1 The significant morbidity and mortality associated with RSV infection emphasises the urgent need for vaccines against RSV infection. The failure of formalin-inactivated RSV clinical trials in the 1960s2 directed researches towards finding new approaches for the development of RSV vaccines. In this study, a B cell epitope KNYIDKQLLPIVNKQS from the RSV F protein, known to be the target of neutralizing antibody, was chosen for vaccine development. The proposed vaccine strategy utilizes the lipid core peptide (LCP) delivery system with self-adjuvanting properties 3, 4 in conjunction with the B-cell peptide epitope and Pan DR (PADRE) as a T helper epitope (Figure 1). The vaccine candidates were designed, synthesized and their purity and identity confirmed by RP-HPLC and ESI-MS, respectively. The secondary structure analysis and potential of specific antibodies to recognize the synthetic vaccine candidates were studied. LCP delivery system as well as the coil-promoting sequence from yeast GCN4 protein was required to generate the native (desired) helical confirmation of the epitope. CD results and ELISA data indicated that candidates with helical confirmation could bind to specific antibodies. In addition, dynamic light scattering (DLS) and TEM showed that the GCN4 construct formed small nanoparticles which are expected to induce strong immune responses. Figure 1: Schematic presentation of LCP construct.