Abstract
The pneumoviruses respiratory syncytial virus (RSV) and human metapneumovirus (hMPV) are two widespread human pathogens that can cause severe disease in the young, the elderly, and the immunocompromised. Despite the discovery of RSV over 60 years ago, and hMPV nearly 20 years ago, there are no approved vaccines for either virus. Antibody-mediated immunity is critical for protection from RSV and hMPV, and, until recently, knowledge of the antibody epitopes on the surface glycoproteins of RSV and hMPV was very limited. However, recent breakthroughs in the recombinant expression and stabilization of pneumovirus fusion proteins have facilitated in-depth characterization of antibody responses and structural epitopes, and have provided an enormous diversity of new monoclonal antibody candidates for therapeutic development. These new data have primarily focused on the RSV F protein, and have led to a wealth of new vaccine candidates in preclinical and clinical trials. In contrast, the major structural antibody epitopes remain unclear for the hMPV F protein. Overall, this review will cover recent advances in characterizing the antigenic sites on the RSV and hMPV F proteins.
Highlights
The recently reclassified Pneumoviridae virus family includes the human pathogens respiratory syncytial virus (RSV) and human metapneumovirus [1]
Antigenic sites IV and III from the RSV F protein have been found to be conserved on human metapneumovirus (hMPV) F due to the isolation of cross-reactive monoclonal antibody (mAb) discussed in the RSV section. hMPV F-specific mAbs have shown success in neutralizing hMPV both in vitro and in vivo
Pre-fusionstabilized constructs have allowed for isolation of mAbs with optimal neutralization potency, including those binding at antigenic site Ø and V on the RSV F protein
Summary
The recently reclassified Pneumoviridae virus family includes the human pathogens respiratory syncytial virus (RSV) and human metapneumovirus (hMPV) [1]. Vaccination with pre-fusion RSV F induces higher levels of neutralizing IgG than vaccination with post-fusion RSV F [36], FIGURE 1 | X-ray crystal structures of pneumovirus F proteins alone and in complex monoclonal antibody fragments. Antigenic site V was described recently, based on mAb isolation to new pre-fusion-stabilized constructs [46, 59].
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