Vaccination with the postfusion hMPV B2 F protein generated a balanced Th1/Th2 response and targeted two previously discovered neutralizing epitopes.
The structural and immunogenic characterization of the postfusion hMPV F protein provides foundational knowledge for vaccine development against human metapneumovirus.
Human metapneumovirus (hMPV) is an important cause of viral respiratory disease. In this paper, we report the X-ray crystal structure of the hMPV fusion (F) protein in the postfusion conformation from genotype B. We also assessed binding of the hMPV F protein to heparin and heparan sulfate, a previously reported receptor for the hMPV F protein. Furthermore, we determined the immunogenicity and protective efficacy of postfusion hMPV B2 F protein, which is the first study using a homogenous conformation of the protein. Antibodies generated in response to vaccination give a balanced Th1/Th2 response and target two previously discovered neutralizing epitopes.
Huang et al. (Wed,) conducted a other in Human metapneumovirus (hMPV). Postfusion hMPV B2 F protein was evaluated on Immunogenicity and protective efficacy. Vaccination with the postfusion hMPV B2 F protein generated a balanced Th1/Th2 response and targeted two previously discovered neutralizing epitopes.