@article{mbs:/content/journal/jgv/10.1099/vir.0.2008/005199-0, author = "Ulbrandt, Nancy D. and Ji, Hong and Patel, Nita K. and Barnes, Arnita S. and Wilson, Susan and Kiener, Peter A. and Suzich, JoAnn and McCarthy, Michael P.", title = "Identification of antibody neutralization epitopes on the fusion protein of human metapneumovirus", journal= "Journal of General Virology", year = "2008", volume = "89", number = "12", pages = "3113-3118", doi = "https://doi.org/10.1099/vir.0.2008/005199-0", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/vir.0.2008/005199-0", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", abstract = "Human metapneumovirus (hMPV) is genetically related to respiratory syncytial virus (RSV); both cause respiratory tract illnesses ranging from a mild cough to bronchiolitis and pneumonia. The F protein-directed monoclonal antibody (mAb) palivizumab has been shown to prevent severe lower respiratory tract RSV infection in animals and humans. We have previously reported on a panel of mAbs against the hMPV F protein that neutralize hMPV in vitro and, in two cases, in vivo. Here we describe the generation of hMPV mAb-resistant mutants (MARMs) to these neutralizing antibodies. Sequencing the F proteins of the hMPV MARMs identified several neutralizing epitopes. Interestingly, some of the epitopes mapped on the hMPV F protein coincide with homologous regions mapped previously on the RSV F protein, including the site against which the broadly protective mAb palivizumab is directed. This suggests that these homologous regions play important, conserved functions in both viruses.", }