Respiratory syncytial virus (RSV) and its close relative, human metapneumovirus (hMPV), are leading causes of lower respiratory tract infections in infants and children yet there are no licensed vaccines available to prevent these viral infections.
Attempts to develop an effective vaccine have been focused on a highly conserved viral protein called the fusion or F protein. When activated, the protein achieves infection by triggering fusion of viral and cell membranes in the lung.
Several antibodies that bind the F protein have been isolated previously. Using blood samples from healthy donors, Jarrod Mousa, PhD, James Crowe, Jr., MD, and colleagues generated four new monoclonal antibodies that are specific to the site IV region of the RSV F protein.
One of the antibodies was highly potent in neutralizing RSV in laboratory studies, while another neutralized both RSV and hMPV. The findings, published this week in the journal PLOS Pathogens, reveal important structural features of the F protein that could be used in rational structure-based vaccine design.
This research was supported with funding from the Ann Scott Carell Chair held by Crowe.
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