- Structural characterization of M8C10, a neutralizing antibody targeting a highly conserved prefusion-specific epitope on the metapneumovirus fusion trimerization interface.
Structural characterization of M8C10, a neutralizing antibody targeting a highly conserved prefusion-specific epitope on the metapneumovirus fusion trimerization interface.
Journal of virology (2023-11-30)
Xiao Xiao, Zhiyun Wen, Qing Chen, Jennifer M Shipman, James Kostas, John C Reid, Christopher Warren, Aimin Tang, Bin Luo, Gregory O'Donnell, Arthur Fridman, Zhifeng Chen, Kalpit A Vora, Lan Zhang, Hua-Poo Su, Michael J Eddins
PMID38032197
ABSTRACT
Human metapneumovirus (hMPV) is a common pathogen causing lower respiratory tract infections worldwide and can develop severe symptoms in high-risk populations such as infants, the elderly, and immunocompromised patients. There are no approved hMPV vaccines or neutralizing antibodies available for therapeutic or prophylactic use. The trimeric hMPV fusion F protein is the major target of neutralizing antibodies in human sera. Understanding the immune recognition of antibodies to hMPV-F antigen will provide critical insights into developing efficacious hMPV monoclonal antibodies and vaccines.
MATERIALI
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Sigma-Aldrich
Anti-Human Metapneumovirus Antibody, clone 132, clone 132, Chemicon®, from mouse