Structural characterization of M8C10, a neutralizing antibody targeting a highly conserved prefusion-specific epitope on the metapneumovirus fusion trimerization interface

M8C10 的结构表征,M8C10 是一种中和抗体,针对亚肺病毒融合三聚化界面上高度保守的融合前特异性表位

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作者: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

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.

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