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

ABSTRACT:

Importance

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.

SUBMITTER: Xiao X

PROVIDER: S-EPMC10734504 | biostudies-literature | 2023 Dec

REPOSITORIES: biostudies-literature

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

Xiao Xiao X Wen Zhiyun Z Chen Qing Q Shipman Jennifer M JM Kostas James J Reid John C JC Warren Christopher C Tang Aimin A Luo Bin B O'Donnell Gregory G Fridman Arthur A Chen Zhifeng Z Vora Kalpit A KA Zhang Lan L Su Hua-Poo H-P Eddins Michael J MJ

Journal of virology 20231130 12

<h4>Importance</h4>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 t ...[more]

PMID: 38032197

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