Profiling of hMPV F-specific antibodies isolated from human memory B cells View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2022-05-10

AUTHORS

Xiao Xiao, Arthur Fridman, Lu Zhang, Pavlo Pristatsky, Eberhard Durr, Michael Minnier, Aimin Tang, Kara S. Cox, Zhiyun Wen, Renee Moore, Dongrui Tian, Jennifer D. Galli, Scott Cosmi, Michael J. Eddins, Nicole L. Sullivan, Xiaodong Yan, Andrew J. Bett, Hua-Poo Su, Kalpit A. Vora, Zhifeng Chen, Lan Zhang

ABSTRACT

Human metapneumovirus (hMPV) belongs to the Pneumoviridae family and is closely related to respiratory syncytial virus (RSV). The surface fusion (F) glycoprotein mediates viral fusion and is the primary target of neutralizing antibodies against hMPV. Here we report 113 hMPV-F specific monoclonal antibodies (mAbs) isolated from memory B cells of human donors. We characterize the antibodies’ germline usage, epitopes, neutralization potencies, and binding specificities. We find that unlike RSV-F specific mAbs, antibody responses to hMPV F are less dominant against the apex of the antigen, and the majority of the potent neutralizing mAbs recognize epitopes on the side of hMPV F. Furthermore, neutralizing epitopes that differ from previously defined antigenic sites on RSV F are identified, and multiple binding modes of site V and II mAbs are discovered. Interestingly, mAbs that bind preferentially to the unprocessed prefusion F show poor neutralization potency. These results elucidate the immune recognition of hMPV infection and provide novel insights for future hMPV antibody and vaccine development. More... »

PAGES

2546

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41467-022-30205-x

DOI

http://dx.doi.org/10.1038/s41467-022-30205-x

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1147765532

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/35538099


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