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Structural and mechanistic basis of neutralization by a pan-hantavirus protective antibody
Department of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, NY, USA.
CNRS UMR3569, Structural Virology Unit, Institut Pasteur, Paris, France.
Adimab LLC, Lebanon, NH,USA.
U.S. Army Medical Research Institute of Infectious Diseases, Fort Detrick, Frederick, United States; The Geneva Foundation, Tacoma, WA, USA.
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2023 (English)In: Science Translational Medicine, ISSN 1946-6234, E-ISSN 1946-6242, Vol. 15, no 700, article id eadg1855Article in journal (Refereed) Published
Abstract [en]

Emerging rodent-borne hantaviruses cause severe diseases in humans with no approved vaccines or therapeutics. We recently isolated a monoclonal broadly neutralizing antibody (nAb) from a Puumala virus-experienced human donor. Here, we report its structure bound to its target, the Gn/Gc glycoprotein heterodimer comprising the viral fusion complex. The structure explains the broad activity of the nAb: It recognizes conserved Gc fusion loop sequences and the main chain of variable Gn sequences, thereby straddling the Gn/Gc heterodimer and locking it in its prefusion conformation. We show that the nAb's accelerated dissociation from the divergent Andes virus Gn/Gc at endosomal acidic pH limits its potency against this highly lethal virus and correct this liability by engineering an optimized variant that sets a benchmark as a candidate pan-hantavirus therapeutic.

Place, publisher, year, edition, pages
American Association for the Advancement of Science (AAAS), 2023. Vol. 15, no 700, article id eadg1855
National Category
Microbiology in the medical area Infectious Medicine
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URN: urn:nbn:se:umu:diva-211153DOI: 10.1126/scitranslmed.adg1855PubMedID: 37315110Scopus ID: 2-s2.0-85161965332OAI: oai:DiVA.org:umu-211153DiVA, id: diva2:1779083
Available from: 2023-07-03 Created: 2023-07-03 Last updated: 2023-07-03Bibliographically approved

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Tynell, JanneGröning, RemigiusAhlm, ClasForsell, Mattias N. E.

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