Structure-based design of prefusion-stabilized human metapneumovirus fusion proteins

Ching-Lin Hsieh; Scott A. Rush; Concepcion Palomo; Chia-Wei Chou; Whitney Pickens; Vicente Más; Jason S. McLellan

doi:10.1038/s41467-022-28931-3

Nature Communications (Mar 2022)

Structure-based design of prefusion-stabilized human metapneumovirus fusion proteins

Ching-Lin Hsieh,
Scott A. Rush,
Concepcion Palomo,
Chia-Wei Chou,
Whitney Pickens,
Vicente Más,
Jason S. McLellan

Affiliations

Ching-Lin Hsieh: Department of Molecular Biosciences, The University of Texas at Austin
Scott A. Rush: Department of Molecular Biosciences, The University of Texas at Austin
Concepcion Palomo: Centro Nacional de Microbiología, Instituto de Salud Carlos III
Chia-Wei Chou: Department of Molecular Biosciences, The University of Texas at Austin
Whitney Pickens: Department of Molecular Biosciences, The University of Texas at Austin
Vicente Más: Centro Nacional de Microbiología, Instituto de Salud Carlos III
Jason S. McLellan: Department of Molecular Biosciences, The University of Texas at Austin

DOI: https://doi.org/10.1038/s41467-022-28931-3
Journal volume & issue: Vol. 13, no. 1
pp. 1 – 11

Abstract

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The degree to which the conformation of the human metapneumovirus fusion (F) protein affects immunogenicity has been debated. Here, Hsieh et al. engineer prefusion-stabilized F variants with enhanced thermostability that elicit higher neutralizing antibody titers in mice than postfusion F.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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