Journal Article

PUBDB-2024-05665

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Structure, function, and evolution of the Orthobunyavirus membrane fusion glycoprotein

Hellert, J.CSSB* ; Aebischer, A. ; Haouz, A. ; Guardado-Calvo, P. ; Reiche, S. ; Beer, M. (Corresponding author) ; Rey, F. A. (Corresponding author)

2023
Elsevier [New York, NY]

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Please use a persistent id in citations: doi:10.1016/j.celrep.2023.112142  doi:10.3204/PUBDB-2024-05665

Abstract: La Crosse virus, responsible for pediatric encephalitis in the United States, and Schmallenberg virus, a highly teratogenic veterinary virus in Europe, belong to the large Orthobunyavirus genus of zoonotic arthropod-borne pathogens distributed worldwide. Viruses in this under-studied genus cause CNS infections or fever with debilitating arthralgia/myalgia syndromes, with no effective treatment. The main surface antigen, glycoprotein Gc (∼1,000 residues), has a variable N-terminal half (GcS) targeted by the patients’ antibody response and a conserved C-terminal moiety (GcF) responsible for membrane fusion during cell entry. Here, we report the X-ray structure of post-fusion La Crosse and Schmallenberg virus GcF, revealing the molecular determinants for hairpin formation and trimerization required to drive membrane fusion. We further experimentally confirm the role of residues in the fusion loops and in a vestigial endoplasmic reticulum (ER) translocation sequence at the GcS-GcF junction. The resulting knowledge provides essential molecular underpinnings for future development of potential therapeutic treatments and vaccines.

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Contributing Institute(s):

1. CSSB - Leibniz-Institut für Experimentelle Virologie (LIV) - Kay Grünewald (CSSB-LIV-KG)

Research Program(s):

1. 899 - ohne Topic (POF4-899) (POF4-899)
2. ZAPI - Zoonotic Anticipation and Preparedness Initiative (115760) (115760)

Experiment(s):

1. No specific instrument

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