Journal Article

PUBDB-2024-05666

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Organisation of the orthobunyavirus tripodal spike and the structural changes induced by low pH and K+ during entry

Hover, S. ; Charlton, F. W. ; Hellert, J.CSSB* ; Swanson, J. J. ; Mankouri, J. (Corresponding author) ; Barr, J. N. (Corresponding author) ; Fontana, J. (Corresponding author)

2023
Nature Publishing Group UK [London]

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Please use a persistent id in citations: doi:10.1038/s41467-023-41205-w  doi:10.3204/PUBDB-2024-05666

Abstract: Following endocytosis, enveloped viruses employ the changing environmentof maturing endosomes as cues to promote endosomal escape, a processoften mediated by viral glycoproteins. We previously showed that both high[K+] and low pH promote entry of Bunyamwera virus (BUNV), the prototypicalbunyavirus. Here, we use sub-tomogram averaging and AlphaFold, to generatea pseudo-atomic model of the whole BUNV glycoprotein envelope. Weunambiguously locate the Gc fusion domain and its chaperone Gn within thefloor domain of the spike. Furthermore, viral incubation at low pH and high[K+], reminiscent of endocytic conditions, results in a dramatic rearrangementof the BUNV envelope. Structural and biochemical assays indicate that pH 6.3/K+ in the absence of a target membrane elicits a fusion-capable triggeredintermediate state of BUNV GPs; but the same conditions induce fusion whentarget membranes are present. Taken together, we provide mechanisticunderstanding of the requirements for bunyavirus entry

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Contributing Institute(s):

1. CSSB - Leibniz-Institut für Experimentelle Virologie (LIV) / UKE - Maya Topf (CSSB-LIV/UKE-MT)

Research Program(s):

1. 899 - ohne Topic (POF4-899) (POF4-899)

Experiment(s):

1. No specific instrument

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