ArticleNature communications2024
Structural transition of GP64 triggered by a pH-sensitive multi-histidine switch.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- The native conformational landscape and priming mechanism of herpes simplex virus glycoprotein B.Science advances · 2026Article
- Computational methods in physical virology: a critical perspective across lengths and timescales.FEMS microbiology reviews · 2026Review
- Viro3D: a comprehensive database of virus protein structure predictions.Molecular systems biology · 2025Article
- Essential histidine residues in Bombyx mori nucleopolyhedrovirus GP64 mediate pH-dependent membrane fusion.Microbiology spectrum · 2025Article
- Experimental and evolutionary evidence for horizontal transfer of an envelope fusion protein gene between thogotoviruses and baculoviruses.Journal of virology · 2025Article
- Distinctive Features of Extracellular Vesicles Present in the Gastric Juice of Patients with Gastric Cancer and Healthy Subjects.International journal of molecular sciences · 2025Article
- Baculovirus Variant Detection from Transient CRISPR-Cas9-Mediated Disruption ofInternational journal of molecular sciences · 2025Article
- Article
- Coordination of the host Vps4-Vta1 complex and the viral core protein Ac93 facilitates entry of Autographa californica multiple nucleopolyhedrovirus budded virions.Journal of virology · 2025Article
- Unraveling dual fusion mechanisms in BmNPV GP64: critical roles of CARC motifs and signal peptide retention.Journal of virology · 2025Article
Corrections and comments
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Authors and funding
12 authors.
Funding
Abstract
The fusion of viruses with cellular membranes is a critical step in the life cycle of enveloped viruses. This process is facilitated by viral fusion proteins, many of which are conformationally pH-sensitive. The specifics of how changes in pH initiate this fusion have remained largely elusive. This study presents the cryo-electron microscopy (cryo-EM) structures of a prototype class III fusion protein, GP64, in its prefusion and early intermediate states, revealing the structural intermediates accompanying the membrane fusion process. The structures identify the involvement of a pH-sensitive switch, comprising H23, H245, and H304, in sensing the low pH that triggers the initial step of membrane fusion. The pH sensing role of this switch is corroborated by assays of cell-cell syncytium formation and dual dye-labeling. The findings demonstrate that coordination between multiple histidine residues acts as a pH sensor and activator. The involvement of a multi-histidine switch in viral fusion is applicable to fusogens of human-infecting thogotoviruses and other viruses, which could lead to strategies for developing anti-viral therapies and vaccines.
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