ArticleVirology2007
Mutagenesis of the La Crosse Virus glycoprotein supports a role for Gc (1066-1087) as the fusion peptide.
Article in Virology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 71 citations in OpenAlex.
- The La Crosse virus M segment determines virus isolate cell-to-cell spread and virulence.bioRxiv : the preprint server for biology · 2026Article
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- The La Crosse virus Gc head domain is a major determinant of infection and pathogenesis.Journal of virology · 2025Article
- Research Progress on the Gc Proteins of Akabane Virus.Veterinary sciences · 2025Review
- The Role of Orthobunyavirus Glycoprotein Gc in the Viral Life Cycle: From Viral Entry to Egress.Molecules (Basel, Switzerland) · 2025Review
- The La Crosse virus class II fusion glycoproteinJournal of virology · 2023Article
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- Article
- Review
- Recent Advances in Bunyavirus Glycoprotein Research: Precursor Processing, Receptor Binding and Structure.Viruses · 2021Review
- Article
- Throw out the Map: Neuropathogenesis of the Globally Expanding California Serogroup of Orthobunyaviruses.Viruses · 2019Review
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- Article
- Mechanistic Insight into Bunyavirus-Induced Membrane Fusion from Structure-Function Analyses of the Hantavirus Envelope Glycoprotein Gc.PLoS pathogens · 2016Article
- Inhibition of the Hantavirus Fusion Process by Predicted Domain III and Stem Peptides from Glycoprotein Gc.PLoS neglected tropical diseases · 2016Article
- Early Bunyavirus-Host Cell Interactions.Viruses · 2016Review
- Article
- Orthobunyaviruses: recent genetic and structural insights.Nature reviews. Microbiology · 2014Review
- Discovery of a unique novel clade of mosquito-associated bunyaviruses.Journal of virology · 2013Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The La Crosse Virus (LACV) M segment encodes two glycoproteins (Gn and Gc), and plays a critical role in the neuropathogenesis of LACV infection as the primary determinant of neuroinvasion. A recent study from our group demonstrated that the region comprising the membrane proximal two-thirds of Gc, amino acids 860-1442, is critical in mediating LACV fusion and entry. Furthermore, computational analysis identified structural similarities between a portion of this region, amino acids 970-1350, and the E1 fusion protein of two alphaviruses: Sindbis virus and Semliki Forrest virus (SFV). Within the region 970-1350, a 22-amino-acid hydrophobic segment (1066-1087) is predicted to correlate structurally with the fusion peptides of class II fusion proteins. We performed site-directed mutagenesis of key amino acids in this 22-amino acid segment and determined the functional consequences of these mutations on fusion and entry. Several mutations within this hydrophobic domain affected glycoprotein expression to some extent, but all mutations either shifted the pH threshold of fusion below that of the wild-type protein, reduced fusion efficiency, or abrogated cell-to-cell fusion and pseudotype entry altogether. These results, coupled with the aforementioned computational modeling, suggest that the LACV Gc functions as a class II fusion protein and support a role for the region Gc 1066-1087 as a fusion peptide.
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