ArticleThe Journal of biological chemistry2008
The dynamic envelope of a fusion class II virus. E3 domain of glycoprotein E2 precursor in Semliki Forest virus provides a unique contact with the fusion protein E1.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed, 11 citations in OpenAlex.
- Recent progress in anti-Chikungunya virus drug discovery: Focus on the viral life cycle and direct-acting antivirals.Virologica Sinica · 2026Review
- Article
- Neutralizing antibodies against Chikungunya virus and structural elucidation of their mechanism of action.Nature communications · 2025Article
- Cryo-EM structures of alphavirus conformational intermediates in low pH-triggered prefusion states.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Article
- Implication for alphavirus host-cell entry and assembly indicated by a 3.5Å resolution cryo-EM structure.Nature communications · 2018Article
- 4.4 Å cryo-EM structure of an enveloped alphavirus Venezuelan equine encephalitis virus.The EMBO journal · 2011Article
- Functional processing and secretion of Chikungunya virus E1 and E2 glycoproteins in insect cells.Virology journal · 2011Article
- Article
- Interactions and oligomerization of hantavirus glycoproteins.Journal of virology · 2010Article
- A structural and functional perspective of alphavirus replication and assembly.Future microbiology · 2009Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In alphaviruses, here represented by Semliki Forest virus, infection requires an acid-responsive spike configuration to facilitate membrane fusion. The creation of this relies on the chaperone function of glycoprotein E2 precursor (p62) and its maturation cleavage into the small external E3 and the membrane-anchored E2 glycoproteins. To reveal how the E3 domain of p62 exerts its control of spike functions, we determine the structure of a p62 cleavage-impaired mutant virus particle (SQL) by electron cryomicroscopy. A comparison with the earlier solved wild type virus structure reveals that the E3 domain of p62(SQL) forms a bulky side protrusion in the spike head region. This establishes a gripper over part of domain II of the fusion protein, with a cotter-like connection downward to a hydrophobic cluster in its central beta-sheet. This finding reevaluates the role of the precursor from being only a provider of a shield over the fusion loop to a structural playmate in formation of the fusogenic architecture.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.