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Deep time structural evolution of retroviral and filoviral surface envelope proteins
Open accessPreprint — published as 10.1128/jvi.00063-22 · Paper page
Abstract
The retroviral surface envelope protein subunit (SU) mediates receptor binding and triggers membrane fusion by the transmembrane subunit (TM). SU evolves rapidly under strong selective conditions, resulting in seemingly unrelated SU structures in highly divergent retroviruses. Structural modeling of the SU of several retroviruses and related endogenous retroviral elements with AlphaFold identifies a TM-proximal SU β-sandwich structure that has been conserved in the orthoretroviruses for at least 110 million years. The SU of orthoretroviruses diversified by differential expansion of the β -sandwich core to form domains involved in virus-host interactions. The β-sandwich domain is also conserved in the SU equivalent GP 1 of Ebola virus although with a significantly different orientation in the trimeric envelope protein structure. The unified structural view of orthoretroviral SU and filoviral GP 1 identifies an ancient, structurally conserved and evolvable domain underlying the structural diversity of orthoretroviral SU and filoviral GP 1 .
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Highly accurate protein structure prediction with AlphaFold
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Metadata
- Authors
- Hötzel, I.
- Affiliations
- Genentech (US)
- Corresponding author
- Hötzel, Isidro
- ORCID
- Hötzel, Isidro
- Venue
- Journal of Virology
- Publisher
- openRxiv
- Published
- 2021-11-05
- Volume
- 96
- Issue
- 7
- Pages
- e0006322-e0006322
- ISSN
- 0022-538X (ISSN-L)
- PMC
- PMC9006886
- OpenAlex
- W4221129934
- Cited by
- 9
- References
- 1
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 3 · 2023: 4
- FWCI
- 0.65
- Type
- journal article
- Language
- en
- Open access
- green
- doi.org
- Licence
- cc-by-nc-nd
- Locations
- Journal of Virology (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
- Life Sciences › Immunology and Microbiology › Immunology › T-cell and Retrovirus Studies
- Health Sciences › Medicine › Epidemiology › Virology and Viral Diseases
- Keywords
- structural relationships, sequence divergence, lentivirus, protein structure
- MeSH terms
- Humans, Viral Envelope Proteins, Gene Products, env, Endogenous Retroviruses, Ebolavirus
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