HIV entry and envelope glycoprotein-mediated fusion
Open accessAbstract
HIV entry involves binding of the trimeric viral envelope glycoprotein (Env) gp120/gp41 to cell surface receptors, which triggers conformational changes in Env that drive the membrane fusion reaction. The conformational landscape that the lipids and Env navigate en route to fusion has been examined by biophysical measurements on the microscale, whereas electron tomography, x-rays, and NMR have provided insights into the process on the nanoscale and atomic scale. However, the coupling between the lipid and protein pathways that give rise to fusion has not been resolved. Here, we discuss the known and unknown about the overall HIV Env-mediated fusion process.
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Coreceptor binding triggers conformational changes and dissociation of the gp120-gp41 heterotrimer, helping gp41 penetrate the plasma membrane and facilitating fusion of the viral envelope with the plasma membrane, depositing the CA containing viral genetic material into the host cell cytoplasm.
“Coreceptor binding triggers further conformational changes and dissociation of the trimer of gp120–gp41 heterotrimer. This dissociation helps gp41 penetrate the plasma membrane, facilitating fusion of the viral envelope with the plasma membrane, allowing the deposition of the CA containing the viral genetic material into the cytoplasm of the host cell (Carlson et al. 2008, Blumenthal et al. 2012).”
From Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication (2026) · cites this paper as Blumenthal et al. 2012
Cites
Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9
McLellan, J. S., Pancera, M., Carrico, C., Gorman, J., Julien, J.-P., Khayat, R., Louder, R., Pejchal, R., Sastry, M., Dai, K., et al. (2011) · Nature · doi:10.1038/nature10696 · Cited by 830 · see citing works
Inhibition of furin-mediated cleavage activation of HIV-1 glycoprotein gpl60
Hallenberger, S., Bosch, V., Angliker, H., Shaw, E., Klenk, H.-D., & Garten, W. (1992) · Nature · doi:10.1038/360358a0 · Cited by 582 · see citing works
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Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication
Jehad, M. A., Ali, L. M., Pillai, V. N., Prabhu, S. G., Mustafa, F., & Rizvi, T. A. (2026) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuaf066 · Cited by 5 · see citing works
“This dissociation helps gp41 penetrate the plasma membrane, facilitating fusion of the viral envelope with the plasma membrane, allowing the deposition of the CA containing the viral genetic material into the cytoplasm of the host cell (Carlson et al. 2008 , Blumenthal et al. 2012 ).”
- Authors
- Blumenthal, R., Durell, S., & Viard, M.
- Affiliations
- National Institutes of Health (US)
- Frederick National Laboratory for Cancer Research (US)
- Corresponding author
- Blumenthal, Robert
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2012-11
- Volume
- 287
- Issue
- 49
- Pages
- 40841-40849
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC3510787
- OpenAlex
- W2067693929
- Cited by
- 212
- References
- 3
- Citations by year
- 2026: 8 · 2025: 10 · 2024: 7 · 2023: 8 · 2022: 12 · 2021: 14 · 2020: 15 · 2019: 23 · 2018: 19 · 2017: 19 · 2016: 17 · 2015: 19 · 2014: 24 · 2013: 16 · 2012: 1
- FWCI
- 2.40
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Frederick National Laboratory for Cancer Research (HHSN261200800001E.)
- National Institutes of Health (#HHSN261200800001E, HHSN261200800001C, Contract HHSN261200800001E)
- National Cancer Institute (Contract HHSN261200800001E, HHSN261200800001E))
- National Institute of Allergy and Infectious Diseases (HHSN261200800001E)
- Topics
- Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- HIV entry, viral envelope glycoprotein, membrane fusion, conformational change, cell surface receptors, viral fusion
- MeSH terms
- Biophysics, Humans, Lipids, Membrane Fusion, Models, Molecular, Molecular Conformation, Magnetic Resonance Spectroscopy, Protein Conformation, HIV Infections, HIV Envelope Protein gp120, HIV Envelope Protein gp41, Crystallography, X-Ray, Electron Microscope Tomography
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