The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Palmitoylation of the HIV-1 envelope glycoprotein is critical for viral infectivity
Open accessAbstract
Recent studies suggest that HIV-1 budding occurs selectively from detergent-insoluble membrane domains, referred to as lipid rafts. Palmitoylation is thought to be one of the factors responsible for targeting membrane proteins to lipid rafts. The cytoplasmic domain of the HIV-1 envelope glycoprotein (gp160) contains two palmitoylated cysteine residues. In this work, we studied the solubility of gp160 after detergent extraction. We show that wild-type gp160 is mostly insoluble after ice-cold Triton X-100 extraction, but that it becomes almost completely soluble at 37°C. In contrast, we find that a mutant gp160, in which the two palmitoylated cysteine residues are replaced by serine, is Triton X-100 soluble even under ice-cold extraction. These findings are consistent with the properties of proteins that localize to lipid rafts and strongly suggest that gp160 is associated with lipid rafts. Further, removal of both palmitoylation sites results in the formation of virus with low levels of gp160 incorporation as well as a decrease in viral infectivity by 60-fold. Our results strongly support the suggestion that HIV-1 buds from lipid rafts and point to a role for rafts as a viral assembly hub.
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Cites
Functional rafts in cell membranes
Simons, K., & Ikonen, E. (1997) · Nature · doi:10.1038/42408 · Cited by 9,757
Chemokine receptors as HIV-1 coreceptors: roles in viral entry, tropism, and disease
Berger, E. A., Murphy, P. M., & Farber, J. M. (1999) · Annual Review of Immunology · doi:10.1146/annurev.immunol.17.1.657 · Cited by 2,180
Cited by
Virus Entry, Assembly, Budding, and Membrane Rafts
Chazal, N., & Gerlier, D. (2003) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.67.2.226-237.2003 · Cited by 482
Location is Everything: Lipid Rafts and Immune Cell Signaling
Dykstra, M., Cherukuri, A., Sohn, H. W., Tzeng, S.-J., & Pierce, S. K. (2003) · Annual Review of Immunology · doi:10.1146/annurev.immunol.21.120601.141021 · Cited by 477
Greasing Their Way: Lipid Modifications Determine Protein Association with Membrane Rafts
Levental, I., Grzybek, M., & Simons, K. (2010) · Biochemistry · doi:10.1021/bi100882y · Cited by 420
The Many Mechanisms of Viral Membrane Fusion Proteins
Earp, L. J., Delos, S. E., Park, H. E., & White, J. M. (2004) · Current Topics in Microbiology and Immunology · doi:10.1007/3-540-26764-6_2 · Cited by 379
Chan, R., Uchil, P. D., Jin, J., Shui, G., Ott, D. E., Mothes, W., & Wenk, M. R. (2008) · Journal of Virology · doi:10.1128/jvi.00981-08 · Cited by 282
Metadata
- Authors
- Rousso, I., Mixon, M. B., Chen, B. K., & Kim, P. S.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2000-11-28
- Volume
- 97
- Issue
- 25
- Pages
- 13523-13525
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1963729107
- Cited by
- 189
- References
- 2
- FWCI
- 4.33
- Type
- journal article
- Language
- en
- Open access
- green
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- Rousso, I., Mixon, M. B., Chen, B. K., & Kim, P. S. (2000). Palmitoylation of the HIV-1 envelope glycoprotein is critical for viral infectivity. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.240459697
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