The DOI matches its Crossref record; 12 of the 12 references it cites were found in a registry or an index.
Virus Maturation by Budding
Open accessAbstract
SUMMARY: Enveloped viruses mature by budding at cellular membranes. It has been generally thought that this process is driven by interactions between the viral transmembrane proteins and the internal virion components (core, capsid, or nucleocapsid). This model was particularly applicable to alphaviruses, which require both spike proteins and a nucleocapsid for budding. However, genetic studies have clearly shown that the retrovirus core protein, i.e., the Gag protein, is able to form enveloped particles by itself. Also, budding of negative-strand RNA viruses (rhabdoviruses, orthomyxoviruses, and paramyxoviruses) seems to be accomplished mainly by internal components, most probably the matrix protein, since the spike proteins are not absolutely required for budding of these viruses either. In contrast, budding of coronavirus particles can occur in the absence of the nucleocapsid and appears to require two membrane proteins only. Biochemical and structural data suggest that the proteins, which play a key role in budding, drive this process by forming a three-dimensional (cage-like) protein lattice at the surface of or within the membrane. Similarly, recent electron microscopic studies revealed that the alphavirus spike proteins are also engaged in extensive lateral interactions, forming a dense protein shell at the outer surface of the viral envelope. On the basis of these data, we propose that the budding of enveloped viruses in general is governed by lateral interactions between peripheral or integral membrane proteins. This new concept also provides answers to the question of how viral and cellular membrane proteins are sorted during budding. In addition, it has implications for the mechanism by which the virion is uncoated during virus entry.
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Citations
Cites
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BackgroundThree-dimensional structure of the human immunodeficiency virus type 1 matrix protein
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“Budding of Retrovirus Particles Requires Core Proteins Only In 1989, the “early” budding model was clearly shown not to apply to HIV-1 and SIV, because it was found that the Env protein is dispensable for budding of these viruses (48, 90).”
ResultInfluentialParent, L. J., Bennett, R. P., Craven, R. C., Nelle, T. D., Krishna, N. K., Bowzard, J. B., Wilson, C. B., Puffer, B. A., Montelaro, R. C., & Wills, J. W. (1995) · Journal of Virology · doi:10.1128/jvi.69.9.5455-5460.1995 · Cited by 258
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Background
Cited by
Physical Principles of Nanoparticle Cellular Endocytosis
Zhang, S., Gao, H., & Bao, G. (2015) · ACS Nano · doi:10.1021/acsnano.5b03184 · Cited by 1,103
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
Kinetics of SARS-CoV-2 specific IgM and IgG responses in COVID-19 patients
Sun, B., Feng, Y., Mo, X., Zheng, P., Wang, Q., Li, P., Peng, P., Liu, X., Chen, Z., Huang, H., et al. (2020) · Emerging Microbes & Infections · doi:10.1080/22221751.2020.1762515 · Cited by 473
Molecular Interactions in the Assembly of Coronaviruses
de Haan, C. A. M., & Rottier, P. J. M. (2005) · Advances in Virus Research · doi:10.1016/s0065-3527(05)64006-7 · Cited by 408
Expression of the Zinc-Finger Antiviral Protein Inhibits Alphavirus Replication
Bick, M. J., Carroll, J.-W. N., Gao, G., Goff, S. P., Rice, C. M., & MacDonald, M. R. (2003) · Journal of Virology · doi:10.1128/jvi.77.21.11555-11562.2003 · Cited by 384
Metadata
- Authors
- Garoff, H., Hewson, R., & Opstelten, D.-J. E.
- Venue
- Microbiology and Molecular Biology Reviews
- Publisher
- American Society for Microbiology
- Published
- 1998-12
- Volume
- 62
- Issue
- 4
- Pages
- 1171-1190
- ISSN
- 1092-2172 (ISSN-L)
- 1098-5557
- OpenAlex
- W2152215476
- Cited by
- 362
- References
- 12
- FWCI
- 6.95
- Type
- journal article
- Language
- en
- Open access
- green
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.