The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Formation of a Human Immunodeficiency Virus Type 1 Core of Optimal Stability Is Crucial for Viral Replication
Open accessAbstract
Virions of human immunodeficiency virus type 1 (HIV-1) and other lentiviruses contain conical cores consisting of a protein shell composed of the viral capsid protein (CA) surrounding an internal viral ribonucleoprotein complex. Although genetic studies have implicated CA in both early and late stages of the virus replication cycle, the mechanism of core disassembly following penetration of target cells remains undefined. Using quantitative assays for analyzing HIV-1 core stability in vitro, we identified point mutations in CA that either reduce or increase the stability of the HIV-1 core without impairing conical core formation in virions. Alterations in core stability resulted in severely attenuated HIV-1 replication and impaired reverse transcription in target cells with only minimal effects on viral DNA synthesis in permeabilized virions in vitro. We conclude that formation of a viral core of optimal stability is a prerequisite for efficient HIV-1 infection and suggest that disassembly of the HIV-1 core is a regulated step in infection that may be an attractive target for pharmacologic intervention.
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Citations
Cites
Crystal Structure of Human Cyclophilin A Bound to the Amino-Terminal Domain of HIV-1 Capsid
Gamble, T. R., Vajdos, F. F., Yoo, S., Worthylake, D. K., Houseweart, M., Sundquist, W. I., & Hill, C. P. (1996) · Cell · doi:10.1016/s0092-8674(00)81823-1 · Cited by 706 · cited 2×
“Structural studies have revealed that CA consists of two distinct, globular domains connected by a flexible linker: an amino-terminal domain, composed of seven -helices and a -hairpin, and a carboxyl-terminal domain, composed of a 310 helix and four -helices (15, 16, 18, 29, 31).”
BackgroundSelf-citationStructure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein
Gamble, T. R., Yoo, S., Vajdos, F. F., von Schwedler, U. K., Worthylake, D. K., Wang, H., McCutcheon, J. P., Sundquist, W. I., & Hill, C. P. (1997) · Science · doi:10.1126/science.278.5339.849 · Cited by 598 · cited 2×
“Structural studies have revealed that CA consists of two distinct, globular domains connected by a flexible linker: an amino-terminal domain, composed of seven -helices and a -hairpin, and a carboxyl-terminal domain, composed of a 310 helix and four -helices (15, 16, 18, 29, 31).”
BackgroundMethodSelf-citationCytokine Signals Are Sufficient for HIV-1 Infection of Resting Human T Lymphocytes
Unutmaz, D., KewalRamani, V. N., Marmon, S., & Littman, D. R. (1999) · The Journal of Experimental Medicine · doi:10.1084/jem.189.11.1735 · Cited by 427
Proteolytic refolding of the HIV‐1 capsid protein amino‐terminus facilitates viral core assembly
von Schwedler, U. K., Stemmler, T. L., Klishko, V. Y., Li, S., Albertine, K. H., Davis, D. R., & Sundquist, W. I. (1998) · The EMBO Journal · doi:10.1093/emboj/17.6.1555 · Cited by 337
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Self-citationMature HIV-1 capsid structure by cryo-electron microscopy and all-atom molecular dynamics
Zhao, G., Perilla, J. R., Yufenyuy, E. L., Meng, X., Chen, B., Ning, J., Ahn, J., Gronenborn, A. M., Schulten, K., Aiken, C., et al. (2013) · Nature · doi:10.1038/nature12162 · Cited by 801
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Metadata
- Authors
- Forshey, B. M., von Schwedler, U., Sundquist, W. I., & Aiken, C.
- Venue
- Journal of Virology
- Publisher
- American Society for Microbiology
- Published
- 2002-06
- Volume
- 76
- Issue
- 11
- Pages
- 5667-5677
- ISSN
- 0022-538X (ISSN-L)
- 1098-5514
- OpenAlex
- W2111673257
- Cited by
- 522
- References
- 4
- FWCI
- 5.60
- Type
- journal article
- Language
- en
- Open access
- green
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- The paper
- Forshey, B. M., von Schwedler, U., Sundquist, W. I., & Aiken, C. (2002). Formation of a Human Immunodeficiency Virus Type 1 Core of Optimal Stability Is Crucial for Viral Replication. Journal of Virology. https://doi.org/10.1128/jvi.76.11.5667-5677.2002
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
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.
