The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Specific recognition and accelerated uncoating of retroviral capsids by the TRIM5α restriction factor
Abstract
The host restriction factor TRIM5α mediates species-specific, early blocks to retrovirus infection; susceptibility to these blocks is determined by viral capsid sequences. Here we demonstrate that TRIM5α variants from Old World monkeys specifically associate with the HIV type 1 (HIV-1) capsid and that this interaction depends on the TRIM5α B30.2 domain. Human and New World monkey TRIM5α proteins associated less efficiently with the HIV-1 capsid, accounting for the lack of restriction in cells of these species. After infection, the expression of a restricting TRIM5α in the target cells correlated with a decrease in the amount of particulate capsid in the cytosol. In some cases, this loss of particulate capsid was accompanied by a detectable increase in soluble capsid protein. Inhibiting the proteasome did not abrogate restriction. Thus, TRIM5α restricts retroviral infection by specifically recognizing the capsid and promoting its rapid, premature disassembly.
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Citations
Cites
Cyclophilin A retrotransposition into TRIM5 explains owl monkey resistance to HIV-1
Sayah, D. M., Sokolskaja, E., Berthoux, L., & Luban, J. (2004) · Nature · doi:10.1038/nature02777 · Cited by 662
High-resolution structure of a retroviral capsid hexameric amino-terminal domain
Mortuza, G. B., Haire, L. F., Stevens, A., Smerdon, S. J., Stoye, J. P., & Taylor, I. A. (2004) · Nature · doi:10.1038/nature02915 · Cited by 185
Cited by
TRIM5 is an innate immune sensor for the retrovirus capsid lattice
Pertel, T., Hausmann, S., Morger, D., Züger, S., Guerra, J., Lascano, J., Reinhard, C., Santoni, F. A., Uchil, P. D., Chatel, L., et al. (2011) · Nature · doi:10.1038/nature09976 · Cited by 645
HIV-1 capsid: the multifaceted key player in HIV-1 infection
Campbell, E. M., & Hope, T. J. (2015) · Nature Reviews Microbiology · doi:10.1038/nrmicro3503 · Cited by 430
Structural basis for PRYSPRY-mediated tripartite motif (TRIM) protein function
James, L. C., Keeble, A. H., Khan, Z., Rhodes, D. A., & Trowsdale, J. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0609174104 · Cited by 386
Studies of endogenous retroviruses reveal a continuing evolutionary saga
Stoye, J. P. (2012) · Nature Reviews Microbiology · doi:10.1038/nrmicro2783 · Cited by 350
The Interferon-Inducible MxB Protein Inhibits HIV-1 Infection
Liu, Z., Pan, Q., Ding, S., Qian, J., Xu, F., Zhou, J., Cen, S., Guo, F., & Liang, C. (2013) · Cell Host & Microbe · doi:10.1016/j.chom.2013.08.015 · Cited by 334
Metadata
- Authors
- Stremlau, M., Perron, M., Lee, M., Li, Y., Song, B., Javanbakht, H., Diaz-Griffero, F., Anderson, D. J., Sundquist, W. I., & Sodroski, J.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2006-04-04
- Volume
- 103
- Issue
- 14
- Pages
- 5514-5519
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2156829363
- Cited by
- 739
- References
- 2
- FWCI
- 16.03
- Type
- journal article
- Language
- en
- Open access
- closed
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- Stremlau, M., Perron, M., Lee, M., Li, Y., Song, B., Javanbakht, H., Diaz-Griffero, F., Anderson, D. J., Sundquist, W. I., & Sodroski, J. (2006). Specific recognition and accelerated uncoating of retroviral capsids by the TRIM5α restriction factor. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0509996103
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