The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Natural Variation in Vif: Differential Impact on APOBEC3G/3F and a Potential Role in HIV-1 Diversification
Open accessAbstract
The HIV-1 Vif protein counteracts the antiviral activity exhibited by the host cytidine deaminases APOBEC3G and APOBEC3F. Here, we show that defective vif alleles can readily be found in HIV-1 isolates and infected patients. Single residue changes in the Vif protein sequence are sufficient to cause the loss of Vif-induced APOBEC3 neutralization. Interestingly, not all the detected defects lead to a complete inactivation of Vif function since some mutants retained selective neutralizing activity against APOBEC3F but not APOBEC3G or vice versa. Concordantly, independently hypermutated proviruses with distinguishable patterns of G-to-A substitution attributable to cytidine deamination induced by APOBEC3G, APOBEC3F, or both enzymes were present in individuals carrying proviruses with completely or partly defective Vif variants. Natural variation in Vif function may result in selective and partial neutralization of cytidine deaminases and thereby promote viral sequence diversification within HIV-1 infected individuals.
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Martin-Serrano, J., Zang, T., & Bieniasz, P. D. (2001) · Nature Medicine · doi:10.1038/nm1201-1313 · Cited by 710
Self-citationAncient adaptive evolution of the primate antiviral DNA-editing enzyme APOBEC3G
Sawyer, S. L., Emerman, M., & Malik, H. S. (2004) · PLoS Biology · doi:10.1371/journal.pbio.0020275 · Cited by 485
Cited by
Keele, B. F., Giorgi, E. E., Salazar-Gonzalez, J. F., Decker, J. M., Pham, K. T., Salazar, M. G., Sun, C., Grayson, T., Wang, S., Li, H., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0802203105 · Cited by 1,912
Plasma Membrane Is the Site of Productive HIV-1 Particle Assembly
Jouvenet, N., Neil, S. J. D., Bess, C., Johnson, M. C., Virgen, C. A., Simon, S. M., & Bieniasz, P. D. (2006) · PLoS Biology · doi:10.1371/journal.pbio.0040435 · Cited by 357
Self-citationTwo-stepping through time: mammals and viruses
Meyerson, N. R., & Sawyer, S. L. (2011) · Trends in Microbiology · doi:10.1016/j.tim.2011.03.006 · Cited by 133
Multifaceted antiviral actions of APOBEC3 cytidine deaminases
Chiu, Y.-L., & Greene, W. C. (2006) · Trends in Immunology · doi:10.1016/j.it.2006.04.003 · Cited by 72
Dispersed Sites of HIV Vif-Dependent Polyubiquitination in the DNA Deaminase APOBEC3F
Albin, J. S., Anderson, J. S., Johnson, J. R., Harjes, E., Matsuo, H., Krogan, N. J., & Harris, R. S. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.01.010 · Cited by 25
Metadata
- Authors
- Simon, V., Zennou, V., Murray, D., Huang, Y., Ho, D. D., & Bieniasz, P. D.
- Venue
- PLoS Pathogens
- Publisher
- Public Library of Science (PLoS)
- Published
- 2005-07-22
- Volume
- 1
- Issue
- 1
- Pages
- e6
- ISSN
- 1553-7366 (ISSN-L)
- 1553-7374
- OpenAlex
- W2059238079
- Cited by
- 249
- References
- 2
- FWCI
- 6.93
- Type
- journal article
- Language
- en
- Open access
- gold
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- Simon, V., Zennou, V., Murray, D., Huang, Y., Ho, D. D., & Bieniasz, P. D. (2005). Natural Variation in Vif: Differential Impact on APOBEC3G/3F and a Potential Role in HIV-1 Diversification. PLoS Pathogens. https://doi.org/10.1371/journal.ppat.0010006
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