Expression of HIV-1 Vif and Human APOBEC3G with a Bicistronic Vector

Yi Shu Yang; Xiao Na Sun; Di Liu; Xiao Li Wang; Si Si Shen; Ze Lin Li; Yi Zeng

doi:10.4028/www.scientific.net/AMM.108.141

Paper Titles

Characterization of Ionic Currents in Peptidergic Neurons from Eyestalks of Chinese Mitten Crab Eriocheir sinensis
p.116

Optimization of Poly(β-L-malic acid) Production Using Aureobasidium Pullulans by Response Surface Methodology
p.121

Antagonistic Mechanism of Fusarium Oxysporum of Soybean Root Rot by Bacillus Subtilis
p.127

Determination of Mating Type of Phytophthora Infestans and Long Term Preservation by Using Mineral Oil
p.132

Expression of HIV-1 Vif and Human APOBEC3G with a Bicistronic Vector
p.141

The Seperation of Flavonoids and Polyphenols from Eucommia Ulmoides Leaves and their Antioxidation In Vivo
p.146

Separation and Purification of Alcaligenes Biodemulsifier by Dichloromethane-Water Extraction and Silica Gel Column Chromatograph
p.152

Breeding of Oleaginous Rhodotorula Glutinis and the Synthesis of Biodiesel
p.159

Phosphate Solubilizing Rhizospherebacterial T21 Isolated from Dongxiang Wild Rice Species Promotes Cultivated Rice Growth
p.167

HomeApplied Mechanics and MaterialsApplied Mechanics and Materials Vol. 108Expression of HIV-1 Vif and Human APOBEC3G with a...

Expression of HIV-1 Vif and Human APOBEC3G with a Bicistronic Vector

Abstract:

Novel targets against HIV-1 are booming recently. APOBEC3G has the potential to inhibit the replication of HIV-1, while its antiviral activity is counteracted by Vif. The antiviral mechanism of APOBEC3G and the antagonistic mechanism of Vif have drawn great attention. Considering the occurrence of interaction between Vif and APOBEC3G should be based on that these two proteins coexist in the same cells, a eukaryotic bicistronic vector was adopted to express both Vif and APOBEC3G simultaneously. The expression and distribution of Vif and APOBEC3G proteins are detected with fluorescent microscope.

You might also be interested in these eBooks

Mechanical Engineering and Materials Science (ICMEMS)

View Preview

Info:

Periodical:

Applied Mechanics and Materials (Volume 108)

Pages:

141-145

DOI:

https://doi.org/10.4028/www.scientific.net/AMM.108.141

Citation:

Cite this paper

Online since:

October 2011

Authors:

Yi Shu Yang, Xiao Na Sun, Di Liu, Xiao Li Wang, Si Si Shen, Ze Lin Li, Yi Zeng

Keywords:

Apolipoprotein B MRNA Editing Enzyme-Catalytic Polypeptide-Like 3G (APOBEC3G), Eukaryotic Bicistronic Vector, Human Immunodeficiency Virus (HIV), Viral Infectivity Factor (VIF)

Export:

RIS, BibTeX

Price:

Permissions CCC:

Request Permissions

Permissions PLS:

Request Permissions

Сopyright:

Citation:

References

[1] A. M. Sheehy, N. C. Gaddis, J. D. Choi, M. H. Malim, Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein, Nature, vol. 418, Aug. 2002, pp.646-650, doi: 10. 1038/nature00939.

DOI: 10.1038/nature00939

Google Scholar

[2] R. Suspene, P. Sommer, M. Henry, S. Ferris, D. Guetard, S. Pochet, et al, APOBEC3G is a single-stranded DNA cytidine deaminase and functions independently of HIV reverse transcriptase, Nucleic Acids Res, vol. 32, Mar. 2004, pp.2421-2429.

DOI: 10.1093/nar/gkh554

Google Scholar

[3] H. Zhang, B. Yang, R. J. Pomerantz, C. Zhang, S. C. Arunachalam, L. Gao, The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA, Nature, vol. 424, Jul. 2003, pp.94-98, doi: 10. 1038/nature01707.

DOI: 10.1038/nature01707

Google Scholar

[4] K. Shindo, A. Takaori-Kondo, M. Kobayashi, A. Abudu, K. Fukunaga, T. Uchiyama, The enzymatic activity of CEM15/Apobec-3G is essential for the regulation of the infectivity of HIV-1 virion but not a sole determinant of its antiviral activity, J. Biol. Chem, vol. 278, Nov. 2003, pp.44412-44416.

DOI: 10.1074/jbc.c300376200

Google Scholar

[5] R. Mariani, D. Chen, B. Schrofelbauer, F. Navarro, R. Konig, B. Bollman, et al, Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif, Cell, vol. 114, Jul. 2003, pp.21-31, doi: 10. 1016/S0092-8674(03)00515-4.

DOI: 10.1016/s0092-8674(03)00515-4

Google Scholar

[6] S. G. Conticello, R. S. Harris, M. S. Neuberger, The Vif protein of HIV triggers degradation of the human antiretroviral DNA deaminase APOBEC3G, Curr. Biol, vol. 13, Nov. 2003, pp.2009-2013, doi: 10. 1016/j. cub. 2003. 10. 034.

DOI: 10.1016/j.cub.2003.10.034

Google Scholar

[7] R. S. Harris, K. N. Bishop, A. M. Sheehy, H. M. Craig, S. K. Petersen-Mahrt, I. N. Watt, DNA deamination mediates innate immunity to retroviral infection, Cell, vol. 113, Jun. 2003, pp.803-809, doi: 10. 1016/S0092-8674(03)00423-9.

DOI: 10.1016/s0092-8674(03)00423-9

Google Scholar

[8] D. Lecossier, F. Bouchonnet, F. Clavel, A. J. Hance, Hypermutation of HIV-1 DNA in the absence of the Vif protein, Science, vol. 300, May. 2003, p.1112, doi: 10. 1126/science. 1083338.

DOI: 10.1126/science.1083338

Google Scholar

[9] B. Mangeat, P. Turelli, G. Caron, M. Friedli, L. Perrin, D. Trono, Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts, Nature, vol. 424, Jul. 2003, pp.99-103, doi: 10. 1038/nature01709.

DOI: 10.1038/nature01709

Google Scholar

[10] S. Kao, M. A. Khan, E. Miyagi, R. Plishka, A. Buckler-White, K. Strebel, The human immunodeficiency virus Type 1 Vif protein reduces intracellular expression and inhibits packaging of APOBEC3G (CEM15), a cellular inhibitor of virus infectivity, J. Virol, vol. 77, Nov. 2003, pp.11398-11407, doi: 10. 1128/JVI. 77. 21. 11398-11407. (2003).

DOI: 10.1128/jvi.77.21.11398-11407.2003

Google Scholar

[11] A. Mehle, B. Strack, P. Ancuta, C. Zhang, M. McPike, D. Gabuzda, Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin–proteasome pathway, J. Biol. Chem, vol. 279, Feb. 2004, pp.7792-7798.

DOI: 10.1074/jbc.m313093200

Google Scholar

[12] X. Yu, Y. Yu, B. Liu, K. Luo, W. Kong, P. Mao, et al, Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif–Cul5–SCF complex, Science, vol. 302, Nov. 2003, pp.1056-1060, doi: 10. 1126/science. 1089591.

DOI: 10.1126/science.1089591

Google Scholar

[13] K. Stopak, C. de Noronha, W. Yonemoto, W. C. Greene, HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability, Mol. Cell, vol. 12, Sep. 2003, pp.591-601.

DOI: 10.1016/s1097-2765(03)00353-8

Google Scholar