Role of cellular proteins in the life cycle of human immunodeficiency virus


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Abstract

The paper shows a role of cellular proteins that control the early and late stages of HIV infection due to the keen genetic parasitism of human immunodeficiency virus (HIV). In its early life cycle, the virus uses the cell receptors CD4, CCR5, G-protein processor, and actin filaments of the cytoskeleton for nuclear transport. The cellular proteins transport the preintegration complex through the nuclear pores and assist complementary DNA to integrate with cellular DNA. At late stages, the cellular proteins provide the transport of viral components to the assemblage site - lipid rafts, the strong binding to them, the insertion of glycoproteins into the viral particle, and the cellular escape of the virus. To inhibit the cellular mechanisms involved in the infectious process is a new antiviral strategy approach to treating AIDS.

References

  1. Букринская А. Г., Букринский М. И. Внутриклеточный транспорт вируса иммунодефицита человека // Биол. мембраны. - 2007. - Т. 24, № 5. - С. 355-362.
  2. Auewaracul P., Wachrapornin P., Sricatrapimuk S. et al. Uncoating of HIV-1 requires cellular activation // Virology. - 2005. - Vol. 337. - P. 93-101.
  3. Bhattacharya J., Repik A., Clapham P. Gag regulates association of HIV-1 envelope with detergent-resistant membranes // J. Virol. - 2006. - Vol. 80, N 4. - P. 5292-5300.
  4. Brugger B., Glass B., Haberkant P. et al. The HIV lipidome: a raft with an unusual composition // Proc. Natl. Acad. Sci. USA. - 2006. - Vol. 103, N 8. - P. 2641-2646.
  5. Bukrinskaya A., Brichachek B., Mann A. et al. Establishment of a functional HIV-1 reverse transcription complex involves the cytoskeleton // J. Exp. Med. - 1996. - Vol. 188. - P. 2113-2125.
  6. Bukrinskaya A. HIV-1 assembly and maturation // Arch. Virol. - 2004. - Vol. 149. - P. 1067-1082.
  7. Bukrinsaya A. HIV-1 matrix protein: a mysterious regulator of the viral life cycle // Virus Res. - 2007. - Vol. 124, N 1-2. - P. 1-11.
  8. Bukrinsky M. A hard way to the nucleus // Mol. Med. - 2004. - Vol. 10. - P. 1-5.
  9. Choe H., Farzan M., Sun Y. et al. The beta-chemokine receptors CCR3 and CCR5 facilitate infection by primary HIV-1 isolates // Cell. - 1996. - Vol. 85. - P. 1135-1148.
  10. Deng H., Liu R., Ellmeyer W. et al. Identification of a major coreceptor for primary isolates of HIV-1 // Nature. - 1996. - Vol. 381. - P. 661-666.
  11. Feng Y., Broder C., Kennedy P. et al. HIV entry cofactor // Science. - 1996. - Vol. 272. - P. 872-877.
  12. Freed E. HIV-1 Gag: Flipped out for P1(4,5)P2 // Proc. Natl. Acad. Sci. USA. - 2006. - Vol. 103, N 30. - P. 11101-11103.
  13. Hearps A., Jans D. HIV-1 integrase is capable of targeting DNA to the nucleus via an importin alpha-beta dependent mechanism // Biochem. J. - 2006. - Vol. 395. - P. 475-484.
  14. Jacke J. M., Stevenson M. The inner nuclear envelope protein emerin regulates HIV-1 infectivity // Nature. - 2006. - Vol. 441. - P. 641-645.
  15. Kenakin T. Allosteric modulators: the new generation of receptor antagonist // J. Pharmacol. Exp. Ther. - 2005. - Vol. 313, N 3. - P. 1150-1162.
  16. Kenakin T. Inverse, protein and ligand-selective agonism // J. Pharmacol. Exp. Ther. - 2007. - Vol. 323, N 2. - P. 701-707.
  17. Landelier C., von Schwedler U., Fisher R. et al. Human ESCRT-II complex and its role in HIV-1 release // J. Virol. - 2006. - Vol. 80. - P. 9465-9480.
  18. Lopez-Verges S., Camus J., Blot G. et al. Tail-interacting protein TIP47 is a connector between Gag and Env and is required for Env incorporation into HIV-1 virions //Proc. Natl. Acad. Sci. USA. - 2006. - Vol. 103. - P. 14947-14952.
  19. Ono A., Freed E. Plasma membrane rafts play a critical role in HIV-1 assembly and release // Proc. Natl. Acad. Sci. USA. - 2001. - Vol. 98. - P. 13925-13930.
  20. Ono A., Ablan S., Lockett S. et al. Phosphatidylinositol (4,5) biphosphate regulates HIV-1 targeting to the plasma membrane // Proc. Natl. Acad. Sci. USA. - 2004. - Vol. 101. - P. 14889-14894.
  21. Qi M., Aiken C. Selective restriction of nef-defective HIV-1 by a proteasome-dependent mechanism // J. Virol. - 2007. - Vol. 81. - P. 1534-1536.
  22. Rey O., Canon J., Krogstat P. HIV-1 Gag protein associates with F actin present in microfilaments // Virology. - 1996. - Vol. 220. - P. 530-534.
  23. Saad J., Miller J., Tai J. et al. Structural basis for targeting HIV-1 Gag protein to the plasma membrane for virus assembly // Proc. Natl. Acad. Sci. USA. - 2006. - Vol. 103, N 30. - P. 11364-11369.
  24. Sasaki H., Ozaki H., Karaki H. et al. Actin filaments play an essential role for transport of nascent HIV-1 proteins in host cell // Biochem. Biophys. Res. Commun. - 2004. - Vol. 316. - P. 588-593.
  25. Shkriabai N., Datta S., Zhao Z. et al. Interactions of HIV-1 Gag with assembly cofactors // Biochemistry. - 2006. - Vol. 45, N 13. - P. 4077-4083.
  26. Tang C., Loeliger E., Lungsword P. et al. Entropic switch regulates myristate exposure in the HIV-1 matrix protein // Proc. Natl. Acad. Sci. USA. - 2004. - Vol. 101, N 2. - P. 517-522.

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