Altered HIV-1 Gag protein interactions with cyclophilin A (CypA) on the acquisition of H219Q and H219P substitutions in the CypA binding loop.

@article{Gatanaga2006AlteredHG,
  title={Altered HIV-1 Gag protein interactions with cyclophilin A (CypA) on the acquisition of H219Q and H219P substitutions in the CypA binding loop.},
  author={Hiroyuki Gatanaga and Debananda Das and Yasuhiro Suzuki and Damaris D Yeh and Khaja Azhar Hussain and Arun K. Ghosh and Hiroaki Mitsuya},
  journal={The Journal of biological chemistry},
  year={2006},
  volume={281 2},
  pages={1241-50}
}
HIV-1 Gag protein interaction with cyclophilin A (CypA) is critical for viral fitness. Among the amino acid substitutions identified in Gag noncleavage sites in HIV-1 variants resistant to protease inhibitors, H219Q (Gatanaga, H., Suzuki, Y., Tsang, H., Yoshimura, K., Kavlick, M. F., Nagashima, K., Gorelick, R. J., Mardy, S., Tang, C., Summers, M. F., and Mitsuya, H. (2002) J. Biol. Chem. 277, 5952-5961) and H219P substitutions in the viral CypA binding loop confer the greatest replication… CONTINUE READING

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