A physical model for the selective assembly of HIV-1.

ORAL

Abstract

We report on finding an intramolecular bound state of the structural Gag capsid protein of HIV-1 using a combination of all-atom Molecular Dynamics (MD) simulations and statistical mechanical modeling. The presence of this bound state prevents premature capsid assembly on non-viral host RNA. It would unify numerous observations that have been made on HIV-1. We show that the presence of a GFP sequence inserted into the Gag gene interferes with the formation of the bound-state, suggesting that such constructs can not be considered as representative of the wild-type Gag. The central role of the bound-state for the kinetics suggests a variety of possible routes for interfering with HIV-1 assembly.

*We thank the NSF-DMR for support under Grant 1610384 (SD, BS, RB);

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Presenters

  • Chen Lin

    • Chemistry and Biochemistry, University of California, Los Angeles

Authors

  • Chen Lin

    • Chemistry and Biochemistry, University of California, Los Angeles

  • Ioulia Rouzina

    • Department of Chemistry and Biochemistry, Ohio State University
    • Molecular Biology, The Ohio State University

  • Paola Espinosa

    • Department of Physics, UAM (Iztapalapa)

  • Orlando Guzman

    • Department of Physics, UAM (Iztapalapa)

  • Jose-Antonio Moreno

    • Department of Physics, UAM (Iztapalapa)

  • Robijn Bruinsma

    • Physics and Astronomy, University of California, Los Angeles