-
- Akash Bhattacharya
- Department of Biochemistry and Cancer Therapy and Research Center, University of Texas Health Science Center at San Antonio, San Antonio, TX 78229;
-
- Steven L. Alam
- Department of Biochemistry, University of Utah, Salt Lake City, UT 84112;
-
- Thomas Fricke
- Department of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, NY 10461; and
-
- Kaneil Zadrozny
- Department of Molecular Physiology and Biological Physics,
-
- Jaroslaw Sedzicki
- Department of Molecular Physiology and Biological Physics,
-
- Alexander B. Taylor
- Department of Biochemistry and Cancer Therapy and Research Center, University of Texas Health Science Center at San Antonio, San Antonio, TX 78229;
-
- Borries Demeler
- Department of Biochemistry and Cancer Therapy and Research Center, University of Texas Health Science Center at San Antonio, San Antonio, TX 78229;
-
- Owen Pornillos
- Department of Molecular Physiology and Biological Physics,
-
- Barbie K. Ganser-Pornillos
- Department of Molecular Physiology and Biological Physics,
-
- Felipe Diaz-Griffero
- Department of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, NY 10461; and
-
- Dmitri N. Ivanov
- Department of Biochemistry and Cancer Therapy and Research Center, University of Texas Health Science Center at San Antonio, San Antonio, TX 78229;
-
- Mark Yeager
- Department of Molecular Physiology and Biological Physics,
説明
<jats:title>Significance</jats:title> <jats:p>Events that occur between entry of the HIV-1 capsid into the cytoplasm of the target cell and the delivery of the viral genetic material into the nucleus constitute some of the less well understood processes in the viral life cycle. We demonstrated that PF74, a small-molecule inhibitor of HIV-1, and the host proteins CPSF6 and NUP153 bind to a preformed pocket within the CA protein hexamers that exist within the assembled capsid. Our results suggest that key features of the CA hexameric lattice remain intact upon docking at the nuclear pore. In addition, low molecular weight ligands that better mimic virus–host, protein–protein interactions at the intersubunit interfaces within the assembled viral capsid may offer novel avenues for therapeutic intervention.</jats:p>
収録刊行物
-
- Proceedings of the National Academy of Sciences
-
Proceedings of the National Academy of Sciences 111 (52), 18625-18630, 2014-12-17
Proceedings of the National Academy of Sciences
