Inositol phosphates are assembly co-factors for HIV-1
Abstract
A short, 14-amino-acid segment called SP1, located in the Gag structural protein, has a critical role during the formation of the HIV-1 virus particle. During virus assembly, the SP1 peptide and seven preceding residues fold into a six-helix bundle, which holds together the Gag hexamer and facilitates the formation of a curved immature hexagonal lattice underneath the viral membrane. Upon completion of assembly and budding, proteolytic cleavage of Gag leads to virus maturation, in which the immature lattice is broken down; the liberated CA domain of Gag then re-assembles into the mature conical capsid that encloses the viral genome and associated enzymes. Folding and proteolysis of the six-helix bundle are crucial rate-limiting steps of both Gag assembly and disassembly, and the six-helix bundle is an established target of HIV-1 inhibitors. Here, using a combination of structural and functional analyses, we show that inositol hexakisphosphate (InsP6, also known as IP6) facilitates the formation of the six-helix bundle and assembly of the immature HIV-1 Gag lattice. IP6 makes ionic contacts with two rings of lysine residues at the centre of the Gag hexamer. Proteolytic cleavage then unmasks an alternative binding site, where IP6 interaction promotes the assembly of the mature capsid lattice.more »
- Authors:
-
- Cornell Univ., Ithaca, NY (United States)
- Univ. of Virginia, Charlottesville, VA (United States)
- Univ. of Delaware, Newport, DE (United States)
- EMBL, Heidelberg (Germany); Inst. of Science and Technology Austria, Klosterneuburg (Austria)
- Univ. of Missouri, Columbia, MO (United States)
- Publication Date:
- Research Org.:
- Argonne National Laboratory (ANL), Argonne, IL (United States)
- Sponsoring Org.:
- National Inst. of Health; German Research Foundation (DFG); National Science Foundation (NSF)
- OSTI Identifier:
- 1474170
- Grant/Contract Number:
- R01-GM116961; OCI-1053575; ACI-1445606; R01-GM107013; R01-GM105684; P30-GM110758; P50-GM082251; R01-AI129678; U54-GM103297; R01-GM110776; BR 3635/2-1
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Nature (London)
- Additional Journal Information:
- Journal Name: Nature (London); Journal Volume: 560; Journal Issue: 7719; Journal ID: ISSN 0028-0836
- Publisher:
- Nature Publishing Group
- Country of Publication:
- United States
- Language:
- ENGLISH
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; biochemistry; molecular biology
Citation Formats
Dick, Robert A., Zadrozny, Kaneil K., Xu, Chaoyi, Schur, Florian K. M., Lyddon, Terri D., Ricana, Clifton L., Wagner, Jonathan M., Perilla, Juan R., Ganser-Pornillos, Barbie K., Johnson, Marc C., Pornillos, Owen, and Vogt, Volker M. Inositol phosphates are assembly co-factors for HIV-1. United States: N. p., 2018.
Web. doi:10.1038/s41586-018-0396-4.
Dick, Robert A., Zadrozny, Kaneil K., Xu, Chaoyi, Schur, Florian K. M., Lyddon, Terri D., Ricana, Clifton L., Wagner, Jonathan M., Perilla, Juan R., Ganser-Pornillos, Barbie K., Johnson, Marc C., Pornillos, Owen, & Vogt, Volker M. Inositol phosphates are assembly co-factors for HIV-1. United States. https://doi.org/10.1038/s41586-018-0396-4
Dick, Robert A., Zadrozny, Kaneil K., Xu, Chaoyi, Schur, Florian K. M., Lyddon, Terri D., Ricana, Clifton L., Wagner, Jonathan M., Perilla, Juan R., Ganser-Pornillos, Barbie K., Johnson, Marc C., Pornillos, Owen, and Vogt, Volker M. Wed .
"Inositol phosphates are assembly co-factors for HIV-1". United States. https://doi.org/10.1038/s41586-018-0396-4. https://www.osti.gov/servlets/purl/1474170.
@article{osti_1474170,
title = {Inositol phosphates are assembly co-factors for HIV-1},
author = {Dick, Robert A. and Zadrozny, Kaneil K. and Xu, Chaoyi and Schur, Florian K. M. and Lyddon, Terri D. and Ricana, Clifton L. and Wagner, Jonathan M. and Perilla, Juan R. and Ganser-Pornillos, Barbie K. and Johnson, Marc C. and Pornillos, Owen and Vogt, Volker M.},
abstractNote = {A short, 14-amino-acid segment called SP1, located in the Gag structural protein, has a critical role during the formation of the HIV-1 virus particle. During virus assembly, the SP1 peptide and seven preceding residues fold into a six-helix bundle, which holds together the Gag hexamer and facilitates the formation of a curved immature hexagonal lattice underneath the viral membrane. Upon completion of assembly and budding, proteolytic cleavage of Gag leads to virus maturation, in which the immature lattice is broken down; the liberated CA domain of Gag then re-assembles into the mature conical capsid that encloses the viral genome and associated enzymes. Folding and proteolysis of the six-helix bundle are crucial rate-limiting steps of both Gag assembly and disassembly, and the six-helix bundle is an established target of HIV-1 inhibitors. Here, using a combination of structural and functional analyses, we show that inositol hexakisphosphate (InsP6, also known as IP6) facilitates the formation of the six-helix bundle and assembly of the immature HIV-1 Gag lattice. IP6 makes ionic contacts with two rings of lysine residues at the centre of the Gag hexamer. Proteolytic cleavage then unmasks an alternative binding site, where IP6 interaction promotes the assembly of the mature capsid lattice. Furthermore, these studies identify IP6 as a naturally occurring small molecule that promotes both assembly and maturation of HIV-1.},
doi = {10.1038/s41586-018-0396-4},
journal = {Nature (London)},
number = 7719,
volume = 560,
place = {United States},
year = {Wed Aug 01 00:00:00 EDT 2018},
month = {Wed Aug 01 00:00:00 EDT 2018}
}
Web of Science
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