Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Comment
. 2018 Jul 31:7:e38895.
doi: 10.7554/eLife.38895.

The secrets of the stability of the HIV-1 capsid

Martin Obr  1 , Hans-Georg Kräusslich  1
Affiliations
Comment

The secrets of the stability of the HIV-1 capsid

Martin Obr et al. Elife. .

Abstract

Structural and biophysical studies help to follow the disassembly of the HIV-1 capsid in vitro, and reveal the role of a small molecule called IP6 in regulating capsid stability.

Keywords: CA lattice; HIV-1; IP6; PF74; R18 pore; capsid; human; infectious disease; microbiology; molecular biophysics; structural biology; virus.

PubMed Disclaimer

Conflict of interest statement

MO, HK No competing interests declared

Figures

Figure 1.
Figure 1.. Molecular structure of the HIV-1 capsid and the small molecule IP6 binding to the R18 pore.
(A) Transmission electron microscopy image of an authentic negative stained HIV-1 capsid. The capsid is formed of hundreds of CA proteins organized in hexamers and pentamers. (B). The structure of a CA hexamer, revealed by X-ray crystallography (PDB ID: 3H47). (C). Detail of the small molecule IP6 (IP6; in the center) binding to a ring of six arginines (R18; on the outside) within the R18 pore at the center of a CA hexamer. IP6 contains six negatively charged phosphate groups , which are coordinated by the positively charged guanidino groups of the R18 side chains. Dashed lines indicate interactions between the guanidino and phosphate groups (Panel C is adapted from Mallery et al., 2018).
See this image and copyright information in PMC

Comment on

References

    1. Bhattacharya A, Alam SL, Fricke T, Zadrozny K, Sedzicki J, Taylor AB, Demeler B, Pornillos O, Ganser-Pornillos BK, Diaz-Griffero F, Ivanov DN, Yeager M. Structural basis of HIV-1 capsid recognition by PF74 and CPSF6. PNAS. 2014;111:18625–18630. doi: 10.1073/pnas.1419945112. - DOI - PMC - PubMed
    1. Campbell EM, Hope TJ. HIV-1 capsid: the multifaceted key player in HIV-1 infection. Nature Reviews Microbiology. 2015;13:471–483. doi: 10.1038/nrmicro3503. - DOI - PMC - PubMed
    1. Campbell S, Fisher RJ, Towler EM, Fox S, Issaq HJ, Wolfe T, Phillips LR, Rein A. Modulation of HIV-like particle assembly in vitro by inositol phosphates. PNAS. 2001;98:10875–10879. doi: 10.1073/pnas.191224698. - DOI - PMC - PubMed
    1. Forshey BM, von Schwedler U, Sundquist WI, Aiken C. Formation of a human immunodeficiency virus type 1 core of optimal stability is crucial for viral replication. Journal of Virology. 2002;76:5667–5677. doi: 10.1128/JVI.76.11.5667-5677.2002. - DOI - PMC - PubMed
    1. Jacques DA, McEwan WA, Hilditch L, Price AJ, Towers GJ, James LC. HIV-1 uses dynamic capsid pores to import nucleotides and fuel encapsidated DNA synthesis. Nature. 2016;536:349–353. doi: 10.1038/nature19098. - DOI - PMC - PubMed

LinkOut - more resources