ePrints

Lipid directed assembly of the HIV capsid protein

Lookup NU author(s): Dr Daniel Frankel

Downloads

Full text for this publication is not currently held within this repository. Alternative links are provided below where available.

Abstract

Experimental evidence for in vivo capsid assembly suggests that capsid formation initiates from interactions between capsid (CA) proteins and lipids in the viral envelope. Various in vitro studies aiming to elucidate the detailed mechanisms of capsid self-assembly products have been carried out in conditions far removed from those, which would be encountered in a physiological environment. In this work we used lipid bilayers as a platform for studying the assembly of the CA protein with the rationale that the lipid–CA interactions play an important role in the nucleation of these structures. Observations using atomic force microscopy (AFM) have allowed a ‘curling tadpole’ mechanism to be suggested for the capsid self-assembly process. Stable dimeric CA proteins are able to move across the lipid bilayer to associate into trimers-of-dimers. These trimers form distinctly curved chains, which coil up to form larger features. As the feature grows additional trimers associate with the feature, giving a tadpole-like appearance. By comparing capsid assembly on mica, on single component lipid bilayers, and phase separated lipid bilayers, it was possible to determine the effect of lipid–protein interactions on capsid assembly.

Publication metadata

Author(s): Miles P, Frankel DJ

Publication type: Article

Publication status: Published

Journal: Soft Matter

Year: 2014

Volume: 10

Issue: 47

Pages: 9562-9567

Print publication date: 21/12/2014

Online publication date: 23/10/2014

Acceptance date: 20/10/2014

ISSN (print): 1744-683X

ISSN (electronic): 1744-6848

Publisher: Royal Society of Chemistry

URL: http://dx.doi.org/10.1039/C4SM01860E

DOI: 10.1039/C4SM01860E

Altmetrics

Share