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Self assembly and pore formation of HIV GP160 revealed at molecular resolution

Lookup NU author(s): Dr Lynn Donlon, Dr Daniel Frankel

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Abstract

Protein assembly at interfaces is fundamental to disease pathology and biological function. Here we report on the self assembly of the HIV viral envelope protein HIV GP160 and its interaction with phospholipids. The protein can assemble to form either pores or large aggregates. The process of aggregation can be observed at molecular resolution giving a rare insight into the assembly process. HIV GP160 was reconstituted into lipid bilayers simulating the HIV viral envelope and exhibited similar self assembly behaviour to the naked protein. When HIV GP160 was adsorbed on top of a pure single phase phospholipid bilayer it gradually "sank in" over time. Such a variety of self assembly modes and lipid interactions could be critical to the behaviour of the protein in the viral envelope and subsequent viral infection.


Publication metadata

Author(s): Donlon L, Frankel D

Publication type: Article

Publication status: Published

Journal: Soft Matter

Year: 2013

Volume: 9

Issue: 1

Pages: 283-290

Print publication date: 18/10/2012

ISSN (print): 1744-683X

ISSN (electronic): 1744-6848

Publisher: RSC Publications

URL: http://dx.doi.org/10.1039/c2sm26980e

DOI: 10.1039/c2sm26980e


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