Journal
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
Volume 1808, Issue 2, Pages 554-560Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamem.2010.08.005
Keywords
Hepatitis C virus; P7; Membrane protein; Vpu; Human immunodeficiency virus; Nuclear magnetic resonance
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Funding
- NIBIB NIH HHS [R01 EB005161, R01 EB005161-05, R01 EB005161-04S1, P41 EB002031, P41 EB002031-18] Funding Source: Medline
- NIGMS NIH HHS [R01 GM066978, R01 GM066978-08, R01 GM075877-04, R01 GM075877] Funding Source: Medline
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The p7 protein from hepatitis C virus and the Vpu protein from HIV-1 are members of the viroporin family of small viral membrane proteins. It is essential to determine their structures in order to obtain an understanding of their molecular mechanisms and to develop new classes of anti-viral drugs. Because they are membrane proteins, it is challenging to study them in their native phospholipid bilayer environments by most experimental methods. Here we describe applications of NMR spectroscopy to both p7 and Vpu. Isotopically labeled p7 and Vpu samples were prepared by heterologous expression in bacteria, initial isolation as fusion proteins, and final purification by chromatography. The purified proteins were studied in the model membrane environments of micelles by solution NMR spectroscopy and in aligned phospholipid bilayers by solid-state NMR spectroscopy. The resulting structural findings enable comparisons to be made between the two proteins, demonstrating that they have quite different architectures. Most notably, Vpu has one trans-membrane helix and p7 has two trans-membrane helices; in addition, there are significant differences in the structures and dynamics of their internal loop and terminal regions. (C) 2010 Elsevier B.V. All rights reserved.
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