ReviewBiochimica et biophysica acta2011
Comparative NMR studies demonstrate profound differences between two viroporins: p7 of HCV and Vpu of HIV-1.
Review in Biochimica et biophysica acta, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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Who cites it
21 citing papers in PubMed, 32 citations in OpenAlex.
- Advances in Viroporin Function and Structure: A Comparative Analysis of Alphavirus 6K with Well-Characterized Viroporins.Viruses · 2025Review
- Review
- Functional characterization of p7 viroporin from hepatitis C virus produced in a cell-free expression system.Protein expression and purification · 2016Article
- Targeting the Channel Activity of Viroporins.Advances in protein chemistry and structural biology · 2016Review
- Article
- Review
- Relating structure and function of viral membrane-spanning miniproteins.Current opinion in virology · 2015Review
- Magic angle spinning NMR of viruses.Progress in nuclear magnetic resonance spectroscopy · 2015Review
- Two different conformations in hepatitis C virus p7 protein account for proton transport and dye release.PloS one · 2014Article
- Impact of histidine residues on the transmembrane helices of viroporins.Molecular membrane biology · 2013Article
- When detergent meets bilayer: birth and coming of age of lipid bicelles.Progress in nuclear magnetic resonance spectroscopy · 2013Review
- On the role of NMR spectroscopy for characterization of antimicrobial peptides.Methods in molecular biology (Clifton, N.J.) · 2013Review
- The magic of bicelles lights up membrane protein structure.Chemical reviews · 2012Review
- In silico investigations of possible routes of assembly of ORF 3a from SARS-CoV.Journal of molecular modeling · 2012Article
- Changes in Lysozyme Flexibility upon Mutation Are Frequent, Large and Long-Ranged.PLoS computational biology · 2012Article
- The p7 protein of hepatitis C virus forms structurally plastic, minimalist ion channels.PLoS computational biology · 2012Article
- 'q-Titration' of long-chain and short-chain lipids differentiates between structured and mobile residues of membrane proteins studied in bicelles by solution NMR spectroscopy.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2012Article
- The HIV-1 Vpu viroporin inhibitor BIT225 does not affect Vpu-mediated tetherin antagonism.PloS one · 2011Article
- Article
- Beyond Channel Activity: Protein-Protein Interactions Involving Viroporins.Sub-cellular biochemistryReview
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.