ArticlePloS one2014
Bacteria-based analysis of HIV-1 Vpu channel activity.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 22 citations in OpenAlex.
- Ion-Channel-Targeting Drugs for Chikungunya Virus.Molecules (Basel, Switzerland) · 2025Article
- Identification and Structural Characterization of Viroporins from Deadly Hemorrhagic Viruses.Viruses · 2025Article
- A bacteria-based search for drugs against avian and swine flu yields a potent and resistance-resilient channel blocker.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Viroporins of Mpox Virus.International journal of molecular sciences · 2023Article
- Exhaustive mutational analysis of severe acute respiratory syndrome coronavirus 2 ORF3a: An essential component in the pathogen's infectivity cycle.Protein science : a publication of the Protein Society · 2023Article
- Article
- Zika M-A Potential Viroporin: Mutational Study and Drug Repurposing.Biomedicines · 2022Article
- Identification of SARS-CoV-2 E Channel Blockers from a Repurposed Drug Library.Pharmaceuticals (Basel, Switzerland) · 2021Article
- Article
- SARS-CoV-2 E protein is a potential ion channel that can be inhibited by Gliclazide and Memantine.Biochemical and biophysical research communications · 2020Article
- Potential Viroporin Candidates From Pathogenic Viruses Using Bacteria-Based Bioassays.Viruses · 2019Article
- Pathophysiological Consequences of Calcium-Conducting Viroporins.Annual review of virology · 2015Review
- Vpu Protein: The Viroporin Encoded by HIV-1.Viruses · 2015Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
HIV-1 Vpu is a small, single-span membrane protein with two attributed functions that increase the virus' pathogenicity: degradation of CD4 and inactivation of BST-2. Vpu has also been shown to possess ion channel activity, yet no correlation has been found between this attribute and Vpu's role in viral release. In order to gain further insight into the channel activity of Vpu we devised two bacteria-based assays that can examine this function in detail. In the first assay Vpu was over-expressed, such that it was deleterious to bacterial growth due to membrane permeabilization. In the second and more sensitive assay, the channel was expressed at low levels in K(+) transport deficient bacteria. Consequently, Vpu expression enabled the bacteria to grow at otherwise non permissive low K(+) concentrations. Hence, Vpu had the opposite impact on bacterial growth in the two assays: detrimental in the former and beneficial in the latter. Furthermore, we show that channel blockers also behave reciprocally in the two assays, promoting growth in the first assay and hindering it in the second assay. Taken together, we investigated Vpu's channel activity in a rapid and quantitative approach that is amenable to high-throughput screening, in search of novel blockers.
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