ArticleScientific reports2015
The C-terminal region of the non-structural protein 2B from Hepatitis A Virus demonstrates lipid-specific viroporin-like activity.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Enterovirus 2B protein: From viroporin to membrane stress sensor, mechanistic principles of multi-pathway regulation.Virulence · 2027Review
- Highly versatile small virus-encoded proteins in cellular membranes: A structural perspective on how proteins' inherent conformational plasticity couples with host membranes' properties to control cellular processes.Journal of structural biology: X · 2025Article
- Identification of mutations in viral proteins involved in cell adaptation using a reverse genetic system of the live attenuated hepatitis A virus vaccine H2 strain.Virologica Sinica · 2024Article
- Role of Disulphide Bonds in Membrane Partitioning of a Viral Peptide.The Journal of membrane biology · 2022Review
- Functions of Viroporins in the Viral Life Cycle and Their Regulation of Host Cell Responses.Frontiers in immunology · 2022Review
- Triple-target stimuli-responsive anti-COVID-19 face mask with physiological virus-inactivating agents.Biomaterials science · 2021Article
- The effect of amantadine on an ion channel protein from Chikungunya virus.PLoS neglected tropical diseases · 2019Article
- Biological Function and Application of Picornaviral 2B Protein: A New Target for Antiviral Drug Development.Viruses · 2019Review
- Emerging Diversity in Lipid-Protein Interactions.Chemical reviews · 2019Review
- Apoptosis and Autophagy in Picornavirus Infection.Frontiers in microbiology · 2019Review
- A direct role for hepatitis B virus X protein in inducing mitochondrial membrane permeabilization.Journal of viral hepatitis · 2018Article
- The Strategy of Picornavirus Evading Host Antiviral Responses: Non-structural Proteins Suppress the Production of IFNs.Frontiers in microbiology · 2018Review
- Organelle luminal dependence of (+)strand RNA virus replication reveals a hidden druggable target.Science advances · 2018Article
- Cholesterol-directed nanoparticle assemblies based on single amino acid peptide mutations activate cellular uptake and decrease tumor volume.Chemical science · 2017Article
- Control of the negative IRES trans-acting factor KHSRP by ubiquitination.Nucleic acids research · 2017Article
- Inhibitor-Based Therapeutics for Treatment of Viral Hepatitis.Journal of clinical and translational hepatology · 2016Review
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Authors and funding
5 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Viroporins are virally encoded, membrane-active proteins, which enhance viral replication and assist in egress of viruses from host cells. The 2B proteins in the picornaviridae family are known to have viroporin-like properties, and play critical roles during virus replication. The 2B protein of Hepatitis A Virus (2B), an unusual picornavirus, is somewhat dissimilar from its analogues in several respects. HAV 2B is approximately 2.5 times the length of other 2B proteins, and does not disrupt calcium homeostasis or glycoprotein trafficking. Additionally, its membrane penetrating properties are not yet clearly established. Here we show that the membrane interacting activity of HAV 2B is localized in its C-terminal region, which contains an alpha-helical hairpin motif. We show that this region is capable of forming small pores in membranes and demonstrates lipid specific activity, which partially rationalizes the intracellular localization of full-length 2B. Using a combination of biochemical assays and molecular dynamics simulation studies, we also show that HAV 2B demonstrates a marked propensity to dimerize in a crowded environment, and probably interacts with membranes in a multimeric form, a hallmark of other picornavirus viroporins. In sum, our study clearly establishes HAV 2B as a bona fide viroporin in the picornaviridae family.
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