ArticleProtein science : a publication of the Protein Society2008
Structure and ion channel activity of the human respiratory syncytial virus (hRSV) small hydrophobic protein transmembrane domain.
Article in Protein science : a publication of the Protein Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed.
- The SH protein of mumps virus is a druggable pentameric viroporin.Science advances · 2025Article
- Review
- Defining the Assembleome of the Respiratory Syncytial Virus.Sub-cellular biochemistry · 2023Review
- Receptors for Respiratory Syncytial Virus Infection and Host Factors Regulating the Life Cycle of Respiratory Syncytial Virus.Frontiers in cellular and infection microbiology · 2022Review
- Innate Immune Components that Regulate the Pathogenesis and Resolution of hRSV and hMPV Infections.Viruses · 2020Review
- Contribution of Dendritic Cells in Protective Immunity against Respiratory Syncytial Virus Infection.Viruses · 2020Review
- Phylogenetic evidence of a novel lineage of canine pneumovirus and a naturally recombinant strain isolated from dogs with respiratory illness in Thailand.BMC veterinary research · 2019Article
- Potential Viroporin Candidates From Pathogenic Viruses Using Bacteria-Based Bioassays.Viruses · 2019Article
- Immune-Modulation by the Human Respiratory Syncytial Virus: Focus on Dendritic Cells.Frontiers in immunology · 2019Review
- Modulation of Host Immunity by Human Respiratory Syncytial Virus Virulence Factors: A Synergic Inhibition of Both Innate and Adaptive Immunity.Frontiers in cellular and infection microbiology · 2017Review
- Structure and functional dynamics characterization of the ion channel of the human respiratory syncytial virus (hRSV) small hydrophobic protein (SH) transmembrane domain by combining molecular dynamics with excited normal modes.Journal of molecular modeling · 2016Article
- Human Respiratory Syncytial Virus: Infection and Pathology.Seminars in respiratory and critical care medicine · 2016Review
- Targeting the Channel Activity of Viroporins.Advances in protein chemistry and structural biology · 2016Review
- Pathophysiological Consequences of Calcium-Conducting Viroporins.Annual review of virology · 2015Review
- Partial Attenuation of Respiratory Syncytial Virus with a Deletion of a Small Hydrophobic Gene Is Associated with Elevated Interleukin-1β Responses.Journal of virology · 2015Article
- Novel antigens for RSV vaccines.Current opinion in immunology · 2015Review
- Review
- Protein-Protein Interactions of Viroporins in Coronaviruses and Paramyxoviruses: New Targets for Antivirals?Viruses · 2015Review
- Sedimentation equilibrium of a small oligomer-forming membrane protein: effect of histidine protonation on pentameric stability.Journal of visualized experiments : JoVE · 2015Article
- Inhibition of the human respiratory syncytial virus small hydrophobic protein and structural variations in a bicelle environment.Journal of virology · 2014Article
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Authors and funding
5 authors.
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No grant is acknowledged in the PubMed record.
Abstract
The small hydrophobic (SH) protein from the human respiratory syncytial virus (hRSV) is a glycoprotein of approximately 64 amino acids with one putative alpha-helical transmembrane domain. Although SH protein is important for viral infectivity, its exact role during viral infection is not clear. Herein, we have studied the secondary structure, orientation, and oligomerization of the transmembrane domain of SH (SH-TM) in the presence of lipid bilayers. Only one oligomer, a pentamer, was observed in PFO-PAGE. Using polarized attenuated total reflection-Fourier transform infrared (PATR-FTIR) spectroscopy, we show that the SH-TM is alpha-helical. The rotational orientation of SH-TM was determined by site-specific infrared dichroism (SSID) at two consecutive isotopically labeled residues. This orientation is consistent with that of an evolutionary conserved pentameric model obtained from a global search protocol using 13 homologous sequences of RSV. Conductance studies of SH-TM indicate ion channel activity, which is cation selective, and inactive below the predicted pK(a) of histidine. Thus, our results provide experimental evidence that the transmembrane domain of SH protein forms pentameric alpha-helical bundles that form cation-selective ion channels in planar lipid bilayers. We provide a model for this pore, which should be useful in mutagenesis studies to elucidate its role during the virus cycle.
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