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Protein-to-structure pipeline for ambient-temperature in situ crystallography at VMXi (2023)
Journal Article
Mikolajek, H., Sanchez-Weatherby, J., Sandy, J., Gildea, R. J., Campeotto, I., Cheruvara, H., …Hough, M. A. (2023). Protein-to-structure pipeline for ambient-temperature in situ crystallography at VMXi. IUCrJ, 10(4), 420-429. https://doi.org/10.1107/s2052252523003810

The utility of X-ray crystal structures determined under ambient-temperature conditions is becoming increasingly recognized. Such experiments can allow protein dynamics to be characterized and are particularly well suited to challenging protein targe... Read More about Protein-to-structure pipeline for ambient-temperature in situ crystallography at VMXi.

Editorial: Community series - innovative approaches in diagnosis of emerging/re-emerging infectious diseases, volume II (2023)
Journal Article
Foster, T., & Khaiboullina, S. (2023). Editorial: Community series - innovative approaches in diagnosis of emerging/re-emerging infectious diseases, volume II. Frontiers in Microbiology, 14, Article 1193841. https://doi.org/10.3389/fmicb.2023.1193841

Editorial on the Research Topic: Community series - innovative approaches in diagnosis of emerging/re-emerging infectious diseases, volume II

Inhibition of Arenavirus Entry and Replication by the Cell-Intrinsic Restriction Factor ZMPSTE24 Is Enhanced by IFITM Antiviral Activity (2022)
Journal Article
Stott-Marshall, R. J., & Foster, T. L. (2022). Inhibition of Arenavirus Entry and Replication by the Cell-Intrinsic Restriction Factor ZMPSTE24 Is Enhanced by IFITM Antiviral Activity. Frontiers in Microbiology, 13, Article 840885. https://doi.org/10.3389/fmicb.2022.840885

In the absence of effective vaccines and treatments, annual outbreaks of severe human haemorrhagic fever caused by arenaviruses, such as Lassa virus, continue to pose a significant human health threat. Understanding the balance of cellular factors th... Read More about Inhibition of Arenavirus Entry and Replication by the Cell-Intrinsic Restriction Factor ZMPSTE24 Is Enhanced by IFITM Antiviral Activity.

Rationally derived inhibitors of hepatitis C virus (HCV) p7 channel activity reveal prospect for bimodal antiviral therapy (2020)
Journal Article
Shaw, J., Gosain, R., Kalita, M. M., Foster, T. L., Kankanala, J., Mahato, D. R., …Griffin, S. (2020). Rationally derived inhibitors of hepatitis C virus (HCV) p7 channel activity reveal prospect for bimodal antiviral therapy. eLife, 9, Article e52555. https://doi.org/10.7554/eLife.52555

© 2020, Shaw et al. Since the 1960s, a single class of agent has been licensed targeting virus-encoded ion channels, or 'viroporins', contrasting the success of channel blocking drugs in other areas of medicine. Although resistance arose to these pro... Read More about Rationally derived inhibitors of hepatitis C virus (HCV) p7 channel activity reveal prospect for bimodal antiviral therapy.

Site-directed M2 proton channel inhibitors enable synergistic combination therapy for rimantadine-resistant pandemic influenza (2020)
Journal Article
Scott, C., Kankanala, J., Foster, T. L., Goldhill, D. H., Bao, P., Simmons, K., …Griffin, S. (2020). Site-directed M2 proton channel inhibitors enable synergistic combination therapy for rimantadine-resistant pandemic influenza. PLoS Pathogens, 16(8), Article e1008716. https://doi.org/10.1371/journal.ppat.1008716

Pandemic influenza A virus (IAV) remains a significant threat to global health. Preparedness relies primarily upon a single class of neuraminidase (NA) targeted antivirals, against which resistance is steadily growing. The M2 proton channel is an alt... Read More about Site-directed M2 proton channel inhibitors enable synergistic combination therapy for rimantadine-resistant pandemic influenza.

Distinct Molecular Mechanisms of Host Immune Response Modulation by Arenavirus NP and Z Proteins (2020)
Journal Article
Stott, R. J., Strecker, T., & Foster, T. L. (2020). Distinct Molecular Mechanisms of Host Immune Response Modulation by Arenavirus NP and Z Proteins. Viruses, 12(7), Article 784. https://doi.org/10.3390/v12070784

Endemic to West Africa and South America, mammalian arenaviruses can cross the species barrier from their natural rodent hosts to humans, resulting in illnesses ranging from mild flu-like syndromes to severe and fatal haemorrhagic zoonoses. The incre... Read More about Distinct Molecular Mechanisms of Host Immune Response Modulation by Arenavirus NP and Z Proteins.

Inhibiting the ins and outs of HIV replication: cell-intrinsic antiretroviral restrictions at the plasma membrane (2018)
Journal Article
Foster, T. L., Pickering, S., & Neil, S. J. D. (2018). Inhibiting the ins and outs of HIV replication: cell-intrinsic antiretroviral restrictions at the plasma membrane. Frontiers in Immunology, 8, Article 1853. https://doi.org/10.3389/fimmu.2017.01853

© 2018 Foster, Pickering and Neil. Like all viruses, human immunodeficiency viruses (HIVs) and their primate lentivirus relatives must enter cells in order to replicate and, once produced, new virions need to exit to spread to new targets. These proc... Read More about Inhibiting the ins and outs of HIV replication: cell-intrinsic antiretroviral restrictions at the plasma membrane.

The envelope gene of transmitted HIV-1 resists a late interferon gamma-induced block (2017)
Journal Article
Rihn, S. J., Foster, T. L., Busnadiego, I., Aziz, M. A., Hughes, J., Neil, S. J. D., & Wilson, S. J. (2017). The envelope gene of transmitted HIV-1 resists a late interferon gamma-induced block. Journal of Virology, 91(7), Article e02254-16. https://doi.org/10.1128/JVI.02254-16

Type I interferon (IFN) signaling engenders an antiviral state that likely plays an important role in constraining HIV-1 transmission and contributes to defining subsequent AIDS pathogenesis. Type II IFN (IFN-?) also induces an antiviral state but is... Read More about The envelope gene of transmitted HIV-1 resists a late interferon gamma-induced block.

Resistance of transmitted founder HIV-1 to IFITM-mediated restriction (2016)
Journal Article
Foster, T., Wilson, H., Iyer, S., Coss, K., Doores, K., Smith, S., …Neil, S. (2016). Resistance of transmitted founder HIV-1 to IFITM-mediated restriction. Cell Host and Microbe, 20(4), 429-442. https://doi.org/10.1016/j.chom.2016.08.006

Interferon-induced transmembrane proteins (IFITMs) restrict the entry of diverse enveloped viruses through incompletely understood mechanisms. While IFITMs are reported to inhibit HIV-1, their in vivo relevance is unclear. We show that IFITM sensitiv... Read More about Resistance of transmitted founder HIV-1 to IFITM-mediated restriction.

Serine phosphorylation of HIV-1 Vpu and its binding to tetherin regulates interaction with clathrin adaptors (2015)
Journal Article
Kueck, T., Foster, T. L., Weinelt, J., Sumner, J. C., Pickering, S., & Neil, S. J. D. (2015). Serine phosphorylation of HIV-1 Vpu and its binding to tetherin regulates interaction with clathrin adaptors. PLoS Pathogens, 11(8), https://doi.org/10.1371/journal.ppat.1005141

HIV-1 Vpu prevents incorporation of tetherin (BST2/ CD317) into budding virions and targets it for ESCRT-dependent endosomal degradation via a clathrin-dependent process. This requires a variant acidic dileucine-sorting motif (ExxxLV) in Vpu. Structu... Read More about Serine phosphorylation of HIV-1 Vpu and its binding to tetherin regulates interaction with clathrin adaptors.

Mutations in hepatitis C virus p7 reduce both the egress and infectivity of assembled particles via impaired proton channel function (2013)
Journal Article
Bentham, M. J., Foster, T. L., McCormick, C., & Griffin, S. (2013). Mutations in hepatitis C virus p7 reduce both the egress and infectivity of assembled particles via impaired proton channel function. Journal of General Virology, 94, 2236-2248. https://doi.org/10.1099/vir.0.054338-0

Hepatitis C virus (HCV) p7 protein is critical for the efficient production of infectious virions in culture. p7 undergoes genotype-specific protein–protein interactions as well as displaying channel-forming activity, making it unclear whether the ph... Read More about Mutations in hepatitis C virus p7 reduce both the egress and infectivity of assembled particles via impaired proton channel function.

Structure-guided design affirms inhibitors of hepatitis C virus p7 as a viable class of antivirals targeting virion release (2013)
Journal Article
Foster, T. L., Thompson, G. S., Kalverda, A. P., Kankanala, J., Bentham, M., Wetherill, L. F., …Griffin, S. (2014). Structure-guided design affirms inhibitors of hepatitis C virus p7 as a viable class of antivirals targeting virion release. Hepatology, 59(2), 408-422. https://doi.org/10.1002/hep.26685

Current interferon‐based therapy for hepatitis C virus (HCV) infection is inadequate, prompting a shift toward combinations of direct‐acting antivirals (DAA) with the first protease‐targeted drugs licensed in 2012. Many compounds are in the pipeline... Read More about Structure-guided design affirms inhibitors of hepatitis C virus p7 as a viable class of antivirals targeting virion release.

Resistance mutations define specific antiviral effects for inhibitors of the hepatitis C virus p7 ion channel (2011)
Journal Article
Foster, T. L., Verow, M., Wozniak, A. L., Bentham, M. J., Thompson, J., Atkins, E., …Griffin, S. (2011). Resistance mutations define specific antiviral effects for inhibitors of the hepatitis C virus p7 ion channel. Hepatology, 54(1), 79-90. doi:10.1002/hep.24371

The hepatitis C virus (HCV) p7 ion channel plays a critical role during infectious virus production and represents an important new therapeutic target. Its activity is blocked by structurally distinct classes of small molecules, with sensitivity vary... Read More about Resistance mutations define specific antiviral effects for inhibitors of the hepatitis C virus p7 ion channel.

Cyclophilin A interacts with domain II of hepatitis C virus NS5A and stimulates RNA binding in an isomerase-dependent manner (2011)
Journal Article
Foster, T. L., Gallay, P., Stonehouse, N. J., & Harris, M. (2011). Cyclophilin A interacts with domain II of hepatitis C virus NS5A and stimulates RNA binding in an isomerase-dependent manner. Journal of Virology, 85(14), 7460-7464. doi:10.1128/jvi.00393-11

NS5A plays a critical, yet poorly defined, role in hepatitis C virus genome replication. The protein consists of three domains, each of which is able to bind independently to the 3? untranslated region (UTR) of the viral positive strand genomic RNA.... Read More about Cyclophilin A interacts with domain II of hepatitis C virus NS5A and stimulates RNA binding in an isomerase-dependent manner.

All three domains of the Hepatitis C virus nonstructural NS5A protein contribute to RNA binding (2010)
Journal Article
Foster, T. L., Belyaeva, T., Stonehouse, N. J., Pearson, A. R., & Harris, M. (2010). All three domains of the Hepatitis C virus nonstructural NS5A protein contribute to RNA binding. Journal of Virology, 84(18), 9267-9277. doi:10.1128/jvi.00616-10

The hepatitis C virus (HCV) nonstructural protein NS5A is critical for viral genome replication and is thought to interact directly with both the RNA-dependent RNA polymerase, NS5B, and viral RNA. NS5A consists of three domains which have, as yet, un... Read More about All three domains of the Hepatitis C virus nonstructural NS5A protein contribute to RNA binding.

Direct visualization of the small hydrophobic protein of human respiratory syncytial virus reveals the structural basis for membrane permeability (2010)
Journal Article
Carter, S. D., Dent, K. C., Atkins, E., Foster, T. L., Verow, M., Gorny, P., …Barr, J. N. (2010). Direct visualization of the small hydrophobic protein of human respiratory syncytial virus reveals the structural basis for membrane permeability. FEBS Letters, 584(13), 2786-2790. https://doi.org/10.1016/j.febslet.2010.05.006

Human respiratory syncytial virus (HRSV) is the leading cause of lower respiratory tract disease in infants. The HRSV small hydrophobic (SH) protein plays an important role in HRSV pathogenesis, although its mode of action is unclear. Analysis of the... Read More about Direct visualization of the small hydrophobic protein of human respiratory syncytial virus reveals the structural basis for membrane permeability.

A comparative analysis of the fluorescence properties of the wild-type and active site mutants of the hepatitis C virus autoprotease NS2-3 (2009)
Journal Article
Foster, T. L., Tedbury, P. R., Pearson, A. R., & Harris, M. (2010). A comparative analysis of the fluorescence properties of the wild-type and active site mutants of the hepatitis C virus autoprotease NS2-3. BBA - Proteins and Proteomics, 1804(1), 212-222. https://doi.org/10.1016/j.bbapap.2009.10.006

Hepatitis C virus encodes an autoprotease, NS2-3, which is required for processing of the viral polyprotein between the non-structural NS2 and NS3 proteins. This protease activity is vital for the replication and assembly of the virus and therefore r... Read More about A comparative analysis of the fluorescence properties of the wild-type and active site mutants of the hepatitis C virus autoprotease NS2-3.

Determinants of hepatitis C virus p7 ion channel function and drug sensitivity identified in vitro (2009)
Journal Article
StGelais, C., Foster, T. L., Verow, M., Atkins, E., Fishwick, C. W. G., Rowlands, D., …Griffin, S. (2009). Determinants of hepatitis C virus p7 ion channel function and drug sensitivity identified in vitro. Journal of Virology, 83(16), 7970-7981. https://doi.org/10.1128/jvi.00521-09

Hepatitis C virus (HCV) chronically infects 170 million individuals, causing severe liver disease. Although antiviral chemotherapy exists, the current regimen is ineffective in 50% of cases due to high levels of innate virus resistance. New, virus-sp... Read More about Determinants of hepatitis C virus p7 ion channel function and drug sensitivity identified in vitro.

Morphological characteristics of the limbal epithelial crypt (2006)
Journal Article
Shanmuganathan, V. A., Foster, T., Kulkarni, B. B., Hopkinson, A., Gray, T., Powe, D. G., …Dua, H. S. (2007). Morphological characteristics of the limbal epithelial crypt. British Journal of Ophthalmology, 91(4), 514-519. https://doi.org/10.1136/bjo.2006.102640

Aim: In 2005 we reported the discovery of a novel anatomical structure at the limbus, which we termed the limbal epithelial crypt (LEC). The purpose of this study was to further evaluate the distribution, immunophenotypical, and ultra structural char... Read More about Morphological characteristics of the limbal epithelial crypt.