Research Topics
| Terry JacksonSummaryAffiliation: Institute for Animal Health Country: UK Publications
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Detail Information
Publications
Integrin alphavbeta8 functions as a receptor for foot-and-mouth disease virus: role of the beta-chain cytodomain in integrin-mediated infectionTerry Jackson
Department of Molecular Biology, Institute for Animal Health, Pirbright, Surrey GU24 ONF, United Kingdom
J Virol 78:4533-40. 2004..These data suggest that the beta6 cytodomain is important for maintaining alphavbeta6 in a conformation required for productive infection by FMDV...- Integrin alphavbeta1 is a receptor for foot-and-mouth disease virusTerry Jackson
Department of Molecular Biology, Institute for Animal Health, Pirbright, Surrey GU24 ONF, UK
J Virol 76:935-41. 2002..In addition, data are presented suggesting that amino acid residues near the RGD motif may be important for differentiating between the binding specificities of alphavbeta1 and alphavbeta6... - The epithelial integrin alphavbeta6 is a receptor for foot-and-mouth disease virusT Jackson
Department of Molecular Biology, Institute for Animal Health, Pirbright, Surrey GU24 ONF, United Kingdom
J Virol 74:4949-56. 2000..These studies establish a role for alphavbeta6 as a cellular receptor for FMDV... 
Foot-and-mouth disease virus is a ligand for the high-affinity binding conformation of integrin alpha5beta1: influence of the leucine residue within the RGDL motif on selectivity of integrin bindingT Jackson
Department of Molecular Biology, Institute for Animal Health, Pirbright Laboratory, Ash Road, Pirbright, Surrey GU24 0NF, UK
J Gen Virol 81:1383-91. 2000....- Early events in integrin alphavbeta6-mediated cell entry of foot-and-mouth disease virusStephen Berryman
Mammalian Virology, Institute for Animal Health, Pirbright, Surrey GU24 ONF, United Kingdom
J Virol 79:8519-34. 2005..These findings are all consistent with FMDV infection proceeding via clathrin-dependent endocytosis... - Specificity of the VP1 GH loop of Foot-and-Mouth Disease virus for alphav integrinsAlison Burman
Division of Microbiology, Institute for Animal Health, Pirbright, Surrey, GU24 ONF, United Kingdom
J Virol 80:9798-810. 2006..Taken together, our data suggest that the integrin binding loop of FMDV has most likely evolved for binding to alphavbeta6 with a higher affinity than to alphavbeta3 and alphavbeta8... - The alpha(v)beta6 integrin receptor for Foot-and-mouth disease virus is expressed constitutively on the epithelial cells targeted in cattlePaul Monaghan
Institute for Animal Health, Pirbright Laboratory, Ash Road, Pirbright, Surrey GU24 0NF, UK
J Gen Virol 86:2769-80. 2005..Together, these data suggest that in cattle, alpha(v)beta6, rather than alpha(v)beta3, serves as the major receptor that determines the tropism of FMDV for the epithelia normally targeted by this virus... 
Integrin sub-unit expression in cell cultures used for the diagnosis of foot-and-mouth diseaseDonald P King
Institute for Animal Health, Ash Road, Pirbright, Surrey, GU24 0NF, United Kingdom
Vet Immunol Immunopathol 140:259-65. 2011....- Foot-and-mouth disease virus replicates only transiently in well-differentiated porcine nasal epithelial cellsPradyot Dash
Institute for Animal Health, Pirbright Laboratory, Pirbright, Woking, Surrey GU24 0NF, United Kingdom
J Virol 84:9149-60. 2010.... - A clathrin independent macropinocytosis-like entry mechanism used by bluetongue virus-1 during infection of BHK cellsSarah Gold
Pirbright Laboratory, Institute for Animal Health, Woking, United Kingdom
PLoS ONE 5:e11360. 2010.... - Utility of recombinant integrin alpha v beta6 as a capture reagent in immunoassays for the diagnosis of foot-and-mouth diseaseNigel P Ferris
Institute for Animal Health, Pirbright Laboratory, Woking, Surrey GU24 0NF, UK
J Virol Methods 127:69-79. 2005.... - A dominant-negative mutant of rab5 inhibits infection of cells by foot-and-mouth disease virus: implications for virus entryHelen L Johns
Pirbright Laboratory, Institute for Animal Health, Pirbright, Surrey, United Kingdom
J Virol 83:6247-56. 2009..However, our results suggest that infection may not be exclusive to EE and that a small amount of infection could occur from within PNRE... - Rational engineering of recombinant picornavirus capsids to produce safe, protective vaccine antigenClaudine Porta
The Pirbright Insitute, Pirbright, Woking, United Kingdom
PLoS Pathog 9:e1003255. 2013..Similar strategies that will optimize host cell viability during expression of a foreign toxic gene and/or improve capsid stability could allow the production of safe vaccines for other pathogenic picornaviruses of humans and animals... - Foot-and-mouth disease virus, but not bovine enterovirus, targets the host cell cytoskeleton via the nonstructural protein 3CproHannah Armer
Institute for Animal Health, Woking, Surrey, United Kingdom
J Virol 82:10556-66. 2008..In contrast, infection of cells with another picornavirus, bovine enterovirus, did not affect gamma-tubulin distribution, and the microtubule network remained relatively unaffected... - Arginine-glycine-aspartic acid-specific binding by foot-and-mouth disease viruses to the purified integrin alpha(v)beta3 in vitroT Jackson
Pirbright Laboratory, Institute for Animal Health, Surrey, United Kingdom
J Virol 71:8357-61. 1997.... - Characterization of epitope-tagged foot-and-mouth disease virusJulian Seago
Pirbright Laboratory, Institute for Animal Health, Woking, Surrey, GU24 0NF, UK
J Gen Virol 93:2371-81. 2012..Tagged FMDV offers a feasible alternative to the current methods of vaccine concentration and purification, a potential to develop FMD vaccine conjugates and a unique tool for FMDV research... - Foot-and-mouth disease virus exhibits an altered tropism in the presence of specific immunoglobulins, enabling productive infection and killing of dendritic cellsL Robinson
Pirbright Laboratory, Institute for Animal Health, Woking, Surrey, UK
J Virol 85:2212-23. 2011..Moreover, we propose that DC targeting could prove useful in the development of effective vaccines against FMDV... - Role of the cytoplasmic domain of the beta-subunit of integrin alpha(v)beta6 in infection by foot-and-mouth disease virusL C Miller
Pirbright Laboratory, Institute for Animal Health, Pirbright, Surrey GU24 ONF, United Kingdom
J Virol 75:4158-64. 2001..The importance of endosomal acidification in alpha(v)beta6-mediated infection was confirmed by experiments showing that infection could be blocked by concanamycin A, a specific inhibitor of the vacuolar ATPase... - Foot-and-mouth disease virus induces autophagosomes during cell entry via a class III phosphatidylinositol 3-kinase-independent pathwayStephen Berryman
Institute for Animal Health, Pirbright Laboratories, Woking, Surrey, United Kingdom
J Virol 86:12940-53. 2012..These results suggest that FMDV induces autophagosomes during cell entry to facilitate infection, but not to provide membranes for replication... - Structure and receptor bindingTerry Jackson
Department of Molecular Biology, Institute for Animal Health, Pirbright, Surrey GU24 ONF, UK
Virus Res 91:33-46. 2003 - Efficient production of foot-and-mouth disease virus empty capsids in insect cells following down regulation of 3C protease activityClaudine Porta
Institute for Animal Health, Ash Road, Pirbright, Woking GU24 0NF, UK
J Virol Methods 187:406-12. 2013..Expression was independent of the insect host cell background and leads to capsids that are recognised as authentic by a range of anti-FMDV bovine sera suggesting their feasibility as an alternate vaccine... - Efficient infection of cells in culture by type O foot-and-mouth disease virus requires binding to cell surface heparan sulfateT Jackson
Pirbright Laboratory, Institute for Animal Health, Pirbright, Surrey, United Kingdom
J Virol 70:5282-7. 1996..The results show that entry of type O FMDV into cells is a complex process and suggest that the initial contact with the cell surface is made through heparan sulfate... - Dissecting the roles of VP0 cleavage and RNA packaging in picornavirus capsid stabilization: the structure of empty capsids of foot-and-mouth disease virusS Curry
Pirbright Laboratory, Institute for Animal Health, Surrey, United Kingdom
J Virol 71:9743-52. 1997..A comparison of the putative active sites in FMDV and poliovirus suggests a structural explanation for the sequence specificity of the cleavage reaction... - Perturbations in the surface structure of A22 Iraq foot-and-mouth disease virus accompanying coupled changes in host cell specificity and antigenicityS Curry
Pirbright Laboratory, Institute for Animal Health, Pirbright, Surrey, GU24 0NF, UK
Structure 4:135-45. 1996..Strains of the A22 subtype have been reported to change antigenically when adapted to different growth conditions. To investigate the structural basis of this phenomenon we have determined the structures of two variants of an A22 virus... - The ultrastructure of the developing replication site in foot-and-mouth disease virus-infected BHK-38 cellsPaul Monaghan
Institute for Animal Health, Ash Road, Pirbright, Woking, Surrey GU24 0NF, UK
J Gen Virol 85:933-46. 2004..With conventional fixation, FMDV particles were not seen; however, following high-pressure freezing and freeze-substitution, many clusters of virus-like particles were seen... - Foot-and-mouth disease virus forms a highly stable, EDTA-resistant complex with its principal receptor, integrin alphavbeta6: implications for infectiousnessDanielle DiCara
Centre for Tumour Biology, Barts and the London Queen Mary s Medical and Dental School, Charterhouse Square, London EC1M 6BQ, United Kingdom
J Virol 82:1537-46. 2008..An ability to induce such stable complexes with its cellular receptor is likely to contribute significantly to the high infectiousness of FMDV... - Guinea pig-adapted foot-and-mouth disease virus with altered receptor recognition can productively infect a natural hostJose I Núñez
Centro de Biologia Molecular Severo Ochoa, Cantoblanco, 28049 Madrid, Spain
J Virol 81:8497-506. 2007..These observations illustrate how the appearance of minority variant viruses in an unnatural host can result in the dominance of these viruses on reinfection of the original host species... - Integrin alpha v beta 6 is an RGD-dependent receptor for coxsackievirus A9Cigdem H Williams
Department of Biological Sciences, University of Essex, Colchester CO4 3SQ, United Kingdom
J Virol 78:6967-73. 2004..Thus, integrin alpha(v)beta(6) is an RGD-dependent receptor for CAV9 and may be important in natural CAV9 infections... - Structure of Foot-and-mouth disease virus serotype A10 61 alone and complexed with oligosaccharide receptor: receptor conservation in the face of antigenic variationElizabeth E Fry
Division of Structural Biology, The Henry Wellcome Building for Genomic Medicine, Roosevelt Drive, Headington, Oxford OX3 7BN, UK
J Gen Virol 86:1909-20. 2005..Heparin bound at a similar site and in a similar conformation to that seen in the analogous complex with O(1)BFS, although the binding had a lower affinity and was more ionic...