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Article ; Online: Picornaviruses: A View from 3A.

Jackson, Terry / Belsham, Graham J

2021 Volume 13, Issue 3

Abstract: Picornaviruses are comprised of a positive-sense RNA genome surrounded by a protein shell (or capsid). They are ubiquitous in vertebrates and cause a wide range of important human and animal diseases. The genome encodes a single large polyprotein that is ...

Abstract	Picornaviruses are comprised of a positive-sense RNA genome surrounded by a protein shell (or capsid). They are ubiquitous in vertebrates and cause a wide range of important human and animal diseases. The genome encodes a single large polyprotein that is processed to structural (capsid) and non-structural proteins. The non-structural proteins have key functions within the viral replication complex. Some, such as 3D
MeSH term(s)	Genome, Viral ; Humans ; Picornaviridae/chemistry ; Picornaviridae/classification ; Picornaviridae/genetics ; Picornaviridae/physiology ; Protein Transport ; RNA, Viral/genetics ; Viral Proteins/classification ; Viral Proteins/genetics ; Viral Proteins/metabolism ; Virus Replication/physiology
Chemical Substances	RNA, Viral ; Viral Proteins
Language	English
Publishing date	2021-03-11
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2516098-9
ISSN	1999-4915 ; 1999-4915
ISSN (online)	1999-4915
ISSN	1999-4915
DOI	10.3390/v13030456
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Picornaviruses: A View from 3A

Jackson, Terry / Belsham, Graham J

Viruses. 2021 Mar. 11, v. 13, no. 3

2021

Abstract	Picornaviruses are comprised of a positive-sense RNA genome surrounded by a protein shell (or capsid). They are ubiquitous in vertebrates and cause a wide range of important human and animal diseases. The genome encodes a single large polyprotein that is processed to structural (capsid) and non-structural proteins. The non-structural proteins have key functions within the viral replication complex. Some, such as 3Dᵖᵒˡ (the RNA dependent RNA polymerase) have conserved functions and participate directly in replicating the viral genome, whereas others, such as 3A, have accessory roles. The 3A proteins are highly divergent across the Picornaviridae and have specific roles both within and outside of the replication complex, which differ between the different genera. These roles include subverting host proteins to generate replication organelles and inhibition of cellular functions (such as protein secretion) to influence virus replication efficiency and the host response to infection. In addition, 3A proteins are associated with the determination of host range. However, recent observations have challenged some of the roles assigned to 3A and suggest that other viral proteins may carry them out. In this review, we revisit the roles of 3A in the picornavirus life cycle. The 3AB precursor and mature 3A have distinct functions during viral replication and, therefore, we have also included discussion of some of the roles assigned to 3AB.
Keywords	Picornaviridae ; RNA ; RNA-directed RNA polymerase ; capsid ; host range ; humans ; organelles ; polyproteins ; protein secretion ; viral genome ; virus replication
Language	English
Dates of publication	2021-0311
Publishing place	Multidisciplinary Digital Publishing Institute
Document type	Article
Note	NAL-light
ZDB-ID	2516098-9
ISSN	1999-4915
ISSN	1999-4915
DOI	10.3390/v13030456
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Foot-and-mouth disease virus: Prospects for using knowledge of virus biology to improve control of this continuing global threat.

Belsham, Graham J / Kristensen, Thea / Jackson, Terry

Virus research

2020 Volume 281, Page(s) 197909

Abstract: Understanding of the biology of foot-and-mouth disease virus (FMDV) has grown considerably since the nucleotide sequence of the viral RNA was determined. The ability to manipulate the intact genome and also to express specific parts of the genome ... ...

Abstract	Understanding of the biology of foot-and-mouth disease virus (FMDV) has grown considerably since the nucleotide sequence of the viral RNA was determined. The ability to manipulate the intact genome and also to express specific parts of the genome individually has enabled detailed analyses of viral components, both RNA and protein. Such studies have identified the requirements for specific functional elements for virus replication and pathogenicity. Furthermore, information about the functions of individual virus proteins has enabled the rational design of cDNA cassettes to express non-infectious empty capsid particles that can induce protective immunity in the natural host animals and thus represent new vaccine candidates. Similarly, attempts to block specific virus activities using antiviral agents have also been performed. However, currently, only the well-established, chemically inactivated FMDV vaccines are commercially available and suitable for use to combat this important disease of livestock animals. These vaccines, despite certain shortcomings, have been used very successfully (e.g. in Europe) to control the disease but it still remains endemic in much of Africa, southern Asia and the Middle East. Hence there remains a significant risk of reintroduction of the disease into highly susceptible animal populations with enormous economic consequences.
MeSH term(s)	Animals ; Foot-and-Mouth Disease/genetics ; Foot-and-Mouth Disease/prevention & control ; Foot-and-Mouth Disease/virology ; Foot-and-Mouth Disease Virus/genetics ; Foot-and-Mouth Disease Virus/immunology ; Genome, Viral/genetics ; Viral Proteins/genetics ; Viral Proteins/immunology ; Viral Vaccines/immunology
Chemical Substances	Viral Proteins ; Viral Vaccines
Language	English
Publishing date	2020-02-29
Publishing country	Netherlands
Document type	Journal Article ; Review
ZDB-ID	605780-9
ISSN	1872-7492 ; 0168-1702
ISSN (online)	1872-7492
ISSN	0168-1702
DOI	10.1016/j.virusres.2020.197909
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Article: Foot-and-mouth disease virus: Prospects for using knowledge of virus biology to improve control of this continuing global threat

Belsham, Graham J / Kristensen, Thea / Jackson, Terry

Virus research. 2020 May, v. 281

2020

Abstract	Understanding of the biology of foot-and-mouth disease virus (FMDV) has grown considerably since the nucleotide sequence of the viral RNA was determined. The ability to manipulate the intact genome and also to express specific parts of the genome individually has enabled detailed analyses of viral components, both RNA and protein. Such studies have identified the requirements for specific functional elements for virus replication and pathogenicity. Furthermore, information about the functions of individual virus proteins has enabled the rational design of cDNA cassettes to express non-infectious empty capsid particles that can induce protective immunity in the natural host animals and thus represent new vaccine candidates. Similarly, attempts to block specific virus activities using antiviral agents have also been performed. However, currently, only the well-established, chemically inactivated FMDV vaccines are commercially available and suitable for use to combat this important disease of livestock animals. These vaccines, despite certain shortcomings, have been used very successfully (e.g. in Europe) to control the disease but it still remains endemic in much of Africa, southern Asia and the Middle East. Hence there remains a significant risk of reintroduction of the disease into highly susceptible animal populations with enormous economic consequences.
Keywords	Foot-and-mouth disease virus ; RNA ; animals ; antiviral agents ; capsid ; disease control ; economic impact ; genome ; immunity ; livestock diseases ; nucleotide sequences ; pathogenicity ; risk ; vaccines ; viral proteins ; virus replication ; viruses ; Africa ; Europe ; Middle East ; South Asia
Language	English
Dates of publication	2020-05
Publishing place	Elsevier B.V.
Document type	Article
ZDB-ID	605780-9
ISSN	1872-7492 ; 0168-1702
ISSN (online)	1872-7492
ISSN	0168-1702
DOI	10.1016/j.virusres.2020.197909
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Article ; Online: Sickle Cell Disease and Gene Therapy - Patient and Physician Perspectives.

DeBaun, Michael / Heeney, Matthew / Jackson, Terry / Longo, Dan / Love, Melesa / Love, Trinity / Okwo, Phillip / Thompson, Alexis / Trimnell, Cassandra / Woolford, Teonna

The New England journal of medicine

2022 Volume 387, Issue 13, Page(s) e28

MeSH term(s)	Anemia, Sickle Cell/genetics ; Anemia, Sickle Cell/psychology ; Anemia, Sickle Cell/therapy ; Attitude of Health Personnel ; Attitude to Health ; Genetic Therapy/methods ; Genetic Therapy/psychology ; Humans ; Patients/psychology ; Physicians/psychology
Language	English
Publishing date	2022-09-28
Publishing country	United States
Document type	Journal Article
ZDB-ID	207154-x
ISSN	1533-4406 ; 0028-4793
ISSN (online)	1533-4406
ISSN	0028-4793
DOI	10.1056/NEJMp2212269
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Article ; Online: The Cellular Chaperone Heat Shock Protein 90 Is Required for Foot-and-Mouth Disease Virus Capsid Precursor Processing and Assembly of Capsid Pentamers.

Newman, Joseph / Asfor, Amin S / Berryman, Stephen / Jackson, Terry / Curry, Stephen / Tuthill, Tobias J

Journal of virology

2018 Volume 92, Issue 5

Abstract: Productive picornavirus infection requires the hijacking of host cell pathways to aid with the different stages of virus entry, synthesis of the viral polyprotein, and viral genome replication. Many picornaviruses, including foot-and-mouth disease virus ( ...

Abstract	Productive picornavirus infection requires the hijacking of host cell pathways to aid with the different stages of virus entry, synthesis of the viral polyprotein, and viral genome replication. Many picornaviruses, including foot-and-mouth disease virus (FMDV), assemble capsids via the multimerization of several copies of a single capsid precursor protein into a pentameric subunit which further encapsidates the RNA. Pentamer formation is preceded by co- and posttranslational modification of the capsid precursor (P1-2A) by viral and cellular enzymes and the subsequent rearrangement of P1-2A into a structure amenable to pentamer formation. We have developed a cell-free system to study FMDV pentamer assembly using recombinantly expressed FMDV capsid precursor and 3C protease. Using this assay, we have shown that two structurally different inhibitors of the cellular chaperone heat shock protein 90 (hsp90) impeded FMDV capsid precursor processing and subsequent pentamer formation. Treatment of FMDV permissive cells with the hsp90 inhibitor prior to infection reduced the endpoint titer by more than 10-fold while not affecting the activity of a subgenomic replicon, indicating that translation and replication of viral RNA were unaffected by the drug.
MeSH term(s)	3C Viral Proteases ; Animals ; Benzoquinones/pharmacology ; Capsid Proteins/drug effects ; Capsid Proteins/metabolism ; Cell Line ; Cell Survival ; Cell-Free System ; Cricetinae ; Cysteine Endopeptidases/genetics ; Cysteine Endopeptidases/metabolism ; Foot-and-Mouth Disease/metabolism ; Foot-and-Mouth Disease Virus/genetics ; Foot-and-Mouth Disease Virus/growth & development ; Foot-and-Mouth Disease Virus/metabolism ; HSP90 Heat-Shock Proteins/drug effects ; HSP90 Heat-Shock Proteins/metabolism ; Isoxazoles/pharmacology ; Lactams, Macrocyclic/pharmacology ; Molecular Chaperones/metabolism ; Protein Precursors/drug effects ; Protein Precursors/metabolism ; Protein Processing, Post-Translational ; RNA, Viral/genetics ; RNA, Viral/metabolism ; Resorcinols/pharmacology ; Viral Proteins/drug effects ; Viral Proteins/genetics ; Viral Proteins/metabolism ; Virus Assembly/genetics ; Virus Assembly/physiology ; Virus Replication
Chemical Substances	5-(2,4-dihydroxy-5-isopropylphenyl)-4-(4-morpholin-4-ylmethylphenyl)isoxazole-3-carboxylic acid ethylamide ; Benzoquinones ; Capsid Proteins ; HSP90 Heat-Shock Proteins ; Isoxazoles ; Lactams, Macrocyclic ; Molecular Chaperones ; Protein Precursors ; RNA, Viral ; Resorcinols ; Viral Proteins ; 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (001L2FE0M3) ; Cysteine Endopeptidases (EC 3.4.22.-) ; 3C Viral Proteases (EC 3.4.22.28)
Language	English
Publishing date	2018-02-12
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/JVI.01415-17
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Article ; Online: Foot-and-mouth disease virus replicates independently of phosphatidylinositol 4-phosphate and type III phosphatidylinositol 4-kinases.

Berryman, Stephen / Moffat, Katy / Harak, Christian / Lohmann, Volker / Jackson, Terry

The Journal of general virology

2016 Volume 97, Issue 8, Page(s) 1841–1852

Abstract: Picornaviruses form replication complexes in association with membranes in structures called replication organelles. Common themes to emerge from studies of picornavirus replication are the need for cholesterol and phosphatidylinositol 4-phosphate (PI4P). ...

Abstract	Picornaviruses form replication complexes in association with membranes in structures called replication organelles. Common themes to emerge from studies of picornavirus replication are the need for cholesterol and phosphatidylinositol 4-phosphate (PI4P). In infected cells, type III phosphatidylinositol 4-kinases (PI4KIIIs) generate elevated levels of PI4P, which is then exchanged for cholesterol at replication organelles. For the enteroviruses, replication organelles form at Golgi membranes in a process that utilizes PI4KIIIβ. Other picornaviruses, for example the cardioviruses, are believed to initiate replication at the endoplasmic reticulum and subvert PI4KIIIα to generate PI4P. Here we investigated the role of PI4KIII in foot-and-mouth disease virus (FMDV) replication. Our results showed that, in contrast to the enteroviruses and the cardioviruses, FMDV replication does not require PI4KIII (PI4KIIIα and PI4KIIIβ), and PI4P levels do not increase in FMDV-infected cells and PI4P is not seen at replication organelles. These results point to a unique requirement towards lipids at the FMDV replication membranes.
MeSH term(s)	1-Phosphatidylinositol 4-Kinase/metabolism ; Animals ; Cell Line ; Foot-and-Mouth Disease Virus/physiology ; Humans ; Lipid Metabolism ; Phosphatidylinositol Phosphates/metabolism ; Phosphotransferases (Alcohol Group Acceptor)/metabolism ; Virus Replication
Chemical Substances	Phosphatidylinositol Phosphates ; phosphatidylinositol 4-phosphate ; Phosphotransferases (Alcohol Group Acceptor) (EC 2.7.1.-) ; 1-Phosphatidylinositol 4-Kinase (EC 2.7.1.67) ; PI4KIIIalpha protein, human (EC 2.7.1.67) ; phosphatidylinositol 4-kinase IIIbeta, human (EC 2.7.1.67)
Keywords	covid19
Language	English
Publishing date	2016-04-19
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	219316-4
ISSN	1465-2099 ; 0022-1317
ISSN (online)	1465-2099
ISSN	0022-1317
DOI	10.1099/jgv.0.000485
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Article ; Online: The RNA pseudoknots in foot-and-mouth disease virus are dispensable for genome replication, but essential for the production of infectious virus.

Ward, Joseph C / Lasecka-Dykes, Lidia / Neil, Chris / Adeyemi, Oluwapelumi O / Gold, Sarah / McLean-Pell, Niall / Wright, Caroline / Herod, Morgan R / Kealy, David / Warner, Emma / Jackson, Terry / King, Donald P / Tuthill, Tobias J / Rowlands, David J / Stonehouse, Nicola J

PLoS pathogens

2022 Volume 18, Issue 6, Page(s) e1010589

Abstract: Non-coding regions of viral RNA (vRNA) genomes are critically important in the regulation of gene expression. In particular, pseudoknot (PK) structures, which are present in a wide range of RNA molecules, have a variety of roles. The 5' untranslated ... ...

Abstract	Non-coding regions of viral RNA (vRNA) genomes are critically important in the regulation of gene expression. In particular, pseudoknot (PK) structures, which are present in a wide range of RNA molecules, have a variety of roles. The 5' untranslated region (5' UTR) of foot-and-mouth disease virus (FMDV) vRNA is considerably longer than in other viruses from the picornavirus family and consists of a number of distinctive structural motifs that includes multiple (2, 3 or 4 depending on the virus strain) putative PKs linked in tandem. The role(s) of the PKs in the FMDV infection are not fully understood. Here, using bioinformatics, sub-genomic replicons and recombinant viruses we have investigated the structural conservation and importance of the PKs in the FMDV lifecycle. Our results show that despite the conservation of two or more PKs across all FMDVs, a replicon lacking PKs was replication competent, albeit at reduced levels. Furthermore, in competition experiments, GFP FMDV replicons with less than two (0 or 1) PK structures were outcompeted by a mCherry FMDV wt replicon that had 4 PKs, whereas GFP replicons with 2 or 4 PKs were not. This apparent replicative advantage offered by the additional PKs correlates with the maintenance of at least two PKs in the genomes of FMDV field isolates. Despite a replicon lacking any PKs retaining the ability to replicate, viruses completely lacking PK were not viable and at least one PK was essential for recovery of infections virus, suggesting a role for the PKs in virion assembly. Thus, our study points to roles for the PKs in both vRNA replication and virion assembly, thereby improving understanding the molecular biology of FMDV replication and the wider roles of PK in RNA functions.
MeSH term(s)	5' Untranslated Regions ; Animals ; DNA Viruses ; Foot-and-Mouth Disease/genetics ; Foot-and-Mouth Disease Virus/genetics ; Genome, Viral ; RNA, Viral/chemistry ; Virus Replication/genetics
Chemical Substances	5' Untranslated Regions ; RNA, Viral
Language	English
Publishing date	2022-06-06
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7374
ISSN (online)	1553-7374
ISSN	1553-7374
DOI	10.1371/journal.ppat.1010589
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Article ; Online: Mutagenesis Mapping of RNA Structures within the Foot-and-Mouth Disease Virus Genome Reveals Functional Elements Localized in the Polymerase (3D

Lasecka-Dykes, Lidia / Tulloch, Fiona / Simmonds, Peter / Luke, Garry A / Ribeca, Paolo / Gold, Sarah / Knowles, Nick J / Wright, Caroline F / Wadsworth, Jemma / Azhar, Mehreen / King, Donald P / Tuthill, Tobias J / Jackson, Terry / Ryan, Martin D

mSphere

2021 Volume 6, Issue 4, Page(s) e0001521

Abstract: RNA structures can form functional elements that play crucial roles in the replication of positive-sense RNA viruses. While RNA structures in the untranslated regions (UTRs) of several picornaviruses have been functionally characterized, the roles of ... ...

Abstract	RNA structures can form functional elements that play crucial roles in the replication of positive-sense RNA viruses. While RNA structures in the untranslated regions (UTRs) of several picornaviruses have been functionally characterized, the roles of putative RNA structures predicted for protein coding sequences (or open reading frames [ORFs]) remain largely undefined. Here, we have undertaken a bioinformatic analysis of the foot-and-mouth disease virus (FMDV) genome to predict 53 conserved RNA structures within the ORF. Forty-six of these structures were located in the regions encoding the nonstructural proteins (nsps). To investigate whether structures located in the regions encoding the nsps are required for FMDV replication, we used a mutagenesis method, CDLR mapping, where sequential coding segments were shuffled to minimize RNA secondary structures while preserving protein coding, native dinucleotide frequencies, and codon usage. To examine the impact of these changes on replicative fitness, mutated sequences were inserted into an FMDV subgenomic replicon. We found that three of the RNA structures, all at the 3' termini of the FMDV ORF, were critical for replicon replication. In contrast, disruption of the other 43 conserved RNA structures that lie within the regions encoding the nsps had no effect on replicon replication, suggesting that these structures are not required for initiating translation or replication of viral RNA. Conserved RNA structures that are not essential for virus replication could provide ideal targets for the rational attenuation of a wide range of FMDV strains.
MeSH term(s)	Foot-and-Mouth Disease Virus/enzymology ; Foot-and-Mouth Disease Virus/genetics ; Genome, Viral ; Mutagenesis ; Open Reading Frames ; RNA, Viral/chemistry ; RNA, Viral/genetics ; RNA-Dependent RNA Polymerase/genetics ; RNA-Dependent RNA Polymerase/metabolism
Chemical Substances	RNA, Viral ; RNA-Dependent RNA Polymerase (EC 2.7.7.48)
Language	English
Publishing date	2021-07-14
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2379-5042
ISSN (online)	2379-5042
DOI	10.1128/mSphere.00015-21
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Article ; Online: A low-passage insect-cell isolate of bluetongue virus uses a macropinocytosis-like entry pathway to infect natural target cells derived from the bovine host.

Stevens, Lisa M / Moffat, Katy / Cooke, Lyndsay / Nomikou, Kyriaki / Mertens, Peter P C / Jackson, Terry / Darpel, Karin E

The Journal of general virology

2019 Volume 100, Issue 4, Page(s) 568–582

Abstract: Bluetongue virus (BTV) causes an economically important disease in domestic and wildlife ruminants and is transmitted by Culicoides biting midges. In ruminants, BTV has a wide cell tropism that includes endothelial cells of vascular and lymphatic vessels ...

Abstract	Bluetongue virus (BTV) causes an economically important disease in domestic and wildlife ruminants and is transmitted by Culicoides biting midges. In ruminants, BTV has a wide cell tropism that includes endothelial cells of vascular and lymphatic vessels as important cell targets for virus replication, and several cell types of the immune system including monocytes, macrophages and dendritic cells. Thus, cell-entry represents a particular challenge for BTV as it infects many different cell types in widely diverse vertebrate and invertebrate hosts. Improved understanding of BTV cell-entry could lead to novel antiviral approaches that can block virus transmission from cell to cell between its invertebrate and vertebrate hosts. Here, we have investigated BTV cell-entry using endothelial cells derived from the natural bovine host (BFA cells) and purified whole virus particles of a low-passage, insect-cell isolate of a virulent strain of BTV-1. Our results show that the main entry pathway for infection of BFA cells is dependent on actin and dynamin, and shares certain characteristics with macropinocytosis. The ability to use a macropinocytosis-like entry route could explain the diverse cell tropism of BTV and contribute to the efficiency of transmission between vertebrate and invertebrate hosts.
MeSH term(s)	Actins/genetics ; Actins/metabolism ; Animals ; Bluetongue/genetics ; Bluetongue/metabolism ; Bluetongue/physiopathology ; Bluetongue/virology ; Bluetongue virus/genetics ; Bluetongue virus/growth & development ; Bluetongue virus/physiology ; Cattle ; Cattle Diseases/genetics ; Cattle Diseases/metabolism ; Cattle Diseases/physiopathology ; Cattle Diseases/virology ; Cells, Cultured ; Dynamins/genetics ; Dynamins/metabolism ; Endothelial Cells/virology ; Insecta/virology ; Pinocytosis ; Serial Passage ; Sheep ; Sheep Diseases/virology ; Virus Internalization ; Virus Replication
Chemical Substances	Actins ; Dynamins (EC 3.6.5.5)
Language	English
Publishing date	2019-03-07
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	219316-4
ISSN	1465-2099 ; 0022-1317
ISSN (online)	1465-2099
ISSN	0022-1317
DOI	10.1099/jgv.0.001240
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