Ervin Fodor is a British virologist of Hungarian origin born in Czechoslovakia. He is Professor of Virology holding the position of reader in experimental pathology in the Sir William Dunn School of Pathology at the University of Oxford. He is also a professorial fellow at Exeter College, Oxford.
Fodor has an MSc in Chemical Engineering (Slovak University of Technology in Bratislava) and a DPhil in Pathology (University of Oxford). [1] [2]
After postdoctoral studies at the Icahn School of Medicine at Mount Sinai New York and the Sir William Dunn School of Pathology at the University of Oxford, Fodor has been awarded a MRC Senior Non-Clinical Research Fellowship in 2002 followed by a RCUK Academic Fellowship in 2008. [2]
He was appointed as university lecturer in 2011 and then as reader at the University of Oxford with the title of professor of virology. [2]
Fodor's research focuses on the molecular biology of influenza viruses. [3] [4] [5] An early highlight of his work was the development of a reverse genetics system to generate recombinant influenza viruses following plasmid transfection. [6] This technology, developed in collaboration with Peter Palese and Adolfo García-Sastre at the Icahn School of Medicine and George Brownlee at the University of Oxford, was then used to generate live attenuated influenza virus vaccines that are also used in the UK National Childhood Flu Immunisation Programme. [7] His more recent work focuses on the molecular mechanisms used by influenza viruses to copy their genetic information stored in molecules of RNA, interactions of influenza viruses with the host cell and cellular responses to viral infection. [8] [9] [10] In collaboration with Jonathan Grimes from the Division of Structural Biology at the University of Oxford he contributed to understanding the structural basis of influenza virus RNA synthesis by solving structures of the influenza virus RNA polymerase complex. [11] [12] [13] [14]
He is the recipient of the 2019 AstraZeneca Award from the Biochemical Society. [15] The award was presented on 20–22 November 2019 in London, UK [16] at the meeting of the Biochemical Society entitled‘Transcriptions in Health and Disease’ where Fodor delivered a lecture entitled 'The influenza virus RNA polymerase'.
Fodor is a fellow of the Academy of Medical Sciences [17] and was elected as a member of EMBO in 2021. [18] [19]
In molecular biology, RNA polymerase, or more specifically DNA-directed/dependent RNA polymerase (DdRP), is an enzyme that catalyzes the chemical reactions that synthesize RNA from a DNA template.
Influenza A virus (IAV) is a pathogen that causes the flu in birds and some mammals, including humans. It is an RNA virus whose subtypes have been isolated from wild birds. Occasionally, it is transmitted from wild to domestic birds, and this may cause severe disease, outbreaks, or human influenza pandemics.
Defective interfering particles (DIPs), also known as defective interfering viruses, are spontaneously generated virus mutants in which a critical portion of the particle's genome has been lost due to defective replication or non-homologous recombination. The mechanism of their formation is presumed to be as a result of template-switching during replication of the viral genome, although non-replicative mechanisms involving direct ligation of genomic RNA fragments have also been proposed. DIPs are derived from and associated with their parent virus, and particles are classed as DIPs if they are rendered non-infectious due to at least one essential gene of the virus being lost or severely damaged as a result of the defection. A DIP can usually still penetrate host cells, but requires another fully functional virus particle to co-infect a cell with it, in order to provide the lost factors.
Orthomyxoviridae is a family of negative-sense RNA viruses. It includes seven genera: Alphainfluenzavirus, Betainfluenzavirus, Gammainfluenzavirus, Deltainfluenzavirus, Isavirus, Thogotovirus, and Quaranjavirus. The first four genera contain viruses that cause influenza in birds and mammals, including humans. Isaviruses infect salmon; the thogotoviruses are arboviruses, infecting vertebrates and invertebrates. The Quaranjaviruses are also arboviruses, infecting vertebrates (birds) and invertebrates (arthropods).
Polyadenylation is the addition of a poly(A) tail to an RNA transcript, typically a messenger RNA (mRNA). The poly(A) tail consists of multiple adenosine monophosphates; in other words, it is a stretch of RNA that has only adenine bases. In eukaryotes, polyadenylation is part of the process that produces mature mRNA for translation. In many bacteria, the poly(A) tail promotes degradation of the mRNA. It, therefore, forms part of the larger process of gene expression.
Nucleoproteins are proteins conjugated with nucleic acids. Typical nucleoproteins include ribosomes, nucleosomes and viral nucleocapsid proteins.
Spanish flu research concerns studies regarding the causes and characteristics of the Spanish flu, a variety of influenza that in 1918 was responsible for the worst influenza pandemic in modern history. Many theories about the origins and progress of the Spanish flu persisted in the literature, but it was not until 2005, when various samples of lung tissue were recovered from American World War I soldiers and from an Inupiat woman buried in permafrost in a mass grave in Brevig Mission, Alaska, that significant genetic research was made possible.
RNA-dependent RNA polymerase (RdRp) or RNA replicase is an enzyme that catalyzes the replication of RNA from an RNA template. Specifically, it catalyzes synthesis of the RNA strand complementary to a given RNA template. This is in contrast to typical DNA-dependent RNA polymerases, which all organisms use to catalyze the transcription of RNA from a DNA template.
AlkB (Alkylation B) is a protein found in E. coli, induced during an adaptive response and involved in the direct reversal of alkylation damage. AlkB specifically removes alkylation damage to single stranded (SS) DNA caused by SN2 type of chemical agents. It efficiently removes methyl groups from 1-methyl adenines, 3-methyl cytosines in SS DNA. AlkB is an alpha-ketoglutarate-dependent hydroxylase, a superfamily non-haem iron-containing proteins. It oxidatively demethylates the DNA substrate. Demethylation by AlkB is accompanied with release of CO2, succinate, and formaldehyde.
A virus is a tiny infectious agent that reproduces inside the cells of living hosts. When infected, the host cell is forced to rapidly produce thousands of identical copies of the original virus. Unlike most living things, viruses do not have cells that divide; new viruses assemble in the infected host cell. But unlike simpler infectious agents like prions, they contain genes, which allow them to mutate and evolve. Over 4,800 species of viruses have been described in detail out of the millions in the environment. Their origin is unclear: some may have evolved from plasmids—pieces of DNA that can move between cells—while others may have evolved from bacteria.
Cleavage and polyadenylation specificity factor subunit 4 is a protein that in humans is encoded by the CPSF4 gene.
Professor George Gow Brownlee FRS FMedSci is a British pathologist and Fellow of Lincoln College, Oxford.
Wendy Sue Fox is a British virologist. She is currently head of Department of Infectious Disease and Chair in Influenza Virology at Imperial College London. She leads a team of scientists studying the influenza virus and its physiology and morphology to discover novel vaccines. In particular, they are trying to understand more about influenza virus mutations, and how they can allow scientists to create new vaccines against possible flu pandemics.
Encapsulin nanocompartments, or encapsulin protein cages, are spherical bacterial organelle-like compartments roughly 25-30 nm in diameter that are involved in various aspects of metabolism, in particular protecting bacteria from oxidative stress. Encapsulin nanocompartments are structurally similar to the HK97 bacteriophage and their function depends on the proteins loaded into the nanocompartment. The sphere is formed from 60 or 180 copies of a single protomer, termed encapsulin. Their structure has been studied in great detail using X-ray crystallography and cryo-electron microscopy.
Pneumoviridae is a family of negative-strand RNA viruses in the order Mononegavirales. Humans, cattle, and rodents serve as natural hosts. Respiratory tract infections are associated with member viruses such as human respiratory syncytial virus. There are five species in the family which are divided between the genera Metapneumovirus and Orthopneumovirus. The family used to be considered as a sub-family of Paramyxoviridae, but has been reclassified as of 2016.
Paul Babitzke is a Professor of Biochemistry and Molecular Biology and Director of the Center for RNA Molecular Biology at Pennsylvania State University.
The first step of transcription for some negative, single-stranded RNA viruses is cap snatching, in which the first 10 to 20 residues of a host cell RNA are removed (snatched) and used as the 5′ cap and primer to initiate the synthesis of the nascent viral mRNA. The viral RNA-dependent RNA polymerase (RdRp) can then proceed to replicate the negative-sense genome from the positive-sense template. Cap-snatching also explains why some viral mRNA have 5’ terminal extensions of 10-20 nucleotides that are not encoded for in the genome. Examples of viruses that engage in cap-snatching include influenza viruses (Orthomyxoviridae), Lassa virus (Arenaviridae), hantaan virus (Hantaviridae) and rift valley fever virus (Phenuiviridae). Most viruses snatch 15-20 nucleotides except for the families Arenaviridae and Nairoviridae and the genus Thogotovirus (Orthomyxoviridae) which use a shorter strand.
Negative-strand RNA viruses are a group of related viruses that have negative-sense, single-stranded genomes made of ribonucleic acid. They have genomes that act as complementary strands from which messenger RNA (mRNA) is synthesized by the viral enzyme RNA-dependent RNA polymerase (RdRp). During replication of the viral genome, RdRp synthesizes a positive-sense antigenome that it uses as a template to create genomic negative-sense RNA. Negative-strand RNA viruses also share a number of other characteristics: most contain a viral envelope that surrounds the capsid, which encases the viral genome, −ssRNA virus genomes are usually linear, and it is common for their genome to be segmented.
Enisamium iodide is a derivative of isonicotinic acid. Based on its systematic chemical name of N-benzyl-1-methylpyridin-1-ium-4-carboxamide iodide, the shortened name carbabenzpiride is sometimes used. Enisamium iodide is a registered antiviral drug sold in Ukraine, Kazakhstan, Mongolia, Belarus, and other Eastern European countries under the trade names Amizon, Amizon Max, Amizonchik.
Susan Mary Lea is a British biologist who serves as chief of the center for structural biology at the National Cancer Institute. Her research investigates host-pathogen interactions and biomolecular pathways. She was elected a Fellow of the Royal Society in 2022.
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