Andrew J. P. Scott

ORCID: 0000-0002-7989-2675
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About
Contact & Profiles
Research Areas
  • Bacteriophages and microbial interactions
  • Viral gastroenteritis research and epidemiology
  • Trace Elements in Health
  • Plant Virus Research Studies
  • RNA and protein synthesis mechanisms
  • Bacillus and Francisella bacterial research
  • Animal Disease Management and Epidemiology
  • Transgenic Plants and Applications
  • Historical Medical Research and Treatments
  • Biological Activity of Diterpenoids and Biflavonoids
  • Corrosion Behavior and Inhibition
  • Iron Metabolism and Disorders
  • Plant-derived Lignans Synthesis and Bioactivity
  • Virus-based gene therapy research
  • Viral Infections and Immunology Research
  • Biomedical Ethics and Regulation
  • T-cell and Retrovirus Studies
  • Bacterial Genetics and Biotechnology
  • Enzyme Structure and Function
  • Plant and Fungal Interactions Research
  • Vaccine Coverage and Hesitancy
  • Heavy metals in environment
  • Phytochemistry and Biological Activities
  • Evolutionary Game Theory and Cooperation
  • Plant Stress Responses and Tolerance

Durham University
2017-2025

University of Leeds
2020-2022

Institute of Structural and Molecular Biology
2021

University of California, Los Angeles
2016

Revolution in an RNA-packaging capsid Artificial nucleocapsid proteins, which could be analogous to those used by viruses package their genomes, are a promising way protect and deliver RNAs. Using escalating challenge nucleases, Tetter et al. evolved protein that forms multimeric, spherical cages into highly efficient selectively packages its own encoding RNA. Cryo–electron microscopy of the final design intermediates revealed stepwise expansion size, enabled destabilizing amino acid...

10.1126/science.abg2822 article EN Science 2021-06-10

It has been challenging to test how proteins acquire specific metals in cells. The speciation of metalation is thought depend on the preferences for different competing at intracellular metal-availabilities. This implies mis-metalation may occur if become mis-matched metal-availabilities heterologous Here we use a cyanobacterial MnII-cupin (MncA) as metal trap, predictions metalation. By re-folding MncA buffered metals, metal-preferences are determined. Relating estimated using cellular...

10.1038/s41467-025-56199-w article EN cc-by Nature Communications 2025-01-18

Abstract Viruses are ubiquitous pathogens of global impact. Prompted by the hypothesis that their earliest progenitors recruited host proteins for virion formation, we have used stringent laboratory evolution to convert a bacterial enzyme lacking affinity nucleic acids into an artificial nucleocapsid efficiently packages and protects multiple copies its own encoding mRNA. Revealing remarkable convergence on molecular hallmarks natural viruses, accompanying changes reorganized protein...

10.1101/2020.12.23.423990 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2020-12-23

Abstract The secondary structures of the bacteriophage MS2 ssRNA genome, frozen in defined states, were determined with minimal perturbation using constraints from X-ray synchrotron footprinting (XRF). footprints gRNA virion and as transcript are consistent single, dominant but distinct conformations, reveal presence multiple Packaging Signals potentially involved assembly regulation that have not been detected by other techniques. XRF also reveals dramatic effect unique Maturation Protein...

10.1101/2021.08.10.455819 preprint EN cc-by-nd bioRxiv (Cold Spring Harbor Laboratory) 2021-08-10

Single-stranded RNA viral genomes (gRNA) are dynamic molecules that permit packaging into virions and their subsequent extrusion during infection. For viruses with such genomes, we discovered a previously unsuspected mechanism regulates assembly. This regulation is the result of multiple cognate coat protein (CP)–gRNA contacts distributed across RNA. Collectively, these interactions make assembly highly efficient specific. The regions gRNA signals (PSs) driving this potential drug targets,...

10.3390/proceedings2020050109 article EN cc-by 2020-06-30

Recent developments in cryo-electron microscopy (cryo-EM) hardware along with continuously evolving software tools have led to the discovery of many novel structures that it was not possible solve until now, resulting what is termed “the resolution revolution”. In structural virology, has also a re-evaluation known structures. Most virion solved by X-ray crystallography or cryo-EM are focused on capsid protein (CP) as result application icosahedral symmetry averaging “improve” electron...

10.1099/acmi.ac2020.po0686 article EN cc-by-nc Access Microbiology 2020-07-01

Many single-stranded (ss)RNA viruses regulate their assembly into infectious virions by forming multiple cognate coat protein (CP)-genome contacts at sites termed Packaging Signals (PSs). These could have potentially negative effects on infectivity stabilizing the virion so much that it cannot release its genome start of an infection. The secondary structures MS2 ssRNA (gRNA) frozen in defined states were determined using constraints from X-ray synchrotron footprinting. Comparison these RNA...

10.2139/ssrn.4116298 article EN SSRN Electronic Journal 2022-01-01
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