Virology - Blog Posts

Talent 2030 hosts an annual competition for girls aged 11-18 in the UK to involve themselves in the future of engineering. This year I entered with an essay on the use of engineering to cure cancer, and thought I’d provide the article links I used for research. It’s actually a really interesting topic to delve into if you’re curious 

http://www.popsci.com/fda-approves-first-drug-that-treats-cancer-with-an-engineered-virus

http://fusion.net/story/155183/herpes-fights-cancer-virotherapy-measles-smallpox-cure-cancer/

https://www.standup2cancer.org/dream_teams/view/bioengineering_and_clinical_applications_of_circulating_tumor_cell_chip

https://www.scientificamerican.com/article/a-chip-against-cancer/

What do you name a virus that is 1,000 times larger than the flu virus, has 200 times as many genes, and 93% of those genes are previously unknown to science? The mythical Pandora’s Box seemed an appropriate inspiration, and so the genus was dubbed Pandoravirus.  These extra-large viruses may have been missed in the past because of their size, and were likely thought to be bacteria. Pandoraviruses do not behave typically, and may re-open the conversation regarding viruses as a life form. More info: http://bit.ly/1bwvYuY Image via Chantal Abergel and Jean-Michel Claverie

Please bring me a good news 🤞

WhO wiLL WiN??

Toxin vs Virus

Who do you think will win?

Viruses support photosynthesis in bacteria: An evolutionary advantage?

Viruses propagate by infecting a host cell and reproducing inside. This not only affects humans and animals, but bacteria as well. This type of virus is called bacteriophage. They carry so called auxiliary metabolic genes in their genome, which are responsible for producing certain proteins that give the virus an advantage. Researchers at the University of Kaiserslautern and the Ruhr University Bochum have analysed the structure of such a protein more closely. It appears to stimulate the photosynthesis of host bacteria. The study has now been published in the journal The Journal of Biological Chemistry.

Raphael Gasper, Julia Schwach, Jana Hartmann, Andrea Holtkamp, Jessica Wiethaus, Natascha Riedel, Eckhard Hofmann, Nicole Frankenberg-Dinkel. Auxiliary metabolic genes- Distinct Features of Cyanophage-encoded T-type Phycobiliprotein Lyase θCpeT. Journal of Biological Chemistry, 2017; jbc.M116.769703 DOI: 10.1074/jbc.M116.769703

The association between the virus protein and bacterial pigment is incredibly stable. Furthermore, the complex is highly fluorescent. Credit: AG Frankenberg-Dinkel

Scientists show how drug binds with ‘hidden pocket’ on flu virus

A new study led by scientists at The Scripps Research Institute (TSRI) is the first to show exactly how the drug Arbidol stops influenza infections. The research reveals that Arbidol stops the virus from entering host cells by binding within a recessed pocket on the virus.

The researchers believe this new structural insight could guide the development of future broad-spectrum therapeutics that would be even more potent against influenza virus.

“This is a very interesting molecule, and now we know where it binds and precisely how it works,” said study senior author Ian Wilson, Hanson Professor of Structural Biology, chair of the Department of Integrative Structural and Computational Biology and member of the Skaggs Institute for Chemical Biology at TSRI.

The study was published in the journal Proceedings of the National Academy of Sciences.

Rameshwar U. Kadam, Ian A. Wilson. Structural basis of influenza virus fusion inhibition by the antiviral drug Arbidol. Proceedings of the National Academy of Sciences, 2016; 201617020 DOI: 10.1073/pnas.1617020114

This is a 3-dimensional illustration showing the different features of an influenza virus, including the surface proteins hemagglutinin (HA) and neuraminidase (NA)/CDC

Vexing Virus Shields

Around 36 million people worldwide have HIV. Scientists are trying to develop an HIV vaccine using antibodies, molecules our bodies make to target and tag invading particles. Researchers have found that rabbits exposed to a strain of HIV produce antibodies targeting a specific part of the virus: a hole in its glycan shield. This shield consists of sugar molecules attached to the outside of the virus, protecting it from attack – the hole is thus a gap in its defences. However, although most HIV strains have a hole in their glycan shields, not many strains have one in the same position as was identified, so different antibodies would need to be developed. The image shows how much certain parts of the glycan shield are conserved between different HIV strains – red being 90–100%, and green 50–60%. This is a step towards vaccines, but the shield remains a challenge in vaccine development.

Written by Esther Redhouse White

Image by Sergey Menis, Laura McCoy and James Voss

The Scripps Research Institute, USA and University of Amsterdam, The Netherlands

Image copyright held by original authors

Research published in Cell Reports, August 2016

Published in eLife, June 2016

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