If you are looking for a PhD in the UK, please check out the LIDo program - www.lido-dtp.ac.uk/apply.
If you are interested in viruses and making genetically edited salmon, please look up my icase project.
International students are welcome to apply!
Please reach out if you have questions.

If you are interested in influenza emergence, please check out and use the beautiful figures all made by @fcapelastegui.bsky.social.

Excited to present the first review from my lab!
Which mutations allow H5 influenza to jump into humans or other mammals? How close is H5 to a pandemic? This review has the answers and explains the molecular mechanism behind the mutations.
Led by @fcapelastegui.bsky.social.
doi.org/10.1099/jgv....

Start of the year lab meeting today. We had memes. Highly recommend this for every lab meeting. My students unsurprisingly came up with better ones than this.

This is a really beautiful figure showing avian and mammalian spread of H5N1 in South America from Uhart et al. www.nature.com/articles/s41...

Registration is now open for the Influenza Update Meeting 2023! Register here - t.co/GRscOLi5dI
Submit your abstract here - t.co/5ADTJqwCX8
Small, friendly and cheap!
Great keynote speaker as well.

Big thanks from
@error-prone.bsky.social
and me to Liv for RNA bits. Becky, Rebecca + Laury for mouse work. Ecco+Ervin for CRISPR. Ollie + Kseniya for viral finishing touches.
@peacockflu.bsky.social for loving mutations. Prof Barclay was, as always, the boss. Wait – what about chickens?! 11/n

What is more there are a lot more mutations in the same dimer interface e.g PB2 G74S, PA E349K etc. all of which have been shown to lead to mouse adaptation. Stopping dimerization allowing use of suboptimal ANP32s is a good mechanism explaining all these mutations. 9/n

FluPol also forms a symmetric dimer and our mutations sit in the interface. We showed that PB1 K577E especially breaks this dimer – see also t.co/4CFPiR969C. We theorised that breaking the symmetric dimer may push more FluPol into the asymmetric dimer form allowing it to use a suboptimal ANP32. 6/n

To prove it, CRISPR maestro, Ecco, made a triple knockout without ANP32A, B and E. No ANP32 = no virus! So what’s the mechanism? Dimers! ANP32 binds to the flu polymerase in an asymmetric dimer. The mutations increase binding of ANP32E to the asymmetric dimer but that’s not the whole story. 5/n

So, we evolved avian flu (technically a PR8/AIV hybrid) in ANP32A/B knock-out cells and found good growth after just 2 passages! Tracked down two mutations PB1 K577E and PA Q556R.
Two possibilities:
1. Flu found a new host factor to use.
2. Flu no longer needs to use ANP32.
3/n

Previously, Ecco made double knock-out (DKO) cells with ANP32A and ANP32B knocked out and showed these were essential host factors for flu. Except, when growing virus, there was a teeny little bump after a few days… Weird. 2/n

***PAPER ALERT***
So excited to have this out
@error-prone.bsky.social joint production - www.nature.com/articles/s41...
We asked what happens if you take away a key host factor from influenza?
What cool virology can you uncover?
Polymerase Dimers! ANP32 in mice and chickens?!
Read on for more...