And we got the answer from the one and only #microbetv.bsky.social
Vincent said that the stability of enteric corona/torovirus envelopes has not been studied in a systematic way, so we do not appear to know what allows these enveloped viruses to cause GI infection.

But what about viruses with lots of genome space? I must admit, I am a little bit hazy on the synthesis and maturation pathways of herpesvirus glycoproteins, but I guess if anything uses a viral protease for glycoprotein priming, then it would be those guys.

Thinking about it afterwards, my best guess would be that using a viral protease for glycoprotein priming might be unlikely, because coding an enzyme dedicated to that one specific process would maybe take up too much space on the genome. Better to use a host protease for free, in a sense.

I was presenting examples of virus glycoprotein priming (like gp160-> gp120 + gp41), and the question was whether this priming is sometimes done by a viral (not host) protease. I said I did not know any examples, but I could not say it was entirely impossible.

I played your answer to the students this morning, introducing you as Earth's Virology Professor, of course!
But I got another question later on in the class, this time related to attachment/entry.

Thanks Vincent!

Teleportation

My guess would be that the M protein might stabilize the lipid bilayer, and make it resistant to bile salts, but is this really the case?

Horizon Europe 2026/27 has a call specifically for developing new small molecule antivirals against viruses with pandemic potential. Just sayin'.

I just got quoted 4200 euros article processing charge from a middling journal.

Thank you for coming to my TED Talk 🎤

If you’ve read this far and still need convincing, please check out our preprint arxiv.org/abs/2511.04820 and this infographic: doi.org/10.5281/zeno...
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