Carbohydrate-binding is a small profit affair, so proteins often adopt complex multidomain architectures enabling a mechanism known as 'binding cooperativity', where binding to one monomer contributes to the binding affinity of the whole systems

BUT how does it actually work?

🔥 #glycotime 🧵1/4 ⬇️

Most biologics are glycosylated and some of them heavily. In this “fresh off the press" #glycotime preprint we look into how a filter that accounts for glycosylation explicitly in 3D can help reduce lab costs and increase the efficiency of de novo binder design pipelines. Short 🧵 ⬇️ 1/7

Lectins are known to be low affinity binders with relatively broad glycan target preference. In this work live in @commsbio.nature.com we show how Siglecs change this paradigm, acting as molecular precision tools required to fine tune immune response 🤯 #glycotime 🧵⬇️

doi.org/10.1038/s420...

Happy birthday to us! 🥂🎂🥳 We are only 2 yo, but so much #glycotime happened since Dec 2023! ⬇️🧵

We truly appreciate your support, you fabulous glycoengineers around the world and we have so many exciting new tools for you coming up in 2026 to make your 3D glycoforms even better and faster! 🤩

Tuesday #glycotime 🥄🍬

Glycans are a 🔝 example of "disordered" molecules. Inherent flexibility prevents sugars from adopting fixed, unique 3D positions relative to the crystal lattice, so they often are invisible to X-ray diffraction, unless they are bound and thus restrained in place 1/3 🧵

A fab, sunshiny week in 🇩🇰! Great #glycotime 🧪 at the CBM16 in Helsingør, with posters
Bea: regulation of N-glycosylation by OST (doi.org/10.1101/2025...)
Silvia: Siglec-6 high-recision recognition of glycolipids (doi.org/10.1038/s420...)
Ojas: de novo binders design (doi.org/10.64898/202...)

🧵⬇️

Wee thread 🧵⬇️ on our new #glycotime with @siglecdude.bsky.social John Klassen and @glycocode.bsky.social 🥳 where we show Siglecs as molecular precision tools, able to recognise sialylated glycans with surgical precision in their natural environment, not bad for a lectin! 😎

doi.org/10.1038/s420...

Three part #glycotime🧵⤵️ if you want to know more about a very unique, rare but previous type of glycosylation: C-mannosylation

One of my favourites 💚 (because it is a very special mannose 😁)

When glycan recognition is linked to immune response, you need fine tuning! 😎

Here ⬇️ we show how human Siglecs act as molecular precision tools, recognising the glycan and also the biological environment (or context) these glycans are found in. A 1/5 #glycotime🧵 ⬇️

doi.org/10.1101/2025...

New fabulous #glycotime fresh off the bioRxiv press!⬇️ 🎉 In this brilliant team effort led by Klaudia Sobczak, Jesús Jimenez-Barbero, and June Ereño Orbea 🤩 with many contributions 🌍, we characterised the 3D structure + binding mechanism of sialosides by Siglec-10 🧵 1/3

doi.org/10.1101/2025...

Do you think 🪰 can only do stubby (and boring) oligoman-type N-glycans? Think *again* 🤯

This fabulous #glycotime work ⬇️ led by the N-glycan extraordinaire @iainwilsonwien.bsky.social, shows that different sf9 and high five cells produce VERY fancy glycans 1/3 🧵

www.mcponline.org/article/S153...

Picture this: your fav protein-protein interaction is *entirely* dependent on,
1) glycans 💥
2) the type of glycans 🤯💜
Check out this doi.org/10.1016/j.jb... 🔝 #glycotime fresh off the press in JBC led by Nicki Packer and Len Harrison 🇦🇺 + us 🇮🇪🇬🇧 + @ethangbaus.bsky.social 🇦🇺
🧵1/5

🧵 We published GlyCombo in 2024 and it's still one of my favourite things we've built. Here's what it actually does and why it matters for glycomics labs. (1/4) #glycotime