Nathanael B. Kegel
nathanaelbkegel.bsky.social
Nathanael B. Kegel
@nathanaelbkegel.bsky.social
Biomedical scientist @ Philipps-University Marburg. Interested in RNA modifications and immune sensing 🧬🦠
More information available under the post by @lizeshi.bsky.social:
bsky.app/profile/lize...
#glycotime We hope our b2b publications serve as a heads-up for the #glycoRNA community, and drive the field forward constructively. Links👇
Kim et al. rdcu.be/eP4GQ
@nathanaelbkegel.bsky.social Kegel et al. nature.com/articles/s12276-025-01575-1 (Stefan Bauer lab)
November 18, 2025 at 11:05 AM
Huge thanks to all the people involved, especially the @hoeferlab.bsky.social and @nursedayilmaz.bsky.social for their contributions to this project. What a journey it was! ☺️
November 18, 2025 at 11:05 AM
We initiated our studies shortly after the first Cell paper was published. Back then, we were among the first to work on glycoRNA in our field (immunology). Thus, at least in our field, there was not much controversy. I understand the situation was probably different among e.g. glycobiologists
April 2, 2025 at 9:21 AM
However, as we found glycoproteins in our glycoRNA samples, we stopped the functional analyses and rather focused on identifying which and also why proteins are co-purified, thinking this might help others with interest in glycoRNA‘s function
April 1, 2025 at 3:05 PM
Regarding the question why resources were dedicated, we are a lab that’s interested in nucleic acid sensing. We were asking if RNA glycosylation affects recognition by innate immune receptors.
April 1, 2025 at 3:05 PM
Future studies may leverage proteinase K digestion under denaturing conditions to separate glycoRNA from glycoproteins — paving the way for deeper structural and functional insights into glycoRNA. (9/9)
March 19, 2025 at 10:43 AM
We hypothesize that glycosylation and RNA-binding properties contribute to protein protection during glycoRNA isolation and promote co-purification by enhancing hydrophilicity and shielding cleavage
sites. (8/9)
March 19, 2025 at 10:43 AM
Remarkably, recombinant LAMP1 was extractable from the aqueous phase of TRIzol and bound to silica
columns in an RNA- and alcohol concentration-dependent manner, consistent with observations by Kim et al. (2024) (7/9)
March 19, 2025 at 10:43 AM
Nearly all of these proteins are known to be glycosylated and/or possess RNA-binding properties. One particularly intriguing hit was LAMP1, which we used as a model to explore glycoprotein co-purification. (6/9)
March 19, 2025 at 10:43 AM
In an inspiring collaboration with @hoeferlab.bsky.social and @nursedayilmaz.bsky.social, we identified ten proteins that consistently co-purify with small, but not large, RNA fractions extracted from human and murine cell lines using LC-MS. (5/9)
March 19, 2025 at 10:43 AM