Robert de Vries

Super happy to receive an M-2 weave grant from the NWO (Dutch Research Council). Together with Sayed Abd El-Whab we will study the molecular features of H5Nx HA and NA proteins. #glycotime www.nwo.nl/en/news/gran...

Chemoenzymatically Synthesized O-Acetylated GD3 Gangliosides to Examine Viral Receptor Specificities in a Cellular Context Gangliosides are a class of sialic acid-containing glycosphingolipids involved in a wide range of biological processes. The terminal sialic acid of gangliosides can be O -acetylated at C7 and/or C9 hy...

#glycotime alert! Zhiyong synthesized O-acetylated GD3 gangliosides, which were used to examine viral receptor specificities in a cellular context by @LiangRuonan great work by @zeshi_li and @TheBoonsGroup @uu-cbdd.bsky.social www.biorxiv.org/content/10.1...

Big shout out to @LiangRuonan and many thanks to @TheBoonsGroup , @UnioneLuca @UU_Glycoscience @uuuips.bsky.social

The latter is vital, as many H3N2 viruses bind solely to these complex structures, and many zoonotic avian HAs, engineered to bind human-type receptors, do so as well.

Significant observations indicate that the conserved 195Y, which changes to F, rescues binding properties in specific backgrounds. And symmetric N-glycans with tri-LacNAc arms are not displayed on human tracheal epithelial cells.

She followed those results up with, amongst others, a tissue binding experiment on human tracheal tissues. As glycan binding is one thing, but binding tissues is another.

Here, we aimed to identify the molecular determinant of tri- vs. di-LacNAc binding in strains that have circulated over the last 10 years. Ruonan created a mutant library and utilized complex N-glycans in an ELISA assay to assess specificity and avidity.

Asymmetrical Biantennary Glycans Prepared by a Stop-and-Go Strategy Reveal Receptor Binding Evolution of Human Influenza A Viruses Glycan binding properties of respiratory viruses have been difficult to probe due to a lack of biologically relevant glycans for binding studies. Here, a stop-and-go chemoenzymatic methodology is pres...

We previously demonstrated that human H3N2 viruses can have very strict specificities to complex N-glycans and that this can very depending on antigenic pressure pubs.acs.org/doi/full/10.... www.nature.com/articles/s41...

Epistasis in the receptor-binding domain of contemporary H3N2 viruses that reverted to bind sialylated di-LacNAc repeats Liang et al. shows how contemporary H3N2 viruses reverted to bind sialylated di-LacNAc at the molecular level. Using complex symmetrical and asymmetric N-glycans, major epistatic interactions were rev...

Very happy that our paper on the receptor binding properties of contemporary H3N2 viruses is now published @CellReports # glycotime www.cell.com/cell-reports...

And now published! #glycotime "Sialic Acid-Containing Glycolipids Extend the Receptor Repertoire of Enterovirus-D68" fantastic collaboration with @lisabauervirus.bsky.social @debbyvanriel.bsky.social @TheBoonsGroup enjoy 👍https://pubs.acs.org/doi/10.1021/acsinfecdis.5c00063

Sialic Acid-Containing Glycolipids Extend the Receptor Repertoire of Enterovirus-D68 Enterovirus D68 (EV-D68) emerged as a pathogen of increasing health concern globally, particularly due to its association with outbreaks of severe respiratory diseases and acute flaccid myelitis (AFM) in children. Knowledge regarding the tissue tropism and pathogenesis of EV-D68 within the respiratory tract and central nervous system remains limited, primarily due to an incomplete understanding of the host factors that facilitate the entry of EV-D68 into host cells. Several cellular receptors involved in EV-D68 infections have been identified, including ICAM-5, sialylated glycoproteins, and heparan sulfate (HS). Here, we investigate the receptor requirement of a panel of EV-D68 strains covering all clades, focusing on HS and sialosides utilizing glycan arrays. We found that all EV-D68 strains binding to HS harbor a cell culture adaptive substitution in the structural protein VP1 at position 271, which changes the amino acid into a positively charged one. Glycan array analyses revealed that EV-D68 strains prefer α2,6-linked sialic acids presented on N-glycans, α2,8-linked sialic acids on gangliosides, or both. Inhibition of glycolipid biosynthesis or multivalent glycolipid mimics confirmed that ganglioside structures serve as entry receptors for certain EV-D68 strains. Lastly, we examined whether EV-D68 strains that bind to HS or glycolipids require different uncoating mechanisms. Bafilomycin A1 minimally affected the cell entry of HS-binding EV-D68 strains B2/039 and B2/947, and the ganglioside preferring B1/2013 and other viruses were strongly inhibited. Together, we identified that EV-D68 strains can use disialoglycolipids as novel receptors and that different EV-D68 strains show a promiscuous sialic acid binding repertoire.

We are happy to share the first publication of our consortium:
pubs.acs.org/doi/10.1021/...

Chemoenzymatic Synthesis and Biological Recognition of a Sulfonate Isostere of 6-Sulfo-sialyl Lewisx Sulfation of N-acetylglucosamine (GlcNAc) moieties of glycans is a common modification that has been implicated in many biological and disease processes. Glycans having sulfate replaced by a stable an...

New paper of Yunfei! Here, he synthesized sulfonates in different sialylated epitopes... although not better ligands for most lectins tested, they were tolerated and even preferred by siglec-4. #glycotime pubs.acs.org/doi/10.1021/...

What a great thread and very interesting preprint 👍

Happy Eurovision! Basel is awesome, getting ready for the final!🏳️‍🌈🇫🇮

Bijvoet symposia 👍 #glycotime @uu-cbdd.bsky.social

Characterization of the glycoproteins of novel fish influenza B-like viruses Novel influenza-like virus sequences previously identified in fish and amphibians were found to cluster as a sister clade of influenza B viruses, but have thus far remained uncharacterized. We demonst...

Happy to be able to contribute to this very cool preprint
Characterization of the glycoproteins of novel fish influenza B-like viruses #glycotime #lovevirology @uu-cbdd.bsky.social www.biorxiv.org/content/10.1...

Many thanks to @uu-cbdd.bsky.social @uuuips.bsky.social

Of course, we don't know if precisely these O-glycans enable these viruses' unique zoonotic capabilities, as many other virological and ecological factors are likely involved. However, we do like to hypothesize that these binding properties contribute to these capabilities.

Another observation we made is that the cattle-derived recombinant virus had nearly identical receptor binding properties compared to one of the first 2.3.4.4 viruses isolated over 10 years ago. Receptor specificity is relatively conserved for 2.3.4.4 viruses.

Our colleagues at @scripps.edu determined the structural features of these specificities. And i hope you can appreciate how the fucose lies in the receptor binding site. Fun observation is that we saw the peptide interacting with a very well-known epitope in the HA stalk

Using these mucin-like O-glycans as a glycan array screen, we observed that these 2.3.4.4b were unique in their promiscuous receptor binding properties. These properties resulted in binding to human respiratory tract tissue while not binding human-type receptors.

Many years ago, a carbohydrate chemist, Julia, started to synthesize mucin-like O-glycans, as they were greatly understudied. This was also when 2.3.4.4b H5Nx viruses were taking the stage.

The receptor binding properties of H5Nx influenza A viruses have evolved to promiscuously bind to avian-type mucin-like O-glycans Highly pathogenic H5Nx influenza A viruses are causing unprecedented, season-independent outbreaks across avian and mammalian species, including dairy cattle, a novel reservoir. The sialoside-binding ...

Excited to have this story out on bioRxv! #glycotime #lovevirology #H5N1 The receptor binding properties of H5Nx influenza A viruses have evolved to promiscuously bind to avian-type mucin-like O-glycans.

www.biorxiv.org/content/10.1...

Now published in PNAS, this is a fantastic paper on how HA moves within a virion upon receptor binding. By the way, do check the #badglycans in Figure 6 😐
www.pnas.org/doi/10.1073/...

Vacature: Postdoc Virology The department of Viroscience at the Erasmus MC and the department of Chemical Biology & Drug discovery at Utrecht University have joined forces to identify functional glycan receptors for influenza A...

We a looking for a Postdoc!
Interested in virology, stem-cell derived models, glycans?
Apply before 29th of October!

@thijskuiken.bsky.social @lisabauervirus.bsky.social @marionkoopmans.bsky.social @rpdevrieslab.bsky.social

www.werkenbijerasmusmc.nl/en/vacancy/1...

Receptor-binding specificity of a bovine influenza A virus - Nature Nature - Receptor-binding specificity of a bovine influenza A virus

Now out in Nature! Bovine H5 maintains binding to avian-type receptors. #glycotyme #H5N1 @uu-cbdd.bsky.social

www.nature.com/articles/s41...

The Q226L mutation can convert a highly pathogenic H5 2.3.4.4e virus to bind human-type receptors H5Nx viruses continue to wreak havoc in avian and mammalian species worldwide. The virus distinguishes itself by the ability to replicate to high titers and transmit efficiently in a wide variety of h...

Many thanks to
@TheBoonsGroup @UU_Glycoscience @UUBeta, and if you do not have access, please check the preprint www.biorxiv.org/content/10.1...

Maria and our colleagues at @scrippsresearch have done fantastic work on this. A 2.3.4.4e H5 only needed a single Q226L mutant to bind canonical human-type receptors! A representative H5 from the current cow outbreak did not shift receptor binding with the Q226L only.

Happy to have this story now published in @PNAS
The Q226L mutation can convert a highly pathogenic H5 2.3.4.4e virus to bind human-type receptors | PNAS #glycotime www.pnas.org/doi/10.1073/...

#Viruseslikeitsweet is online! We are a consortium of the department of Viroscience @erasmusmc.bsky.social and the department of Chemical Biology & Drug discovery @utrechtuniversity.bsky.social
Follow our progress here or via our Linked-In account: NWO-XL Consortium Viruses like it Sweet