Joost Snijder
@joostsnijder.bsky.social
a sort of scientist. viruses and antibodies. structure and biophysics. mass spec and cryoEM | Voorzitter SP Culemborg
Reposted by Joost Snijder
Structural determinants of broadly neutralizing human antibodies binding to morphological dengue virus variants. www.biorxiv.org/content/10.64898/2026.02.07.704521v1 #cryoem
February 9, 2026 at 8:10 AM
Structural determinants of broadly neutralizing human antibodies binding to morphological dengue virus variants. www.biorxiv.org/content/10.64898/2026.02.07.704521v1 #cryoem
Reposted by Joost Snijder
Look at this π #CryoEM
Structural basis for CTCF-mediated chromatin organization by @lucas.farnunglab.com @voslab.org
www.biorxiv.org/content/10.6...
Structural basis for CTCF-mediated chromatin organization by @lucas.farnunglab.com @voslab.org
www.biorxiv.org/content/10.6...
February 9, 2026 at 8:32 AM
Look at this π #CryoEM
Structural basis for CTCF-mediated chromatin organization by @lucas.farnunglab.com @voslab.org
www.biorxiv.org/content/10.6...
Structural basis for CTCF-mediated chromatin organization by @lucas.farnunglab.com @voslab.org
www.biorxiv.org/content/10.6...
Reposted by Joost Snijder
We studied how the glycan shield of alphaherpesvirus fusion protein gB mediates host co-receptor interactions. Great work by Sabrina, check it out!
www.biorxiv.org/content/10.6...
www.biorxiv.org/content/10.6...
February 4, 2026 at 10:01 AM
We studied how the glycan shield of alphaherpesvirus fusion protein gB mediates host co-receptor interactions. Great work by Sabrina, check it out!
www.biorxiv.org/content/10.6...
www.biorxiv.org/content/10.6...
Reposted by Joost Snijder
I am very pleased to announce that we have finalised the program for the @eupaproteomics.bsky.social Brixen Proteomics Summer School 2026 now also a @febsj.bsky.social advance lecture course.
www.brixenproteomics.org
www.brixenproteomics.org
In 2026 the established Brixen Proteomics Summer School
FEBS Advanced Lecture Course
www.brixenproteomics.org
February 6, 2026 at 10:04 AM
I am very pleased to announce that we have finalised the program for the @eupaproteomics.bsky.social Brixen Proteomics Summer School 2026 now also a @febsj.bsky.social advance lecture course.
www.brixenproteomics.org
www.brixenproteomics.org
Reposted by Joost Snijder
Congratulations to former LMB postdoc @mfpronker.bsky.social, who is launching his own independent research group at Sanquin Research where he'll use protein engineering and structural biology techniques to study important blood protein complexes.
Best of luck to you Matti!
#LMBAlumni
Best of luck to you Matti!
#LMBAlumni
February 5, 2026 at 1:04 PM
Congratulations to former LMB postdoc @mfpronker.bsky.social, who is launching his own independent research group at Sanquin Research where he'll use protein engineering and structural biology techniques to study important blood protein complexes.
Best of luck to you Matti!
#LMBAlumni
Best of luck to you Matti!
#LMBAlumni
Reposted by Joost Snijder
Nieuwe neussspray met antigriep antilichamen beschermt tegen verschillende subtypen van griep. www.nrc.nl/nieuws/2026/...
Met een neusspray is elke griep te voorkomen
Infectieziekte: Een breed werkende antistof in een neusspray beschermt tegen veel verschillende griepvirussen. Dat kan een belangrijk wapen worden bij een nieuwe pandemie.
www.nrc.nl
February 5, 2026 at 7:44 AM
Nieuwe neussspray met antigriep antilichamen beschermt tegen verschillende subtypen van griep. www.nrc.nl/nieuws/2026/...
Reposted by Joost Snijder
π How do spirochete bacteria swim through thick fluids like champions?
We solved T. denticola flagella structure - asymmetric proteins expand one side, compress the other for perfect corkscrew motion!
@debnathghosal.bsky.social
π doi.org/10.64898/202...
#StructuralBiology #CryoEM #Microbiology
We solved T. denticola flagella structure - asymmetric proteins expand one side, compress the other for perfect corkscrew motion!
@debnathghosal.bsky.social
π doi.org/10.64898/202...
#StructuralBiology #CryoEM #Microbiology
February 5, 2026 at 6:37 AM
π How do spirochete bacteria swim through thick fluids like champions?
We solved T. denticola flagella structure - asymmetric proteins expand one side, compress the other for perfect corkscrew motion!
@debnathghosal.bsky.social
π doi.org/10.64898/202...
#StructuralBiology #CryoEM #Microbiology
We solved T. denticola flagella structure - asymmetric proteins expand one side, compress the other for perfect corkscrew motion!
@debnathghosal.bsky.social
π doi.org/10.64898/202...
#StructuralBiology #CryoEM #Microbiology
Reposted by Joost Snijder
Influenza A virus infection perturbs host cell glycosylation https://www.biorxiv.org/content/10.64898/2026.02.02.703422v1
February 4, 2026 at 2:45 AM
Influenza A virus infection perturbs host cell glycosylation https://www.biorxiv.org/content/10.64898/2026.02.02.703422v1
Reposted by Joost Snijder
The glycan shield of alphaherpesvirus glycoprotein B modulates host co-receptor binding https://www.biorxiv.org/content/10.64898/2026.02.03.703472v1
February 4, 2026 at 2:45 AM
The glycan shield of alphaherpesvirus glycoprotein B modulates host co-receptor binding https://www.biorxiv.org/content/10.64898/2026.02.03.703472v1
We hope these findings give a better handle on how neurotropism of alphaherpesviruses is finetuned by co-receptor interactions. Thanks to Sabrina, Francine and Bert!
February 4, 2026 at 10:01 AM
We hope these findings give a better handle on how neurotropism of alphaherpesviruses is finetuned by co-receptor interactions. Thanks to Sabrina, Francine and Bert!
The interaction of NMHC-IIA is also specific to HSV1 and HSV2, albeit in a glycan-independent manner.
February 4, 2026 at 10:01 AM
The interaction of NMHC-IIA is also specific to HSV1 and HSV2, albeit in a glycan-independent manner.
By contrast, PILRa binds specifically to HSV1 and HSV2, but not VZV. This is in agreement with the glycoproteomics experiments, which found no candidate binding sites in VZV.
February 4, 2026 at 10:01 AM
By contrast, PILRa binds specifically to HSV1 and HSV2, but not VZV. This is in agreement with the glycoproteomics experiments, which found no candidate binding sites in VZV.
With SPR we measured the relative binding of the co-receptors to gB. We found that MAG binds indiscriminately to gB from all three tested alphaherpesviruses, in a glycan-dependent manner, mediated especially by O-glycans.
February 4, 2026 at 10:01 AM
With SPR we measured the relative binding of the co-receptors to gB. We found that MAG binds indiscriminately to gB from all three tested alphaherpesviruses, in a glycan-dependent manner, mediated especially by O-glycans.
Our cryoEM reconstruction of postfusion gB put these finding into context of the folded structure. In both pre- and postfusion states, the candidate binding sites for MAG and PILRa remain exposed and available for binding.
February 4, 2026 at 10:01 AM
Our cryoEM reconstruction of postfusion gB put these finding into context of the folded structure. In both pre- and postfusion states, the candidate binding sites for MAG and PILRa remain exposed and available for binding.
On a side note, we find multiple O-linked sites within N-linked glycosylation sequons. Seeing this again and again and I wonder how the types of modifications talk.
www.biorxiv.org/content/10.1...
www.nature.com/articles/s42...
pubs.acs.org/doi/full/10....
www.biorxiv.org/content/10.1...
www.nature.com/articles/s42...
pubs.acs.org/doi/full/10....
www.biorxiv.org
February 4, 2026 at 10:01 AM
On a side note, we find multiple O-linked sites within N-linked glycosylation sequons. Seeing this again and again and I wonder how the types of modifications talk.
www.biorxiv.org/content/10.1...
www.nature.com/articles/s42...
pubs.acs.org/doi/full/10....
www.biorxiv.org/content/10.1...
www.nature.com/articles/s42...
pubs.acs.org/doi/full/10....
Previous structural work showed that PILRa binds to a2,6 linked sialic acids and makes additional contacts with a proline residues at the +1 position. We found multiple of such sites in gB from HSV1 and 2, but none in VZV.
www.pnas.org/doi/abs/10.1...
www.pnas.org/doi/abs/10.1...
Structural basis for simultaneous recognition of an O-glycan and its attached peptide of mucin family by immune receptor PILRΞ± | PNAS
Paired Ig-like type 2 receptor α (PILRα) recognizes a wide range of O-glycosylated
mucin and related proteins to regulate broad immune responses. H...
www.pnas.org
February 4, 2026 at 10:01 AM
Previous structural work showed that PILRa binds to a2,6 linked sialic acids and makes additional contacts with a proline residues at the +1 position. We found multiple of such sites in gB from HSV1 and 2, but none in VZV.
www.pnas.org/doi/abs/10.1...
www.pnas.org/doi/abs/10.1...
We found a multitude of O-linked glycosylation sites on gB, especially in the flexible N-terminus and a flexible loop in domain II.
February 4, 2026 at 10:01 AM
We found a multitude of O-linked glycosylation sites on gB, especially in the flexible N-terminus and a flexible loop in domain II.
There are 6 or 7 predicted N-linked glycosylation sites, which all exhibit a mixture of complex and high-mannose glycans, and often unmodified asparagines as well. Notably, most sites were only sparsely sialylated.
February 4, 2026 at 10:01 AM
There are 6 or 7 predicted N-linked glycosylation sites, which all exhibit a mixture of complex and high-mannose glycans, and often unmodified asparagines as well. Notably, most sites were only sparsely sialylated.
To get a better picture of candidate binding sites we dove into the N- and O-linked glycosylation patterns of gB from HSV1, HSV2 and VZV with glycoproteomics experiments.
February 4, 2026 at 10:01 AM
To get a better picture of candidate binding sites we dove into the N- and O-linked glycosylation patterns of gB from HSV1, HSV2 and VZV with glycoproteomics experiments.
MAG and PILRο‘ are known to bind to sialic acids and previous studies already pointed to glycan-mediated interactions with gB.
www.nature.com/articles/nco...
www.pnas.org/doi/abs/10.1...
www.nature.com/articles/nco...
www.pnas.org/doi/abs/10.1...
Structural basis of myelin-associated glycoprotein adhesion and signalling - Nature Communications
Myelin-associated glycoprotein (MAG) maintains myelin-axon spacing. Here, the authors report the crystal structures of the MAG full ectodomain in complex with oligosaccharide, and use additional assay...
www.nature.com
February 4, 2026 at 10:01 AM
MAG and PILRο‘ are known to bind to sialic acids and previous studies already pointed to glycan-mediated interactions with gB.
www.nature.com/articles/nco...
www.pnas.org/doi/abs/10.1...
www.nature.com/articles/nco...
www.pnas.org/doi/abs/10.1...
Receptor interactions of gH/gL and gD trigger fusion activity of gB to facilitate entry into cells. In addition, gB has its own interactions with co-receptors MAG (Siglec 4), PILRa, and NMHC-IIA. These interactions finetune infectivity and tropism for different cell types and tissues.
February 4, 2026 at 10:01 AM
Receptor interactions of gH/gL and gD trigger fusion activity of gB to facilitate entry into cells. In addition, gB has its own interactions with co-receptors MAG (Siglec 4), PILRa, and NMHC-IIA. These interactions finetune infectivity and tropism for different cell types and tissues.
We studied how the glycan shield of alphaherpesvirus fusion protein gB mediates host co-receptor interactions. Great work by Sabrina, check it out!
www.biorxiv.org/content/10.6...
www.biorxiv.org/content/10.6...
February 4, 2026 at 10:01 AM
We studied how the glycan shield of alphaherpesvirus fusion protein gB mediates host co-receptor interactions. Great work by Sabrina, check it out!
www.biorxiv.org/content/10.6...
www.biorxiv.org/content/10.6...
Reposted by Joost Snijder
A broadly protective antibody targeting gammaherpesvirus gB pubmed.ncbi.nlm.nih.gov/41629701/ #cryoem
February 3, 2026 at 2:45 PM
A broadly protective antibody targeting gammaherpesvirus gB pubmed.ncbi.nlm.nih.gov/41629701/ #cryoem
Reposted by Joost Snijder
Viral Infections Drive Functional Remodeling of Ribosome-Associated Proteins https://www.biorxiv.org/content/10.64898/2026.01.29.701737v1
January 30, 2026 at 3:18 AM
Viral Infections Drive Functional Remodeling of Ribosome-Associated Proteins https://www.biorxiv.org/content/10.64898/2026.01.29.701737v1