News
26Nov2024
Avian influenza viruses primarily use α2-3-linked sialic acids as their preferred receptors, whereas human influenza viruses typically prefer α2-6-linked sialic acids.
GlycoDisplay's glycoengineered HEK293 cells, which express either α2-3-linked or α2-6-linked sialic acids, were used to study how mutations in influenza hemagglutinin influence its binding preference for α2-6-linked versus α2-3-linked receptors.
Link to the article:
https://www.biorxiv.org/content/10.1101/2024.05.23.595634v2
https://www.pnas.org/doi/full/10.1073/pnas.2026102118
16Oct2023
New article "Direct observation of glycans bonded to proteins and lipids at the single-molecule level" is published.
Mucin reporters produced by GlycoDisplay platform was used for the first direct single-molecule imaging using low-temperatuer scanning tunneling microscopy.
Below you can see the image of single MUC1 molecule mucin reporter (200 aminoacid with 25 trisaccharides):
Link to the article:
Direct observation of glycans bonded to proteins and lipids at the single-molecule level
24Feb2023
New article "A universal GlycoDesign for lysosomal replacement enzymes to improve circulation time and biodistribution" is published.
Most therapeutic biologics are glycoproteins and the structures of the glycans attached to these glycoproteins are important for their circulation and uptake by cells. Lysosomal storage diseases (LSDs) represent a group of rare genetic disorders caused by severe deficiency in lysosomal enzymes, and some of LSDs are treated by supplying recombinant replacement enzymes. Production of lysosomal replacement enzymes in mammalian cells inherently equip these with glycans tagged with Mannose-6-Phosphate (M6P) modifications for cellular uptake and transport to the lysosome. We previously developed a genetic engineering design for mammalian cells that enables production of the lysosomal enzyme a-galactosidase without the M6P tag on glycans, and surprisingly found that this enzyme circulated longer in a mouse Fabry disease model. In the present study, we confirmed this finding in repeated infusion of the a-galactosidase without M6P and further showed that the genetic engineering design for lysosomal enzymes, coined Long-Acting-GlycoDesign (LAGD), is widely applicable to several other replacement enzymes and results in removal of the M6P tag and installation of the common glycan structures with sialic acids. Finally, we demonstrated in preliminary studies that this design of glycans on lysosomal enzymes widely prolongs the half-life of infused enzymes in mice.
Link to the article:
http://glycodisplay.com/cms/?module=pages&function=element&id=493&element=content