InnoScan 1100-AL microarray scanner: new publication
Glycan microarray Unveiled H3N2 tropism shifts
Research demonstrates recent H3N2 virus exhibit stringent binding specificity for α2-6-linked sialic acids on bi-antennary N-glycans extended with three or more poly-LacNAc repeats. This binding profile was quantitatively determined using a glycan microarray, with fluorescence signal acquisition performed by InnoScan 1100AL microarray scanner and analysis performed using MAPIX software. MASS based glycomic analysis of human airway epithelium confirmed that such extended N-glycans are present at significantly higher abundance on tracheal epithelial cells compared to nasal epithelial cells. These findings clarify the primary glycan receptors for current H3N2 viruses and have critical implications for understanding infection initiation and for improving vaccine virus isolation methods.
Keywords:
- Glycan Microarray
- Influenza Virus Tropism
- Receptor Specificity
- InnoScan 1100AL
- H3N2
Original publication: H3N2 influenza virus tropism shifts to glycan receptors on tracheal ciliated cells
The display of sialic acid has consequences on the influenza virus to be specific for either avian-type or human-type receptors. Discover our study in partnership with Dr. Robert de Vries from Utrecht Institute for Parmaceutical Sciences. This study was conducted on large ferret lung tissue sections imaged with our InnoQuant fluorescent slide scanner.