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Journal: Virology Journal
Article Title: Characterization and functional analysis of N-linked glycosylation on the Hendra virus attachment glycoprotein
doi: 10.1186/s12985-026-03095-4
Figure Lengend Snippet: Predominant N-glycosylation and limited O-glycosylation in HeV-G. (A) NetNGlyc 1.0 prediction of N-glycosylation sites in HeV-G sequence, which applies artificial neural networks to evaluate the sequence context of Asn-Xaa-Ser/Thr sequons. ( B ) SDS-PAGE analysis of HeV-G under non-reducing conditions following treatment with the indicated glycosidases. ( C ) Periodic acid–Schiff (PAS) staining of treated HeV-G samples following deglycosylation. Lane 1: Marker; Lane 2: 5 µg Untreated HeV-G; Lane 3: 5 µg HeV-G + PNGase F; Lane 4: 5 µg HeV-G + Rapid PNGase F; Lane 5: 5 µg HeV-G + O-Glycosidase (OG) and Neuraminidase (NA); Lane 6: 5 µg HeV-G + Deglycosylation Mix Ⅱ; Lane 7: Horseradish Peroxidase (HRP, positive control); Lane 8: Soybean Trypsin Inhibitor (STI, negative control). The distinct bands correspond to the HeV-G monomer, dimer and tetramer, while the band below 40 kDa represents PNGase F
Article Snippet: For rapid N-glycan removal, a separate aliquot of glycoprotein (10 μg) was incubated with
Techniques: Glycoproteomics, Sequencing, SDS Page, Staining, Marker, Positive Control, Negative Control