Bruce-Staskal PJ, Woods RM, Borisov OV, Massare MJ. Hemagglutinin from multiple divergent influenza A and B viruses bind to a distinct branched, sialylated poly-LacNAc glycan by surface plasmon resonance. Vaccine. 2020;S0264-410X(20)31078-1
Influenza viruses initiate infection via specific interactions of hemagglutinin (HA) with host cell surface sialic acid-containing glycans. Antigenic drift has resulted in HA amino acid sequence changes that affect binding properties for sialic acids. Further, viral propagation in eggs and cell culture for vaccine production can yield variants with mutations that affect the conformation and affinity of HA for sialic acids. Therefore, influenza vaccine researchers and manufacturers need robust analytical methods to assess directly the ability of vaccine candidates to bind to their specific sialic acid ligand. We developed a surface plasmon resonance method that uses an extended, biantennary glycan terminating with α-2,6 linked sialic acids to bind influenza HA and assess this interaction. Recombinant HA (rHA) from both influenza A and B viruses isolated from 1999 to 2017 strongly and specifically bind this sialic acid ligand, suggesting the binding ability of divergent HA for this ligand is resistant to antigenic drift. Importantly, the method can differentiate between wild type and mutant rHA for which binding to this sialylated glycan and red blood cells in hemagglutination assays is compromised. We believe this method can be a powerful tool to screen influenza A and B vaccine candidates and final vaccine preparations for their functional ability to bind sialic acids, which allows manufacturers to identify preparations in which mutations that affect sialic acid binding have arisen during propagation. Evaluation of vaccine rHA antigen integrity by confirmation of the receptor binding site functionality is a prudent cautionary step to assure the antigenic quality of seasonal influenza vaccines.
See Also:
Latest articles in those days:
- The evolution, complexity, and diversity of swine influenza viruses in China: A hidden public health threat 14 hours ago
- MHC class II proteins mediate sialic acid independent entry of human and avian H2N2 influenza A viruses 14 hours ago
- Histopathologic Features and Viral Antigen Distribution of H5N1 Highly Pathogenic Avian Influenza Virus Clade 2.3.4.4b from the 2022–2023 Outbreak in Iowa Wild Birds 14 hours ago
- Detection and characterization of H5N1 HPAIV in environmental samples from a dairy farm 18 hours ago
- Genomic Characterization of Highly Pathogenic Avian Influenza A H5N1 Virus Newly Emerged in Dairy Cattle 18 hours ago
[Go Top] [Close Window]