Effective binding of sugar chains to influenza virus on the surface by bovine serum albumin localization

The spread of influenza A virus variants requires continuous monitoring because of the high mutation rate. Given that the surveillance of such mutations is essential, the development and use of highly sensitive sensor systems is required. Host changes can manifest as changes in the binding between viral protein and host sugar chains. We employed sugar chains possessing different coordinations of terminal sialic acid and penultimate galactose groups as detection molecules. To enhance sensitivity, we developed an approach that controls the dispersion of molecules using bovine serum albumin (BSA) localization, and it was found that stable distribution was achieved. Several sugar chains were localized at fixed points on the BSA. The active sugar chain on BSA possessed suitable height as observed by atomic force microscopy. The clustering of sugar chains could also enhance the binding activity. Thus, we were able to enhance the sensitivity and availability of the detection of molecules.