Influenza virus surveillance using surface plasmon resonance

Area of Science:

• Virology
• Biochemistry
• Analytical Chemistry

Background:

• Influenza virus hemagglutinin (HA) proteins exhibit specific binding preferences for sialoglycans (Sia glycans). Avian influenza viruses bind to α2-3 Sia glycans, while human-adapted strains prefer α2-6 Sia glycans.
• A shift in glycan specificity from α2-3 to α2-6 Sia glycans is a key factor in influenza virus adaptation and potential pandemic emergence.
• Monitoring these glycan binding adaptations is vital for influenza surveillance and pandemic risk assessment.

Purpose of the Study:

• To describe a reliable surface plasmon resonance (SPR) methodology for analyzing hemagglutinin (HA)-glycan interactions.
• To enhance the sensitivity and efficiency of HA-glycan binding assays for routine surveillance.

Main Methods:

• Utilized synthetic tetravalent glycans (α2-3 and α2-6 Sia glycans) to improve sensor chip capacity and HA affinity, thereby enhancing SPR signal and sensitivity.
• Employed the CAP-chip technology for sensor chip regeneration, enabling routine analysis of multiple samples.
• Integrated these advancements with a BiacoreT100 device for automated, continuous, and closed-environment analysis of numerous HA or virus samples.

Main Results:

• The developed SPR methodology provides reliable and sensitive analyses of HA-glycan interactions.
• The use of synthetic tetravalent glycans significantly improved SPR signal and sensitivity.
• The CAP-chip and automated system allowed for efficient, routine analysis of multiple samples.

Conclusions:

• The described SPR methodology offers a valuable tool for influenza surveillance.
• This approach enables effective monitoring of HA adaptations to different glycans among influenza viruses.
• The methodology contributes to understanding viral evolution and assessing pandemic potential.