Representative Research Publications
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Human Norovirus and Jack bean protein
- Biomaterials / 2017 June
- Kwon, Joseph (corresponding author)
Study Summary
We explore the interactions between HuNoV and concanavalin A (Con A), which could facilitate the development of a sensitive detection tool for HuNoV. Biophysical studies including hydrogen/deuterium exchange (HDX) mass spectrometry and surface plasmon resonance (SPR) revealed that when the metal coordinated region of Con A, which spans Asp16 to His24, is converted to nine alanine residues (mCon AMCR), the affinity for HuNoV (GII.4) diminishes, demonstrating that this Ca2þ and Mn2þ coordinated region is responsible for the observed virus-protein interaction. The mutated carbohydrate binding region of Con A (mCon ACBR) does not affect binding affinity significantly, indicating that MCR of Con A is a major region of interaction to HuNoV (GII.4).
Expected Effects
Rapid methods for the detection and clinical treatment of human norovirus (HuNoV) are needed to control foodborne disease outbreaks, but reliable techniques that are fast and sensitive enough to detect small amounts of HuNoV in food and aquatic environments are not yet available. This method offers many advantages over currently available methods, including a short concentration time. HuNov (GI and GII) can be detected in just 15 min with 90% recovery through Con A-PAB application. In addition, this method can be used over a wide range of pH values (pH 3.0 e 10.0). Overall, this rapid and sensitive detection of HuNoV (GI and GII) will aid in the prevention of virus transmission pathways, and the method developed here may have applicability for other foodborne viral infections.
Figure 1. HDX-MS system and result spectrum
Figure 2. Hydrogen/deuterium exchange (HDX) profile of concanavalin A (Con A),
defining the interaction regions between Con A and HuNoV (GII.4).
Figure 3. Modified SPE chromatography column used for the concentration of HuNoV.