A Secondary Sialic Acid Binding Site on Influenza Virus Neuraminidase: Fact or Fiction ?

摘要

We have previously reported an advanced NMR spectroscopy based approach to study carbohydrates, such as the N-acetylneuraminic acid (1) containing glycan a(2,3)-sialyllac-tose (2), in complex with influenza virus haemagglutinin-expressing virus-like particles (HA-VLP). One advantage of using VLPs is that the influenza virus surface glycoproteins can be studied independently of each other in a close-to native state, which is comparable to an intact virus. These particles are also non-infectious therefore do not require access to a high-level biocontainment laboratory. We and others have shown that saturation-transfer difference (STD) NMR spectroscopy is an ideal tool to study the interaction between virus particles and small ligands because the large NMR signal line width of virions enables saturation without affecting ligand signals.