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Human rhinovirus 2 particles attached to model membranes containing the recombinant MBP-VLDLR1-8 receptor fragment in a tightly packed, long-range order quasi-crystalline arrangement.
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We used dynamic force microscopy to study the attachment of human rhinovirus 2 (HRV2) particles to model membranes. A supported lipid bilayer containing Ni2+-nitrilotriacetate (NTA)-lipids as functional groups in the outer leaflet at high surface density was assembled on mica and showed a flat extended structure of 3 nm in height. The recombinant very-low density lipoprotein receptor fragment MBP-VLDLR1-8, consisting of the ligand binding domain (all eight complement type A repeats) fused at the N-terminus to maltose binding protein (MBP) and containing a hexahistidine (His6)-tag at its C-terminus, was attached to the membranes via the His6-Ni2+NTA bond and revealed monolayer density. The protein-lipid layer was then used as a model to investigate virus binding to its receptor in a planar membrane. The viral particles attached in a tightly packed, long range order quasi-crystalline arrangement. This assembly is thus ideally suited for studies of viral dynamics and recognition under physiological conditions.
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This model membrane assembly allows for the study of viral dynamics and recognition under physiological conditions.
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Kienberger et al. (2001) studied Human rhinovirus 2 (HRV2) attachment. Model cell membranes with recombinant MBP-VLDLR1-8 receptor fragment was evaluated on Viral particle attachment arrangement. Human rhinovirus 2 particles attached to model membranes containing the recombinant MBP-VLDLR1-8 receptor fragment in a tightly packed, long-range order quasi-crystalline arrangement.
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