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Quasi-crystalline Arrangement of Human Rhinovirus 2 on Model Cell Membranes by Ferry Kienberger; Rosita Moser; Hansgeorg Schindler; Dieter Blaas; Peter Hinterdorfer is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Quasi-crystalline Arrangement of Human Rhinovirus 2 on Model Cell Membranes about?

We used dynamic force microscopy to study the attachment of human rhinovirus 2 (HRV2) particles to model membranes. A supported lipid bilayer containing Ni 2+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-Ni 2+ 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.

Who reads Quasi-crystalline Arrangement of Human Rhinovirus 2 on Model Cell Membranes?

Author

Ferry Kienberger; Rosita Moser; Hansgeorg Schindler; Dieter Blaas; Peter Hinterdorfer

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Ltd.; Wiley (ISSN 1438-5163)

Published

2001

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Physical Sciences)