Multiple receptors involved in human rhinovirus attachment to live cells.
Minor group human rhinoviruses (HRVs) attach to members of the low-density lipoprotein receptor family and are internalized via receptor-mediated endocytosis. The attachment of HRV2 to the cell surface, the first step in infection, was characterized at the single-molecule level by atomic force spectroscopy. Sequential binding of multiple receptors was evident from recordings of characteristic quantized force spectra, which suggests that multiple receptors bound to the virus in a timely manner. Unbinding forces required to detach the virus from the cell membrane increased within a time frame of several hundred milliseconds. The number of receptors involved in virus binding was determined, and estimates for on-rate, off-rate, and equilibrium binding constant of the interaction between HRV2 and plasma membrane-anchored receptors were obtained.
Rankl
Christian
C
Institute for Biophysics, Christian Doppler Laboratory for Nanoscopic Methods in Biophysics, University of Linz, Altenbergerstrasse 69, A-4040 Linz, Austria.
Kienberger
Ferry
F
Wildling
Linda
L
Wruss
Jürgen
J
Gruber
Hermann J
HJ
Blaas
Dieter
D
Hinterdorfer
Peter
P
D000818:Animals; D001696:Biomechanical Phenomena; D002460:Cell Line; D002470:Cell Survival; D006801:Humans; D007700:Kinetics; D051379:Mice; D018625:Microscopy, Atomic Force; D011973:Receptors, LDL / Q000378:metabolism; D011991:Receptors, Virus / Q000378:metabolism*; D012229:Rhinovirus / Q000502:physiology*; D013057:Spectrum Analysis; D013997:Time Factors; D014771:Virion / Q000502:physiology / Q000648:ultrastructure; D053585:Virus Attachment
D011973:Receptors, LDL; D011991:Receptors, Virus