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PMID: 8369426 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Single event recording shows that docking onto receptor alters the kinetics of membrane fusion mediated by influenza hemagglutinin.

Biophysical journal ·Vol. 65 ·No. 1 ·1993-07-00 ·Pages 171-6

Niles WD, Cohen FS

Abstract

The initial steps of membrane fusion, receptor binding and membrane destabilization, are mediated by the envelope glycoprotein hemagglutinin of influenza virus. Interaction between these functions was determined from the time course of individual virion fusions to a planar membrane with and without receptor. With receptor, fusion was described by a Poisson process. In the absence of receptor, the time course was more complicated and could not be described with exponential rate constants. The conversion of a non-Markovian process into a simple Markov chain is direct evidence that receptor binding fundamentally alters the route of fusion.

MeSH Terms
Binding Sites Biophysical Phenomena Biophysics Hemagglutinin Glycoproteins, Influenza Virus Hemagglutinins, Viral/physiology Hydrogen-Ion Concentration In Vitro Techniques Kinetics Membrane Fusion/physiology Membrane Lipids/chemistry Membranes, Artificial Phospholipids/chemistry Receptors, Virus/physiology Thermodynamics
Chemicals
Hemagglutinin Glycoproteins, Influenza Virus Hemagglutinins, Viral Membrane Lipids Membranes, Artificial Phospholipids Receptors, Virus
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Niles W D
Department of Physiology, Rush Medical College, Chicago, Illinois 60612.
Cohen F S
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Article Info
Journal
Biophysical journal
Abbr.
Biophys J
ISSN
0006-3495
DOI
10.1016/S0006-3495(93)81049-X
Published
1993-07-00
Pages
171-6
Language
English
Region
United States
NLM ID
0370626
PMCID
PMC1225712
Subset
IM
Grants
NIGMS NIH HHS · GM27367 · United States
External Links
PubMed source DOI: 10.1016/S0006-3495(93)81049-X PMC Full Text View journal details
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