Document Detail


Kinetics of the low pH-induced conformational changes and fusogenic activity of influenza hemagglutinin.
MedLine Citation:
PMID:  7696474     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The decrease of the intrinsic tryptophan fluorescence intensity of purified influenza (X31 strain) hemagglutinin (HA) was used to monitor the low pH-induced conformational change of this protein. The kinetics of the fluorescence decrease depended strongly on the pH. At pH optimal for fusion, the change in tryptophan fluorescence was fast and could be fitted to a monoexponential function. We measured a rate constant of 5.78 s-1 (t1/2 = 120 ms) at pH 4.9 using rapid stopped-flow mixing. Under suboptimal conditions (higher pH), the rate constant was decreased by an order of magnitude. In addition, a slow component appeared and the fluorescence decrease followed a sum of two exponentials. The kinetics of conformational changes were compared with those of the fusion of influenza virus with red blood cell membranes as assessed by the R18-dequenching assay. At optimal pH the HA conformational change was not rate-limiting for the fusion process. However, at sub-optimal pH, the slow transition to the fusogenic conformational of HA resulted in slower kinetics and decreased extent of fusion.
Authors:
M Krumbiegel; A Herrmann; R Blumenthal
Related Documents :
2365074 - Fusion of negatively charged phospholipid vesicles by alpha-latrotoxin.
19601904 - Membrane fusion and fission: enveloped viruses.
18779374 - The mouth of a dense-core vesicle opens and closes in a concerted action regulated by c...
1441954 - Hyperthermia during occipito-cervical fusion with acrylic cement. epidural thermometry ...
7641064 - Sweat responses to pesticide-proof clothing influenced by textile materials.
22060584 - Changes in lactic acid levels during thawing of lamb chops.
Publication Detail:
Type:  In Vitro; Journal Article    
Journal Detail:
Title:  Biophysical journal     Volume:  67     ISSN:  0006-3495     ISO Abbreviation:  Biophys. J.     Publication Date:  1994 Dec 
Date Detail:
Created Date:  1995-05-03     Completed Date:  1995-05-03     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  0370626     Medline TA:  Biophys J     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  2355-60     Citation Subset:  IM    
Affiliation:
Section of Membrane Structure and Function, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Animals
Biophysical Phenomena
Biophysics
Erythrocyte Membrane / physiology
Hemagglutinin Glycoproteins, Influenza Virus
Hemagglutinins, Viral / chemistry*,  physiology*
Humans
Hydrogen-Ion Concentration
Kinetics
Membrane Fusion / physiology*
Orthomyxoviridae / chemistry,  physiology
Protein Conformation
Spectrometry, Fluorescence
Tryptophan / chemistry
Chemical
Reg. No./Substance:
0/Hemagglutinin Glycoproteins, Influenza Virus; 0/Hemagglutinins, Viral; 73-22-3/Tryptophan
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Head group and chain behavior in biological membranes: a molecular dynamics computer simulation.
Next Document:  Characterization of PEG-mediated electrofusion of human erythrocytes.