help button home button Biophys. J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Zhou, Z.
Right arrow Articles by Epand, R. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Zhou, Z.
Right arrow Articles by Epand, R. M.

Biophys J, May 2000, p. 2418-2425, Vol. 78, No. 5

15N NMR Study of the Ionization Properties of the Influenza Virus Fusion Peptide in Zwitterionic Phospholipid Dispersions

Zhe Zhou,* Jed C. Macosko,dagger Donald W. Hughes,Dagger Brian G. Sayer,Dagger John Hawes,§ and Richard M. Epand*Dagger

 *Department of Biochemistry and  Dagger Department of Chemistry, McMaster University, Hamilton, Ontario L8N 3Z5, Canada;  dagger Department of Chemistry, University of California, Berkeley, California 94720 USA; and  §Biochemistry Biotechnology Facility, University of Indiana, Indianapolis, Indiana 46202 USA

Influenza virus hemagglutinin (HA)-mediated membrane fusion involves insertion into target membranes of a stretch of amino acids located at the N-terminus of the HA2 subunit of HA at low pH. The pKa of the alpha -amino group of 1Gly of the fusion peptide was measured using 15N NMR. The pKa of this group was found to be 8.69 in the presence of DOPC (1,2-dioleoyl-sn-glycero-3-phosphocholine). The high value of this pKa is indicative of stabilization of the protonated form of the amine group through noncovalent interactions. The shift reagent Pr3+ had large effects on the 15N resonance from the alpha -amino group of Gly1 of the fusion peptide in DOPC vesicles, indicating that the terminal amino group was exposed to the bulk solvent, even at low pH. Furthermore, electron paramagnetic resonance studies on the fusion peptide region of spin-labeled derivatives of a larger HA construct are consistent with the N-terminus of this peptide being at the depth of the phosphate headgroups. We conclude that at both neutral and acidic pH, the N-terminal of the fusion peptide is close to the aqueous phase and is protonated. Thus neither a change in the state of ionization nor a significant increase in membrane insertion of this group is associated with increased fusogenicity at low pH.

Biophys J, May 2000, p. 2418-2425, Vol. 78, No. 5
© 2000 by the Biophysical Society   0006-3495/00/05/2418/08  $2.00


This article has been cited by other articles:


Home page
 Biophys. JHome page
M. Sammalkorpi and T. Lazaridis
Modeling a Spin-Labeled Fusion Peptide in a Membrane: Implications for the Interpretation of EPR Experiments
Biophys. J., January 1, 2007; 92(1): 10 - 22.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
L. Vaccaro, K. J. Cross, J. Kleinjung, S. K. Straus, D. J. Thomas, S. A. Wharton, J. J. Skehel, and F. Fraternali
Plasticity of Influenza Haemagglutinin Fusion Peptides and Their Interaction with Lipid Bilayers
Biophys. J., January 1, 2005; 88(1): 25 - 36.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
Q. Huang, C.-L. Chen, and A. Herrmann
Bilayer Conformation of Fusion Peptide of Influenza Virus Hemagglutinin: A Molecular Dynamics Simulation Study
Biophys. J., July 1, 2004; 87(1): 14 - 22.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
S. Kamath and T. C. Wong
Membrane Structure of the Human Immunodeficiency Virus gp41 Fusion Domain by Molecular Dynamics Simulation
Biophys. J., July 1, 2002; 83(1): 135 - 143.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2000 by the Biophysical Society.