Fusion of enveloped viruses is promoted
by specific proteins on the surface of
the
virus. These proteins are able
to destabilize bilayer membranes and promote
the formation of fusion intermediates. One
aspect of the study of this process
is to use "viral fusion peptides",
i.e., segments of viral fusion proteins
which have been shown t o be important in
membrane fusion. We wish to identify how these
fusion peptides insert into bilayers and
how they alter the physical properties of
the bilayer. We are also interested
in the role of viral receptors in the
overall fusion process. In general we wish
to separate effects of components on the
binding of the virus to the target
membrane from the subsequent step of membrane
fusion.Finally we are interested in modulation
of the rate of membrane fusion
by alteration of the physical properties of
the target membrane. Coumpounds which are effective
in inhibiting the formation of structures
with negative curvature frequently are inhibitors
of viral fusion. These agents may
function as non-specific anti-viral drugs.
J.N.Campbell,
R.M.Epand and P.S.Russo. 2004. Structural Changes and Aggregation of Human
Influenza Virus.
Biomacromolecules,
5(5):1728-35.
J.A.
Corcoran, R. Syvitski, D.Top, R.M. Epand, R.F. Epand, D. Jakeman and R.
Duncan. 2004.
Myristoylation,
a Protruding Loop, and Structural Plasticity are Essential Features of a
Nonenveloped Virus Fusion Peptide Motif. J. Biol. Chem, 279(49):51386-94.
M.
Shmulevitz, R.F. Epand, R.M. Epand and R. Duncan. 2004.Structural and
functional properties of an unusual internal fusion peptide in a nonenveloped
virus membrane fusion protein. J. Virol. 78(6):2808-18.
A.
Bertocco, F. Formaggio, C. Toniolo, Q.B. Broxterman, R.F. Epand and R.M. Epand.
2003. Design and function of a conformationally restricted analog of the
Influenza virus fusion peptide. J. Peptide Res. 62(1):19-20.
Y.Yao,
K. Ghosh, R.F. Epand, R.M. Epand and H.P. Ghosh. 2003. Membrane fusion
activity of vesicular stomatitis virus glycoprotein G is induced by low pH but
not by heat or denaturant. Virology 310 (2): 319-332.
R.F.
Epand and R.M. Epand. 2003. Unfolding of the neutral pH form of Influenza
Hemagglutinin demonstrates it is not in a metastable state. Biochemistry,
42(17):5052-5057.
S.G.
Peisajovich, L. Blank, R.F. Epand, R.M. Epand and Y. Shai, 2003.On the
interaction between gp41 and membranes: the immunodominant loop stabilizes gp41
helical hairpin conformation. J. Mol. Biol. 326(5):1489-1501.
R.M.
Epand. 2003. Fusion peptides and the mechanism of viral fusion. Biochim.
Biophys. Acta, Biomembranes,1614(1):116-121.
R.
Blumenthal, M.J. Clague, S.R. Durell and R.M. Epand. 2003. Membrane fusion.
Chem Rev., 103(1):53-70.
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