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Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding
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Myristoylation, a protruding loop, and structural plasticity are essential features of a nonenveloped virus fusion

Jennifer A Corcoran1, Raymond Syvitski, Deniz Top

  • 1Department of Microbiology and Immunology, Dalhousie University, Halifax, Nova Scotia B3H 1X5, Canada.

The Journal of Biological Chemistry
|September 28, 2004
PubMed

Insights

The p14 FAST protein

Area of Science:

  • Virology
  • Structural Biology
  • Membrane Biophysics

Background:

  • Fusion-associated small transmembrane (FAST) proteins are key viral membrane fusion mediators.
  • Reoviruses encode FAST proteins, essential for viral entry and cell-cell fusion.
  • The p14 FAST protein from reptilian reovirus features a myristoylated N-terminal ectodomain.

Purpose of the Study:

  • To elucidate the structural and functional properties of the p14 FAST protein ectodomain.
  • To investigate the role of myristoylation and specific sequence elements in p14-mediated membrane fusion.
  • To determine if the p14 ectodomain possesses fusion peptide characteristics.

Main Methods:

  • Mutagenic analysis of the p14 hydrophobic patch.
  • Circular dichroism (CD) spectroscopy of myristoylated and nonmyristoylated peptides.
  • Nuclear Magnetic Resonance (NMR) spectroscopy and simulated annealing for structural determination.
  • Liposome fusion assays to assess lipid mixing activity.

Main Results:

  • Sequence-specific elements within the N-proximal hydrophobic patch are crucial for fusion activity.
  • The p14 ectodomain is largely disordered in solution but gains structure in apolar environments.
  • NMR data revealed an extended loop and proline hinges in the nonmyristoylated ectodomain.
  • Myristoylated p14 ectodomain peptide, but not controls, induced significant lipid mixing in liposomes.
  • Structural plasticity and environmentally induced changes suggest fusion peptide-like behavior.

Conclusions:

  • The p14 ectodomain exhibits characteristics of a fusion peptide, including structural plasticity and environmentally induced conformational changes.
  • Myristoylation is essential for the membrane fusion activity of this p14 ectodomain fusion peptide.
  • This study identifies the first myristoylation-dependent fusion peptide motif within the FAST protein family.

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