NMR Analyses of Fusion Peptide of the Lymantria Dispar Multiple Nucleopolyhedrovirus F Protein

Abstract

Abstract:

LD130 is the fusion protein of baculoviruse Lymantria dispar multiple nucleopolyhedrovirus (LdMNPV). The N terminal conserved region of subunit F₁ in LD130 is the fusion peptide, which actively induces membrane fusion processes. NMR methods were used to identify the solution structure of the fusion peptide under membrane simulated enviornment at low pH. The fusion peptide appeared to be an amphiphilic structure composed of a flexible coil in the N-terminus, and a regular α-helix from L3 to V16. The structure of the LD130 fusion peptide allows us to further investigate the structure-functional relationship of the fusion peptide.

Key words: NMR, structure, 2D NMR, fusion peptide of baculoviruse

CLC Number:

O482.53

XIONG Jing-Wen, ZENG Dan-Yun, JIANG Ling, LIU Mai-Li. NMR Analyses of Fusion Peptide of the Lymantria Dispar Multiple Nucleopolyhedrovirus F Protein[J]. Chinese Journal of Magnetic Resonance, 2012, 29(1): 60-67.

References

[1] Klasse P J, Bron R, Marsh M. Mechanisms of enveloped virus entry into animal cells[J]. Adv Drug Deliv Rev, 1998, 34(1): 65-91.

[2] Weissenhorn W, Hinz A, Gaudin Y. Virus membrane fusion[J]. FEBS Lett, 2007, 581(11): 2 150-2 155.

[3] Harrison S C. Viral membrane fusion[J]. Nat Struct Mol Biol, 2008, 15(7): 690-698.

[4] Colman P M, Lawrence M C. The structural biology of type I viral membrane fusion[J]. Nat Rev Mol Cell Biol, 2003, 4(4): 309-319.

[5] Stiasny K, Heinz F X. Flavivirus membrane fusion[J]. J Gen Virol, 2006, 87(Pt 10): 2 755-2 766.

[6] Roche S, Rey F A, Gaudin Y, et al. Structure of the prefusion form of the vesicular stomatitis virus glycoprotein G[J]. Science, 2007, 315(5 813): 843-848.

[7] Tamm L K, Han X. Viral fusion peptides: a tool set to disrupt and connect biological membranes[J]. Biosci Rep, 2000, 20(6): 501-518.

[8] Pearson M N, Russell R L, Rohrmann G F. Functional analysis of a conserved region of the baculovirus envelope fusion protein, LD130
[J]. Virology, 2002, 304(1): 81-88.

[9] WF I J, Westenberg M, Goldbach R W, et al. A novel baculovirus envelope fusion protein with a proprotein convertase cleavage site[J]. Virology, 2000, 275(1): 30-41.

[10] Long G, Westenberg M, Wang H, et al. Function, oligomerization and N-linked glycosylation of the Helicoverpa armigera single nucleopolyhedrovirus envelope fusion protein[J]. J Gen Virol, 2006, 87(Pt 4): 839-846.

[11] Westenberg M, Wang H, WF I J, et al. Furin is involved in baculovirus envelope fusion protein activation[J]. J Virol, 2002, 76(1): 178-184.
[12] Han X, Bushweller J H, Cafiso D S, et al. Membrane structure and fusion-triggering conformational change of the fusion domain from influenza hemagglutinin[J]. Nat Struct Biol, 2001, 8(8): 715-720.

[13] Chang D K, Cheng S F, Chien W J. The amino-terminal fusion domain peptide of human immunodeficiency virus type 1 gp41 inserts into the sodium dodecyl sulfate micelle primarily as a helix with a conserved glycine at the micelle-water interface[J]. J Virol, 1997, 71(9): 6 593-6 602.

[14] Jaroniec C P, Kaufman J D, Stahl S J, et al. Structure and dynamics of micelle-associated human immunodeficiency virus gp41 fusion domain[J]. Biochemistry, 2005, 44(49): 16 167-16 180.

[15] Li Y, Tamm L K. Structure and plasticity of the human immunodeficiency virus gp41 fusion domain in lipid micelles and bilayers[J]. Biophys J, 2007, 93(3): 876-885.

[16] Tan Y, Jiang L, Wang M, et al. Mutagenesis and nuclear magnetic resonance analyses of the fusion peptide of Helicoverpa armigera single nucleocapsid nucleopolyhedrovirus F protein[J]. J Virol, 2008, 82(16): 8 138-8 148.

[17] Liu M L, Mao X A, Ye C H, et al. Improved WATERGATE pulse sequences for solvent suppression in NMR spectroscopy[J]. J Magn Reson, 1998, 132(1): 125-129.

[18] Delaglio F, Grzesiek S, Vuister G W, et al. Nmrpipe - a multidimensional spectral processing system based on unix pipes[J]. J Biomol NMR, 1995, 6(3): 277-293.

[19] Cornilescu G, Delaglio F, Bax A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology[J]. J Biomol NMR, 1999, 13(3): 289-302.

[20] Guntert P, Mumenthaler C, Wuthrich K. Torsion angle dynamics for NMR structure calculation with the new program DYANA[J]. J Mol Biol, 1997, 273(1): 283-298.

[21] Lovell S C, Davis I W, Arendall W B, et al. Structure validation by Calpha geometry: phi, psi and cbeta deviation[J]. Proteins, 2003, 50(3): 437-450.

[22] Biggin P C, Sansom M S P. Interactions of alpha-helices with lipid bilayers: a review of simulation studies[J]. Biophys Chem, 1999, 76(3): 161-183.

[23] Wimley W C, White S H. Experimentally determined hydrophobicity scale for proteins at membrane interfaces[J]. Nat Struct Biol, 1996, 3(10): 842-848.

[24] Dike A, Cowsik S M. Solution structure of amphibian tachykinin Uperolein bound to DPC micelles[J]. J Struct Biol, 2006, 156(3): 442-452.