NMR Structure of Fusion Peptide of the Helicoverpa Armigera Single Nucleocapsid Nucleopolyhedrovirus F Protein at pH 7.0

Abstract

Abstract:

Fusion between viral and cellular membranes is an essential process for enveloped viruses to enter into cells. This process is usually mediated by fusion proteins on the surfaces of viral membranes. When pH changes from 7.0 to 5.0, the fusion proteins transform and expose their fusion peptide to anchor the cellular membrane and induce the subsequent fusion process. Ha133 (HaF) is the fusion protein of baculoviruse Helicoverpa armigera Single Nucleocapsid Nucleopolyhedrovirus (HearNPV). Its fusion peptide is composed of 20 residues, and located at the N-terminus of the F₁subunit. In this study, NMR methods were used to determine the solution structure of the fusion peptide in a membrane-mimicking environment at pH 7.0. It was found that the structure of the fusion peptide is composed of a 3₁₀ -helix from V⁷ to S⁹, a turn at V¹⁰, a regular α-helix from D¹¹ to G¹⁶ and two flexible coils at the N- and C-terminus. Comparing this structure to the available structure of this fusion peptide at pH 5.0, it is noted that, with decreasing pH, the conformation of the fusion peptide alters to be more stable and to have a more complete amphiphilic surface. These results should allow us to further investigate the mechanism of membrane fusion.

Key words: NMR, structure, fusion peptide, baculoviruse

CLC Number:

O482.53

ZENG Dan-yun1,2, DU Tian-peng1,2, JIANG Ling1*, LIU Mai-li1. NMR Structure of Fusion Peptide of the Helicoverpa Armigera Single Nucleocapsid Nucleopolyhedrovirus F Protein at pH 7.0[J]. Chinese Journal of Magnetic Resonance.

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NMR Structure of Fusion Peptide of the Helicoverpa Armigera Single Nucleocapsid Nucleopolyhedrovirus F Protein at pH 7.0

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