Six-helix bundle assembly and characterization of heptad repeat regions from the F protein of Newcastle disease virus.

Published

Journal Article

Paramyxoviruses may adopt a similar fusion mechanism to other enveloped viruses, in which an anti-parallel six-helix bundle structure is formed post-fusion in the heptad repeat (HR) regions of the envelope fusion protein. In order to understand the fusion mechanism and identify fusion inhibitors of Newcastle disease virus (NDV), a member of the Paramyxoviridae family, we have developed an E. coli system that separately expresses the F protein HR1 and HR2 regions as GST fusion proteins. The purified cleaved HR1 and HR2 have subsequently been assembled into a stable six-helix bundle heterotrimer complex. Furthermore, both the GST fusion protein and the cleaved HR2 show virus-cell fusion inhibition activity (IC(50) of 1.07-2.93 microM). The solubility of the GST-HR2 fusion protein is much higher than that of the corresponding peptide. Hence this provides a plausible method for large-scale production of HR peptides as virus fusion inhibitors.

Full Text

Duke Authors

Cited Authors

  • Yu, M; Wang, E; Liu, Y; Cao, D; Jin, N; Zhang, CW-H; Bartlam, M; Rao, Z; Tien, P; Gao, GF

Published Date

  • March 2002

Published In

Volume / Issue

  • 83 / Pt 3

Start / End Page

  • 623 - 629

PubMed ID

  • 11842257

Pubmed Central ID

  • 11842257

Electronic International Standard Serial Number (EISSN)

  • 1465-2099

International Standard Serial Number (ISSN)

  • 0022-1317

Digital Object Identifier (DOI)

  • 10.1099/0022-1317-83-3-623

Language

  • eng