The F protein of Helicoverpa armigera SNPV can be functionally substituted by an F homologue from Spodoptera exigua MNPV

M. Wang, Y. Tan, F. Yin, F. Deng, J.M. Vlak, Z.H. Hu, H. Wang

Research output: Contribution to journalArticleAcademicpeer-review

18 Citations (Scopus)


F proteins of group II nucleopolyhedroviruses (NPVs) are envelope fusion proteins essential for virus entry and egress. An F-null Helicoverpa armigera single nucleocapsid NPV (HearNPV) bacmid, HaBacF, was constructed. This bacmid could not produce infectious budded virus (BV) when transfected into HzAM1 cells, showing that F protein is essential for cell-to-cell transmission of BVs. When HaBacF was pseudotyped with the homologous F protein (HaBacF-HaF, positive control) or with the heterologous F protein from Spodoptera exigua multinucleocapsid NPV (SeMNPV) (HaBacF-SeF), infectious BVs were produced with similar kinetics. In the late phase of infection, the BV titre of HaBacF-SeF virus was about ten times lower than that of HaBacF-HaF virus. Both pseudotyped viruses were able to fuse HzAM1 cells in a similar fashion. The F proteins of both HearNPV and SeMNPV were completely cleaved into F1 and F2 in the BVs of vHaBacF-HaF and vHaBacF-SeF, respectively, but the cleavage of SeF in vHaBacF-SeF-infected HzAM1 cells was incomplete, explaining the lower BV titre of vHaBacF-SeF. Polyclonal antisera against HaF1 and SeF1 specifically neutralized the infection of vHaBacF-HaF and vHaBacF-SeF, respectively. HaF1 antiserum showed some cross-neutralization with vHaBacF-SeF. These results demonstrate that group II NPV F proteins can be functionally replaced with a homologue of other group II NPVs, suggesting that the interaction of F with other viral or host proteins is not absolutely species-specific.
Original languageEnglish
Pages (from-to)791-798
JournalJournal of General Virology
Issue number3
Publication statusPublished - 2008


  • envelope fusion protein
  • californica multicapsid nucleopolyhedrovirus
  • nuclear polyhedrosis-virus
  • baculovirus gp64
  • membrane-fusion
  • furin
  • cleavage
  • sequence
  • oligomerization
  • identification

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