Function, oligomerization and N-linked glycosylation of the Helicoverpa armigera single nucleopolyhedrovirus envelope fusion protein

G. Long, M. Westenberg, H. Wang, J.M. Vlak, Z. Hu

Research output: Contribution to journalArticleAcademicpeer-review

42 Citations (Scopus)

Abstract

In the family Baculoviridae, two distinct envelope fusion proteins are identified in budded virions (BVs). GP64 is the major envelope fusion protein of group I nucleopolyhedrovirus (NPV) BVs. An unrelated type of envelope fusion protein, named F, is encoded by group II NPVs. The genome of Helicoverpa armigera (Hear) NPV, a group II NPV of the single nucleocapsid or S type, also encodes an F-like protein: open reading frame 133 (Ha133). It was demonstrated by N-terminal sequencing of the major 59 kDa protein present in HearNPV BV that this protein is one of the two F subunits: F1 (transmembrane subunit of 59 kDa) and F2 (surface subunit of 20 kDa), both the result of cleavage by a proprotein convertase and disulfide-linked. The HearNPV F protein proved to be a functional analogue of GP64, as the infectivity of an AcMNPV gp64-deletion mutant was rescued by the introduction of the HearNPV F gene. It was also demonstrated by chemical cross-linking that HearNPV F is present in BVs as an oligomer whereby, unlike GP64, disulfide bonds are not involved. Deglycosylation assays indicated that both F1 and F2 possess N-linked glycans. However, when F was made in Hz2E5 cells, these glycans did not have an ¿-1-3 core fucose modification that usually occurs in insect cells. As ¿-1-3 core fucose is a major inducer of an allergic response in humans, the present observation makes the HearNPV-Hz2E5 system an attractive alternative for the production of recombinant glycoproteins for therapeutic use in humans
Original languageEnglish
Pages (from-to)839-846
JournalJournal of General Virology
Volume87
Issue number4
DOIs
Publication statusPublished - 2006

Keywords

  • californica multicapsid nucleopolyhedrovirus
  • nuclear polyhedrosis-virus
  • viral membrane-fusion
  • baculovirus gp64
  • cell-lines
  • cross-linking
  • insect
  • genome
  • glycoproteins
  • activation

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