The F-like protein Ac23 enhances the infectivity of the budded virus of gp64-null Autographa california multinucleocapsid nucleopolyhedrovirus pseudotyped with baculovirus envelope fusion protein F

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

Research output: Contribution to journalArticleAcademicpeer-review

34 Citations (Scopus)

Abstract

The GP64 and F proteins were previously identified as the sole functional envelope fusion proteins in Baculoviridae. F-like proteins, present only in group I nucleopolyhedroviruses (NPVs), are remnant, nonfunctional F proteins. In this report, we describe the effect of the presence or absence of the F-like protein Ac23 in a gp64-null Autographa californica multinucleocapsid NPV pseudotyped with the F protein from Spodoptera exigua multicapsid NPV (SeF). We found that the presence of Ac23 elevates the infectivity of the pseudotyped virus. This is in contrast to the results of Lung et al. (J. Virol. 76:5729-5736, 2002), who found no such effect. The possible reasons for the differing results are discussed
Original languageEnglish
Pages (from-to)9800-9804
JournalJournal of Virology
Volume82
Issue number19
DOIs
Publication statusPublished - 2008

Keywords

  • multicapsid nucleopolyhedrovirus
  • multiple nucleopolyhedrovirus
  • gp64
  • identification
  • glycoprotein
  • homolog
  • virions
  • gene

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