HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Wang, M. Articles by Wang, H. Search for Related Content PubMed PubMed Citation Articles by Wang, M. Articles by Wang, H. Agricola Articles by Wang, M. Articles by Wang, H.

The F protein of Helicoverpa armigera single nucleopolyhedrovirus can be substituted functionally with its homologue from Spodoptera exigua multiple nucleopolyhedrovirus

¹ State Key Laboratory of Virology and Joint Laboratory of Invertebrate Virology, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, PR China
² Graduate School of the Chinese Academy of Sciences, Beijing 100039, PR China
³ Laboratory of Virology, Wageningen University, 6709 PD Wageningen, The Netherlands

Correspondence
Hualin Wang
h.wang{at}wh.iov.cn

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.

This article has been cited by other articles:

				M. Wang, Y. Tan, F. Yin, F. Deng, J. M. Vlak, Z. Hu, and H. Wang The F-Like Protein Ac23 Enhances the Infectivity of the Budded Virus of gp64-Null Autographa californica Multinucleocapsid Nucleopolyhedrovirus Pseudotyped with Baculovirus Envelope Fusion Protein F J. Virol., October 1, 2008; 82(19): 9800 - 9804. [Abstract] [Full Text] [PDF]

				Y. Tan, L. Jiang, M. Wang, F. Yin, F. Deng, M. Liu, Z. Hu, and H. Wang Mutagenesis and Nuclear Magnetic Resonance Analyses of the Fusion Peptide of Helicoverpa armigera Single Nucleocapsid Nucleopolyhedrovirus F Protein J. Virol., August 15, 2008; 82(16): 8138 - 8148. [Abstract] [Full Text] [PDF]