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 Liang, C. Articles by Chen, X. Search for Related Content PubMed PubMed Citation Articles by Liang, C. Articles by Chen, X. Agricola Articles by Liang, C. Articles by Chen, X.

The GP64 protein of Autographa californica multiple nucleopolyhedrovirus rescues Helicoverpa armigera nucleopolyhedrovirus transduction in mammalian cells

¹ State Key Laboratory of Virology, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, People's Republic of China
² Graduate School of the Chinese Academy of Sciences, Beijing 100039, People's Republic of China

Correspondence
Xinwen Chen
chenxw{at}pentium.whiov.ac.cn

Autographa californica multiple nucleopolyhedrovirus (AcMNPV) belonging to the group I nucleopolyhedroviruses (NPVs) and expressing the envelope-fusion glycoprotein GP64 transduces a variety of mammalian cells to express foreign genes under the control of mammalian promoters. In contrast, the group II Helicoverpa armigera single NPV (HaSNPV) encoding a different envelope protein, the F protein, shows no detectable infectivity towards mammalian cells. This limitation was overcome by expressing AcMNPV GP64 in HaSNPV. Although the transduction ratios were lower overall, the range of mammalian cell types transduced by HaSNPV was consistent with those transduced by AcMNPV. These findings indicate that the F protein functions only in insect cells, whereas the GP64 protein works in both insect and mammalian cells.

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 protein of Helicoverpa armigera single nucleopolyhedrovirus can be substituted functionally with its homologue from Spodoptera exigua multiple nucleopolyhedrovirus J. Gen. Virol., March 1, 2008; 89(3): 791 - 798. [Abstract] [Full Text] [PDF]

				M. Westenberg and J. M. Vlak GP64 of group I nucleopolyhedroviruses cannot readily rescue infectivity of group II f-null nucleopolyhedroviruses J. Gen. Virol., February 1, 2008; 89(2): 424 - 431. [Abstract] [Full Text] [PDF]

				M. Westenberg, P. Uijtdewilligen, and J. M. Vlak Baculovirus envelope fusion proteins F and GP64 exploit distinct receptors to gain entry into cultured insect cells J. Gen. Virol., December 1, 2007; 88(12): 3302 - 3306. [Abstract] [Full Text] [PDF]