Characterization of cell-surface determinants important for baculovirus infection

被引:133
作者
Tani, H
Nishijima, M
Ushijima, H
Miyamura, T
Matsuura, Y [1 ]
机构
[1] Natl Inst Infect Dis, Dept Virol 2, Tokyo 1628640, Japan
[2] Natl Inst Infect Dis, Dept Biochem & Cell Biol, Tokyo 1628640, Japan
[3] Univ Tokyo, Dept Dev Med Sci, Tokyo 1130033, Japan
[4] Osaka Univ, Res Ctr Emerging Infect Dis, Microbial Dis Res Inst, Suita, Osaka 5650871, Japan
关键词
baculovirus; gp64; infection; phospholipids; vector;
D O I
10.1006/viro.2000.0699
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Baculovirus gp64 envelope glycoprotein is a major component of the envelope of the budded virus and is involved in virus entry into the host cells by endocytosis. To investigate the cell-surface molecules important for infection of baculovirus into mammalian cells, we constructed a recombinant baculovirus, Ac64-CAluc, which has gp64 and luciferase genes under the polyhedrin and the CAG promoter, respectively. For controls, we constructed recombinant viruses possessing vesicular stomatitis virus (VSV) G protein, mouse hepatitis virus (MHV) S protein, or green fluorescent protein (GFP) gene under the polyhedrin promoter and the luciferase gene under the CAG promoter (AcVSVG-CAluc, AcMHVS-CAluc, and AcGFP-CAluc). Treatment of HepG2 cells with phospholipase C markedly reduced the reporter gene expression by Ac64-CAluc or AcVSVG-CAluc in a dose-dependent manner, whereas AcMHVS-CAluc was shown to be resistant to the treatment, inhibition with purified lipids and susceptibility to the mutant CHO hamster cell lines deficient in phospholipids synthesis suggest that the interaction of gp64 and phospholipids on the cell surface might play an important role in baculovirus infection into mammalian cells. (C) 2001 Academic Press.
引用
收藏
页码:343 / 353
页数:11
相关论文
共 54 条
[31]   IDENTIFICATION OF A MEMBRANE-FUSION DOMAIN AND AN OLIGOMERIZATION DOMAIN IN THE BACULOVIRUS GP64 ENVELOPE FUSION PROTEIN [J].
MONSMA, SA ;
BLISSARD, GW .
JOURNAL OF VIROLOGY, 1995, 69 (04) :2583-2595
[32]   THE BASIC SCIENCE OF GENE-THERAPY [J].
MULLIGAN, RC .
SCIENCE, 1993, 260 (5110) :926-932
[33]   MEMBRANE-FUSION OF SEMLIKI FOREST VIRUS REQUIRES SPHINGOLIPIDS IN THE TARGET MEMBRANE [J].
NIEVA, JL ;
BRON, R ;
CORVER, J ;
WILSCHUT, J .
EMBO JOURNAL, 1994, 13 (12) :2797-2804
[34]  
NIWA H, 1991, GENE, V108, P193, DOI 10.1016/0378-1119(91)90434-D
[35]   Requirement for GP64 to drive efficient budding of Autographa californica multicapsid nucleopolyhedrovirus [J].
Oomens, AGP ;
Blissard, GW .
VIROLOGY, 1999, 254 (02) :297-314
[36]   THE BACULOVIRUS GP64 ENVELOPE FUSION PROTEIN - SYNTHESIS, OLIGOMERIZATION, AND PROCESSING [J].
OOMENS, AGP ;
MONSMA, SA ;
BLISSARD, GW .
VIROLOGY, 1995, 209 (02) :592-603
[37]   A stable human-derived packaging cell line for production of high titer retrovirus/vesicular stomatitis virus G pseudotypes [J].
Ory, DS ;
Neugeboren, BA ;
Mulligan, RC .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1996, 93 (21) :11400-11406
[38]  
PAULSON JC, 1979, J BIOL CHEM, V254, P2120
[39]   An analysis of the role of the target membrane on the Gp64-induced fusion pore [J].
Plonsky, I ;
Cho, MS ;
Oomens, AGP ;
Blissard, G ;
Zimmerberg, J .
VIROLOGY, 1999, 253 (01) :65-76
[40]   ANALYSIS OF MURINE CORONAVIRUS SURFACE GLYCOPROTEIN FUNCTIONS BY USING MONOCLONAL-ANTIBODIES [J].
ROUTLEDGE, E ;
STAUBER, R ;
PFLEIDERER, M ;
SIDDELL, SG .
JOURNAL OF VIROLOGY, 1991, 65 (01) :254-262