Source:http://linkedlifedata.com/resource/pubmed/id/18272771
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 3
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pubmed:dateCreated |
2008-2-14
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pubmed:abstractText |
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, HaBacDeltaF, 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 HaBacDeltaF was pseudotyped with the homologous F protein (HaBacDeltaF-HaF, positive control) or with the heterologous F protein from Spodoptera exigua multinucleocapsid NPV (SeMNPV) (HaBacDeltaF-SeF), infectious BVs were produced with similar kinetics. In the late phase of infection, the BV titre of HaBacDeltaF-SeF virus was about ten times lower than that of HaBacDeltaF-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 F(1) and F(2) in the BVs of vHaBacDeltaF-HaF and vHaBacDeltaF-SeF, respectively, but the cleavage of SeF in vHaBacDeltaF-SeF-infected HzAM1 cells was incomplete, explaining the lower BV titre of vHaBacDeltaF-SeF. Polyclonal antisera against HaF(1) and SeF(1) specifically neutralized the infection of vHaBacDeltaF-HaF and vHaBacDeltaF-SeF, respectively. HaF(1) antiserum showed some cross-neutralization with vHaBacDeltaF-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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0022-1317
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
89
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
791-8
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pubmed:meshHeading |
pubmed-meshheading:18272771-Animals,
pubmed-meshheading:18272771-Cell Fusion,
pubmed-meshheading:18272771-Cells, Cultured,
pubmed-meshheading:18272771-Giant Cells,
pubmed-meshheading:18272771-Moths,
pubmed-meshheading:18272771-Nucleopolyhedrovirus,
pubmed-meshheading:18272771-Recombination, Genetic,
pubmed-meshheading:18272771-Species Specificity,
pubmed-meshheading:18272771-Spodoptera,
pubmed-meshheading:18272771-Transfection,
pubmed-meshheading:18272771-Viral Fusion Proteins
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pubmed:year |
2008
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pubmed:articleTitle |
The F protein of Helicoverpa armigera single nucleopolyhedrovirus can be substituted functionally with its homologue from Spodoptera exigua multiple nucleopolyhedrovirus.
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pubmed:affiliation |
State Key Laboratory of Virology , Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, People's Republic of China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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