RRC ID |
3467
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著者 |
Katsuma S, Daimon T, Horie S, Kobayashi M, Shimada T.
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タイトル |
N-linked glycans of Bombyx mori nucleopolyhedrovirus fibroblast growth factor are crucial for its secretion.
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ジャーナル |
Biochem Biophys Res Commun
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Abstract |
Bombyx mori nucleopolyhedrovirus (BmNPV) fibroblast growth factor (BmFGF) is a glycosylated protein that is efficiently secreted into the medium. Here, we constructed mutant NPVs expressing His-tagged wild-type (wt) or mutant BmFGFs and showed that the two residues, asparagine 44 and 171, are the glycosylation sites of BmFGF. Also, removal of N-linked glycans from BmFGF resulted in almost complete inhibition of the secretion into the medium, suggesting that N-linked glycans of BmFGF are required for its secretion. These residues are not conserved in closely related Autographa californica NPV (AcMNPV)-encoded vFGF (AcFGF). Western blot analysis suggested that AcFGF is not glycosylated and is poorly secreted. A mutant AcFGF possessing two N-linked glycosylation sites was secreted into the medium more abundantly than that which occurred for wt AcFGF. This is the first direct evidence showing the role of N-linked glycans in the secretion process of a baculovirus protein.
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巻・号 |
350(4)
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ページ |
1069-75
|
公開日 |
2006-12-1
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DOI |
10.1016/j.bbrc.2006.10.001
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PII |
S0006-291X(06)02219-4
|
PMID |
17046716
|
MeSH |
Amino Acid Sequence
Animals
Bombyx / virology*
Fibroblast Growth Factors / chemistry*
Fibroblast Growth Factors / metabolism*
Molecular Sequence Data
Nucleopolyhedroviruses / metabolism*
Polysaccharides / chemistry*
Polysaccharides / metabolism*
|
IF |
2.985
|
引用数 |
15
|
WOS 分野
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BIOPHYSICS
BIOCHEMISTRY & MOLECULAR BIOLOGY
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リソース情報 |
カイコ |
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