| RRC ID |
3467
|
| Author |
Katsuma S, Daimon T, Horie S, Kobayashi M, Shimada T.
|
| Title |
N-linked glycans of Bombyx mori nucleopolyhedrovirus fibroblast growth factor are crucial for its secretion.
|
| Journal |
Biochem Biophys Res Commun
|
| 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.
|
| Volume |
350(4)
|
| Pages |
1069-75
|
| Published |
2006-12-1
|
| DOI |
10.1016/j.bbrc.2006.10.001
|
| 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
|
| Times Cited |
15
|
|
WOS Category
|
BIOPHYSICS
BIOCHEMISTRY & MOLECULAR BIOLOGY
|
| Resource |
| Silkworms |
|
