論文 - 詳細
| RRC ID | 11254 |
|---|---|
| 著者 | Katsuma S, Nakanishi T, Daimon T, Shimada T. |
| タイトル | N-linked glycans located in the pro-region of Bombyx mori nucleopolyhedrovirus V-CATH are essential for the proper folding of V-CATH and V-CHIA. |
| ジャーナル | J Gen Virol |
| Abstract |
Post-mortem host degradation by infection of Bombyx mori nucleopolyhedrovirus (BmNPV) requires the synergistic activation of two virus-encoded genes, cathepsin (v-cath) and chitinase (v-chiA). Previous studies have suggested that V-CHIA is essential for the proper folding of the nascent V-CATH polypeptide in the endoplasmic reticulum, and that the putative V-CHIA-V-CATH interaction might be mediated by N-linked glycans of V-CATH. Sequence analysis shows that BmNPV V-CATH includes three consensus N-linked glycosylation sites (asparagine 38, 65 and 158). To clarify the role of N-linked glycans of V-CATH in its biological activity, we generated three recombinant BmNPVs expressing mutant V-CATHs, and found that the two residues, asparagine 38 and 65, which are localized in the pro-region of V-CATH, are the glycosylation sites of BmNPV V-CATH. Western blot analysis also showed that removal of N-linked glycans from BmNPV V-CATH resulted in production of the insoluble forms of V-CATH and V-CHIA. These results demonstrate that N-linked glycans located in the pro-region of BmNPV V-CATH are essential for the proper folding of V-CATH and V-CHIA. |
| 巻・号 | 90(Pt 1) |
| ページ | 170-6 |
| 公開日 | 2009-1-1 |
| DOI | 10.1099/vir.0.005835-0 |
| PII | 90/1/170 |
| PMID | 19088286 |
| MeSH | Amino Acid Substitution / genetics Animals Bombyx / virology* Cathepsins / genetics Cathepsins / metabolism* Chitinases / metabolism* DNA Mutational Analysis Glycosylation Mutation, Missense Nucleopolyhedroviruses / physiology* Polysaccharides Protein Folding* Viral Proteins / metabolism* |
| IF | 3.376 |
| 引用数 | 14 |
| WOS 分野 | BIOTECHNOLOGY & APPLIED MICROBIOLOGY VIROLOGY |
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| 各媒体での言及数の合計 | 0 |
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