1887

Abstract

Post-mortem host degradation by infection of nucleopolyhedrovirus (BmNPV) requires the synergistic activation of two virus-encoded genes, () and (). 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 -linked glycans of V-CATH. Sequence analysis shows that BmNPV V-CATH includes three consensus -linked glycosylation sites (asparagine 38, 65 and 158). To clarify the role of -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 -linked glycans from BmNPV V-CATH resulted in production of the insoluble forms of V-CATH and V-CHIA. These results demonstrate that -linked glycans located in the pro-region of BmNPV V-CATH are essential for the proper folding of V-CATH and V-CHIA.

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2009-01-01
2019-11-18
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