RRC ID 11254
Author Katsuma S, Nakanishi T, Daimon T, Shimada T.
Title 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.
Journal 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.
Volume 90(Pt 1)
Pages 170-6
Published 2009-1
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 Nucleopolyhedrovirus / physiology* Polysaccharides Protein Folding* Viral Proteins / metabolism*
IF 2.514
Times Cited 11
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