PMID: 9557673Apr 29, 1998Paper

Carbohydrates facilitate correct disulfide bond formation and folding of rotavirus VP7

Journal of Virology
Ali Mirazimi, L Svensson

Abstract

It is well established that glycosylation is essential for assembly of enveloped viruses, but no information is yet available as to the function of carbohydrates on the nonenveloped but glycosylated rotavirus. We show that tunicamycin and, more pronouncedly, a combination of tunicamycin and brefeldin A treatment caused misfolding of the luminal VP7 protein, leading to interdisulfide bond aggregation. While formation of VP7 aggregates could be prevented under reducing conditions, they reoccurred in less than 30 min after a shift to an oxidizing milieu. Furthermore, while glycosylated VP7 interacted during maturation with protein disulfide isomerase, nonglycosylated VP7 did not, suggesting that glycosylation is a prerequisite for protein disulfide isomerase interaction. While native NSP4, which does not possess S-S bonds, was not dependent on N-linked glycosylation or on protein disulfide isomerase assistance for maturation, nonglycosylated NSP4 was surprisingly found to interact with protein disulfide isomerase, further suggesting that protein disulfide isomerase can act both as an enzyme and as a chaperone. In conclusion, our data suggest that the major function of carbohydrates on VP7 is to facilitate correct disulfide bond fo...Continue Reading

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Citations

Aug 10, 2000·Journal of Virology·A Mirazimi, L Svensson
Dec 2, 1999·The Journal of General Virology·A MirazimiL Svensson
Apr 4, 2008·Journal of Virology·Liliana Maruri-AvidalCarlos F Arias
May 14, 2016·World Journal of Virology·Carlos A Guerrero, Orlando Acosta
Mar 26, 2003·The Journal of General Virology·Ali MirazimiLennart Svensson
Dec 18, 2020·The Journal of General Virology·Lina ReslanHassan Zaraket

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