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J Virol, May 1998, p. 3887-3892, Vol. 72, No. 5
Department of Virology, SMI/Karolinska
Institute, 105 21 Stockholm, Sweden
Received 6 October 1997/Accepted 5 February 1998
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 formation and protein
folding.
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Carbohydrates Facilitate Correct Disulfide Bond
Formation and Folding of Rotavirus VP7
*
Corresponding author. Mailing address: Department of
Virology, SMI/Karolinska Institute, 105 21 Stockholm, Sweden. Phone: 46-8-735 12 28. Fax: 46-8-470 56 13. E-mail:
Lensve{at}mbox.ki.se.
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