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Journal of Virology, November 1998, p. 8705-8709, Vol. 72, No. 11
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

The Molecular Chaperone Calnexin Interacts with the NSP4 Enterotoxin of Rotavirus In Vivo and In Vitro

Ali Mirazimi, Mikael Nilsson, and Lennart Svensson*

Department of Virology, SMI/Karolinska Institute, 105 21 Stockholm, Sweden

Received 1 May 1998/Accepted 24 July 1998

Calnexin is an endoplasmic reticulum (ER)-associated molecular chaperone proposed to promote folding and assembly of glycoproteins that traverse the secretory pathway in eukaryotic cells. In this study we examined if calnexin interacts with the ER-associated luminal (VP7) and transmembrane (NSP4) proteins of rotavirus. Only glycosylated NSP4 interacted with calnexin and did so in a time-dependent manner (half-life, 20 min). In vitro translation experiments programmed with gene 10 of rhesus rotavirus confirmed that calnexin recognizes only glycosylated NSP4. Castanospermine (a glucosidase I and II inhibitor) experiments established that calnexin associates only with partly deglucosylated (di- or monoglucosylated) NSP4. Furthermore, enzymatic removal of the remaining glucose residues on the N-linked glycan units was essential to disengage the NSP4-calnexin complex. Novel experiments with castanospermine revealed that glucose trimming and the calnexin-NSP4 interaction were not critical for the assembly of infectious virus.

* Corresponding author. Mailing address: Department of Virology, SMI/Karolinska Institute, 105 21 Stockholm, Sweden. Phone: 46-8-457 26 96. Fax: 46-8-430 16 35. E-mail: Lensve{at}mbox.ki.se.

Journal of Virology, November 1998, p. 8705-8709, Vol. 72, No. 11
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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