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- W2126606502 abstract "ABSTRACT 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." @default.
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- W2126606502 date "1998-11-01" @default.
- W2126606502 modified "2023-10-03" @default.
- W2126606502 title "The Molecular Chaperone Calnexin Interacts with the NSP4 Enterotoxin of Rotavirus In Vivo and In Vitro" @default.
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- W2126606502 doi "https://doi.org/10.1128/jvi.72.11.8705-8709.1998" @default.
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