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A cytoplasmic region of the NSP4 enterotoxin of rotavirus is involved in retention in the endoplasmic reticulum
Department of Virology, Swedish Institute for Infectious Disease Control/Karolinska Institute, Solna, Sweden.
Linköping University, Department of Molecular and Clinical Medicine, Medical Microbiology. Linköping University, Faculty of Health Sciences.
Linköping University, Department of Molecular and Clinical Medicine, Molecular Virology. Linköping University, Faculty of Health Sciences.
2003 (English)In: Journal of General Virology, ISSN 0022-1317, E-ISSN 1465-2099, Vol. 84, no 4, 875-883 p.Article in journal (Refereed) Published
Abstract [en]

The rotavirus genome encodes two glycoproteins, one structural (VP7) and one non-structural (NSP4), both of which mature and remain in the endoplasmic reticulum (ER). While three amino acids in the N terminus have been proposed to function as a retention signal for VP7, no information is yet available on how NSP4 remains associated with the ER. In this study, we have investigated the ER retention motif of NSP4 by producing various C-terminal truncations. Deleting the C terminus by 52 amino acids did not change the intracellular distribution of NSP4, but an additional deletion of 38 amino acids diminished the ER retention and resulted in the expression of NSP4 on the cell surface. Brefeldin A treatment prevented NSP4 from reaching the cell surface, suggesting that C-terminal truncated plasma membrane NSP4 is transported through the normal secretory pathway. On the basis of these results, we propose that the region between amino acids 85 and 123 in the cytoplasmic region of NSP4 are involved in ER retention.

Place, publisher, year, edition, pages
2003. Vol. 84, no 4, 875-883 p.
National Category
Medical and Health Sciences
URN: urn:nbn:se:liu:diva-26542DOI: 10.1099/vir.0.18786-0Local ID: 11104OAI: diva2:247091
Available from: 2009-10-08 Created: 2009-10-08 Last updated: 2012-08-22Bibliographically approved

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Magnusson, Karl-EricSvensson, Lennart
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