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. 2006;309:245–261. doi: 10.1007/3-540-30773-7_9

Rotavirus Assembly: An Alternative Model That Utilizes an Atypical Trafficking Pathway

S Chwetzoff 2, G Trugnan 2,✉
Editor: Polly Roy1
PMCID: PMC7122644  PMID: 16909902

Abstract

We review here recent advances in our knowledge on trafficking and assembly of rotavirus and rotaviral proteins in intestinal cells. Assembly of rotavirus has been extensively studied in nonpolarized kidney epithelial MA104 cells, where several data indicate that most if not all the steps of rotavirus assembly take place within the endoplasmic reticulum (ER) and that rotavirus is release upon cell lysis. We focus here on data obtained in intestinal cells that argue for another scheme of rotavirus assembly, where the final steps seem to take place outside the ER with an apically polarized release of rotavirus without significant cell lysis. One of the key observations made by different groups is that VP4 and other structural proteins interact substantially with specialized membrane microdomains enriched in cholesterol and sphingolipids termed rafts. In addition, recent data point to the fact that VP4 does not localize within the ER or the Golgi apparatus in infected intestinal cells. The mechanisms by which VP4, a cytosolic protein, may be targeted to the apical membrane in these cells and assembles with the other structural proteins are discussed. The identification of cellular proteins such as Hsp70, flotillin, rab5, PRA1 and cytoskeletal components that interact with VP4 may help to define an atypical polarized trafficking pathway to the apical membrane of intestinal cells that will be raft-dependent and by-pass the classical exocytic route.

Keywords: Lipid Raft, Human Intestinal Epithelial Cell, Peroxisomal Target Signal, Nonenveloped Virus, Rotaviral Protein

Contributor Information

Polly Roy, Email: polly.roy@lshtm.ac.uk

G. Trugnan, Email: trugnan@ccr.jussieu.fr

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