| ARTICLE ABSTRACT | |||||||
| DOI: 10.1099/vir.0.19279-0 | ||||||||
| Online 10 July 2003 | ||||||||
Corinne Potel,1 Karin Kaelin,1 Lydia Danglot,2 Antoine Triller,2 Christian Vannier2 and Flore Rozenberg1
1Laboratoire de Virologie, UPRES EA 3622, Faculté de Médecine Cochin, Université Paris V et Inserm U 567, Bâtiment Gustave Roussy, porte 636, 27 rue du Faubourg Saint Jacques, 75014 Paris, France
2Laboratoire de Biologie Cellulaire de la Synapse Normale et Pathologique, Institut National de la Santé et de la Recherche Médicale U497, Ecole Normale Supérieure, 75005 Paris, France
Herpes simplex virus type 1 (HSV-1) is a neuroinvasive human pathogen that spreads in the nervous system in functionally connected neurons. Determining how HSV-1 components are sorted in neurons is critical to elucidate the mechanisms of virus neuroinvasion. By using recombinant viruses expressing glycoprotein B (gB) tagged with green fluorescent protein (GFP), the subcellular localization of this envelope protein was visualized in infected hippocampal neurons in culture. Results obtained using a fully infectious recombinant virus containing GFP inserted into the ectodomain of gB support the view that capsids and gB are transported separately in neuron processes. Moreover, they show that during infection gB is sorted to the dendritic tree and the axons of polarized hippocampal neurons. However, GFP insertion into the cytoplasmic tail of gB impaired the maturation of the resulting fusion protein and caused its retention in the endoplasmic reticulum. The defective protein did not gain access to axons of infected neurons. These results suggest that the cytoplasmic tail of gB plays a role in maturation and transport and subsequently in axonal sorting in differentiated hippocampal neurons.
JGV Direct table of contents
© 2003 SGM
This article is now available in the October 2003 issue of JGV (vol. 84, 2613–2624). The complete issue of the journal may be seen in electronic form on JGV Online.
Click here for full text PDF