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Alphavirus adsorption to mosquito cells as viewed by freeze fracture immunolabeling.pdf
Virology 415 (2011) 132–140
Contents lists available at ScienceDirect
Virology
journal homepage: /locate/yviro
Alphavirus adsorption to mosquito cells as viewed by freeze fracture immunolabeling
Joseph P. Kononchik, Ricardo Vancini, Dennis T. Brown ?
Department of Molecular and Structural Biochemistry, NC State University, Raleigh, NC 27695, USA
article info
Article history: Received 14 December 2010 Returned to author for revision 11 April 2011 Accepted 22 April 2011 Available online 10 May 2011
Keywords: Alphavirus Cell penetration Insect cells Freeze-fracture Electron microscopy
abstract
Sindbis Virus (SV), the prototype alphavirus in the family togaviridae, infects both mammalian and insect cells. The ability of SV to infect cells possessing signi?cantly different biochemical environments suggests that there may be a common mode of entry into each cell type. Previous studies show that up to 4 h post infection cells are permeable to small ions and alpha sarcin suggesting that the plasma membrane is compromised as infection takes place. Thin-section electron microscopy has also shown SV to bind to the plasma membrane and lose its electron dense core through a pore like structure developed upon interaction of the virus with the cell surface. Using freeze-fracture replicas, thin-sections and antibody labeling the data presented herein show virus associated with intramembrane particles on mosquito cells. These data suggest that the intramembrane particles associated with SV may be part of the pore structure consisting of virus proteins and cell receptor.
? 2011 Elsevier Inc. All rights reserved.
Introduction
The structure and function of Sindbis Virus (SV) have been studied extensively. Currently, there is a cryo-reconstruction of the virus showing the T = 4 organization of the outer glycoprotein shell, and its tight interaction with the inner capsid protein shell that surrounds the RNA core (Paredes et al., 1993). Two glycoproteins, E1 and E2, make up the outer prot
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