Structural evidence of glycoprotein assembly in cellular membrane compartments prior to Alphavirus budding

P Soonsawad, L Xing, E Milla, JM Espinoza… - Journal of …, 2010 - Am Soc Microbiol
P Soonsawad, L Xing, E Milla, JM Espinoza, M Kawano, M Marko, C Hsieh, H Furukawa…
Journal of virology, 2010Am Soc Microbiol
Membrane glycoproteins of alphavirus play a critical role in the assembly and budding of
progeny virions. However, knowledge regarding transport of viral glycoproteins to the
plasma membrane is obscure. In this study, we investigated the role of cytopathic vacuole
type II (CPV-II) through in situ electron tomography of alphavirus-infected cells. The results
revealed that CPV-II contains viral glycoproteins arranged in helical tubular arrays
resembling the basic organization of glycoprotein trimers on the envelope of the mature …
Abstract
Membrane glycoproteins of alphavirus play a critical role in the assembly and budding of progeny virions. However, knowledge regarding transport of viral glycoproteins to the plasma membrane is obscure. In this study, we investigated the role of cytopathic vacuole type II (CPV-II) through in situ electron tomography of alphavirus-infected cells. The results revealed that CPV-II contains viral glycoproteins arranged in helical tubular arrays resembling the basic organization of glycoprotein trimers on the envelope of the mature virions. The location of CPV-II adjacent to the site of viral budding suggests a model for the transport of structural components to the site of budding. Thus, the structural characteristics of CPV-II can be used in evaluating the design of a packaging cell line for replicon production.
American Society for Microbiology