Structural Evidence of Glycoprotein Assembly in Cellular Membrane Compartments prior to Alphavirus Budding

Author:

Soonsawad Pan123,Xing Li1,Milla Emerson1,Espinoza Juan M.1,Kawano Masaaki1,Marko Michael4,Hsieh Chyongere4,Furukawa Hiromitsu5,Kawasaki Masahiro5,Weerachatyanukul Wattana2,Srivastava Ranjana6,Barnett Susan W.6,Srivastava Indresh K.6,Cheng R. Holland1

Affiliation:

1. Department of Molecular and Cellular Biology, University of California, Davis, California 95616-8536

2. Department of Anatomy, Faculty of Science, Mahidol University, Bangkok, Thailand

3. Faculty of Dentistry, Mahidol University, Bangkok, Thailand

4. Resources for Visualization of Biological Complexity, Wadsworth Center, Albany, New York 12201

5. Japan Electron Optics Laboratory System and Technology Co., 3-1-2 Musashino, Tokyo, Japan

6. Novartis Vaccines and Diagnostics, Inc., 350 Massachusetts Ave., Cambridge, Massachusetts 02139

Abstract

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.

Publisher

American Society for Microbiology

Subject

Virology,Insect Science,Immunology,Microbiology

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