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

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 el...

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Main Authors: Pan Soonsawad, Li Xing, Emerson Milla, Juan M. Espinoza, Masaaki Kawano, Michael Marko, Chyongere Hsieh, Hiromitsu Furukawa, Masahiro Kawasaki, Wattana Weerachatyanukul, Ranjana Srivastava, Susan W. Barnett, Indresh K. Srivastava, R. Holland Cheng
Other Authors: University of California, Davis
Format: Article
Published: 2018
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Online Access:https://repository.li.mahidol.ac.th/handle/123456789/28557
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spelling th-mahidol.285572018-09-24T16:09:04Z Structural evidence of glycoprotein assembly in cellular membrane compartments prior to alphavirus budding Pan Soonsawad Li Xing Emerson Milla Juan M. Espinoza Masaaki Kawano Michael Marko Chyongere Hsieh Hiromitsu Furukawa Masahiro Kawasaki Wattana Weerachatyanukul Ranjana Srivastava Susan W. Barnett Indresh K. Srivastava R. Holland Cheng University of California, Davis Wadsworth Center for Laboratories and Research Japan Electron Optics Laboratory System and Technology Co. Mahidol University Novartis Vaccines and Diagnostics, Inc. Agricultural and Biological Sciences Immunology and Microbiology 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. Copyright © 2010, American Society for Microbiology. All Rights Reserved. 2018-09-24T08:40:19Z 2018-09-24T08:40:19Z 2010-01-01 Article Journal of Virology. Vol.84, No.21 (2010), 11145-11151 10.1128/JVI.00036-10 10985514 0022538X 2-s2.0-77957957373 https://repository.li.mahidol.ac.th/handle/123456789/28557 Mahidol University SCOPUS https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=77957957373&origin=inward
institution Mahidol University
building Mahidol University Library
continent Asia
country Thailand
Thailand
content_provider Mahidol University Library
collection Mahidol University Institutional Repository
topic Agricultural and Biological Sciences
Immunology and Microbiology
spellingShingle Agricultural and Biological Sciences
Immunology and Microbiology
Pan Soonsawad
Li Xing
Emerson Milla
Juan M. Espinoza
Masaaki Kawano
Michael Marko
Chyongere Hsieh
Hiromitsu Furukawa
Masahiro Kawasaki
Wattana Weerachatyanukul
Ranjana Srivastava
Susan W. Barnett
Indresh K. Srivastava
R. Holland Cheng
Structural evidence of glycoprotein assembly in cellular membrane compartments prior to alphavirus budding
description 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. Copyright © 2010, American Society for Microbiology. All Rights Reserved.
author2 University of California, Davis
author_facet University of California, Davis
Pan Soonsawad
Li Xing
Emerson Milla
Juan M. Espinoza
Masaaki Kawano
Michael Marko
Chyongere Hsieh
Hiromitsu Furukawa
Masahiro Kawasaki
Wattana Weerachatyanukul
Ranjana Srivastava
Susan W. Barnett
Indresh K. Srivastava
R. Holland Cheng
format Article
author Pan Soonsawad
Li Xing
Emerson Milla
Juan M. Espinoza
Masaaki Kawano
Michael Marko
Chyongere Hsieh
Hiromitsu Furukawa
Masahiro Kawasaki
Wattana Weerachatyanukul
Ranjana Srivastava
Susan W. Barnett
Indresh K. Srivastava
R. Holland Cheng
author_sort Pan Soonsawad
title Structural evidence of glycoprotein assembly in cellular membrane compartments prior to alphavirus budding
title_short Structural evidence of glycoprotein assembly in cellular membrane compartments prior to alphavirus budding
title_full Structural evidence of glycoprotein assembly in cellular membrane compartments prior to alphavirus budding
title_fullStr Structural evidence of glycoprotein assembly in cellular membrane compartments prior to alphavirus budding
title_full_unstemmed Structural evidence of glycoprotein assembly in cellular membrane compartments prior to alphavirus budding
title_sort structural evidence of glycoprotein assembly in cellular membrane compartments prior to alphavirus budding
publishDate 2018
url https://repository.li.mahidol.ac.th/handle/123456789/28557
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