Coronavirus envelope (E) protein remains at the site of assembly

Pavithra Venkatagopalan; Sasha M. Daskalova; Lisa A. Lopez; Kelly A. Dolezal; Brenda Hogue

doi:10.1016/j.virol.2015.02.005

Coronavirus envelope (E) protein remains at the site of assembly

Pavithra Venkatagopalan, Sasha M. Daskalova, Lisa A. Lopez, Kelly A. Dolezal, Brenda Hogue

Research output: Contribution to journal › Article › peer-review

159 Scopus citations

Abstract

Coronaviruses (CoVs) assemble at endoplasmic reticulum Golgi intermediate compartment (ERGIC) membranes and egress from cells in cargo vesicles. Only a few molecules of the envelope (E) protein are assembled into virions. The role of E in morphogenesis is not fully understood. The cellular localization and dynamics of mouse hepatitis CoV A59 (MHV) E protein were investigated to further understanding of its role during infection. E protein localized in the ERGIC and Golgi with the amino and carboxy termini in the lumen and cytoplasm, respectively. E protein does not traffic to the cell surface. MHV was genetically engineered with a tetracysteine tag at the carboxy end of E. Fluorescence recovery after photobleaching (FRAP) showed that E is mobile in ERGIC/Golgi membranes. Correlative light electron microscopy (CLEM) confirmed the presence of E in Golgi cisternae. The results provide strong support that E proteins carry out their function(s) at the site of budding/assembly.

Original language	English (US)
Pages (from-to)	75-85
Number of pages	11
Journal	Virology
Volume	478
DOIs	https://doi.org/10.1016/j.virol.2015.02.005
State	Published - Apr 1 2015

Keywords

CLEM
Coronavirus
Envelope protein
FRAP
Live-cell imaging
Protein transport/localization
Virus assembly

ASJC Scopus subject areas

Virology

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10.1016/j.virol.2015.02.005

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title = "Coronavirus envelope (E) protein remains at the site of assembly",

abstract = "Coronaviruses (CoVs) assemble at endoplasmic reticulum Golgi intermediate compartment (ERGIC) membranes and egress from cells in cargo vesicles. Only a few molecules of the envelope (E) protein are assembled into virions. The role of E in morphogenesis is not fully understood. The cellular localization and dynamics of mouse hepatitis CoV A59 (MHV) E protein were investigated to further understanding of its role during infection. E protein localized in the ERGIC and Golgi with the amino and carboxy termini in the lumen and cytoplasm, respectively. E protein does not traffic to the cell surface. MHV was genetically engineered with a tetracysteine tag at the carboxy end of E. Fluorescence recovery after photobleaching (FRAP) showed that E is mobile in ERGIC/Golgi membranes. Correlative light electron microscopy (CLEM) confirmed the presence of E in Golgi cisternae. The results provide strong support that E proteins carry out their function(s) at the site of budding/assembly.",

keywords = "CLEM, Coronavirus, Envelope protein, FRAP, Live-cell imaging, Protein transport/localization, Virus assembly",

author = "Pavithra Venkatagopalan and Daskalova, {Sasha M.} and Lopez, {Lisa A.} and Dolezal, {Kelly A.} and Brenda Hogue",

note = "Publisher Copyright: {\textcopyright} 2015 Elsevier Inc.",

year = "2015",

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doi = "10.1016/j.virol.2015.02.005",

language = "English (US)",

volume = "478",

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AU - Venkatagopalan, Pavithra

AU - Daskalova, Sasha M.

AU - Lopez, Lisa A.

AU - Dolezal, Kelly A.

AU - Hogue, Brenda

PY - 2015/4/1

Y1 - 2015/4/1

N2 - Coronaviruses (CoVs) assemble at endoplasmic reticulum Golgi intermediate compartment (ERGIC) membranes and egress from cells in cargo vesicles. Only a few molecules of the envelope (E) protein are assembled into virions. The role of E in morphogenesis is not fully understood. The cellular localization and dynamics of mouse hepatitis CoV A59 (MHV) E protein were investigated to further understanding of its role during infection. E protein localized in the ERGIC and Golgi with the amino and carboxy termini in the lumen and cytoplasm, respectively. E protein does not traffic to the cell surface. MHV was genetically engineered with a tetracysteine tag at the carboxy end of E. Fluorescence recovery after photobleaching (FRAP) showed that E is mobile in ERGIC/Golgi membranes. Correlative light electron microscopy (CLEM) confirmed the presence of E in Golgi cisternae. The results provide strong support that E proteins carry out their function(s) at the site of budding/assembly.

AB - Coronaviruses (CoVs) assemble at endoplasmic reticulum Golgi intermediate compartment (ERGIC) membranes and egress from cells in cargo vesicles. Only a few molecules of the envelope (E) protein are assembled into virions. The role of E in morphogenesis is not fully understood. The cellular localization and dynamics of mouse hepatitis CoV A59 (MHV) E protein were investigated to further understanding of its role during infection. E protein localized in the ERGIC and Golgi with the amino and carboxy termini in the lumen and cytoplasm, respectively. E protein does not traffic to the cell surface. MHV was genetically engineered with a tetracysteine tag at the carboxy end of E. Fluorescence recovery after photobleaching (FRAP) showed that E is mobile in ERGIC/Golgi membranes. Correlative light electron microscopy (CLEM) confirmed the presence of E in Golgi cisternae. The results provide strong support that E proteins carry out their function(s) at the site of budding/assembly.

KW - CLEM

KW - Coronavirus

KW - Envelope protein

KW - FRAP

KW - Live-cell imaging

KW - Protein transport/localization

KW - Virus assembly

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Coronavirus envelope (E) protein remains at the site of assembly

Abstract

Keywords

ASJC Scopus subject areas

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