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Intracellular targeting signals contribute to localization of coronavirus spike proteins near the virus assembly site.

Identifieur interne : 002E00 ( PubMed/Curation ); précédent : 002D99; suivant : 002E01

Intracellular targeting signals contribute to localization of coronavirus spike proteins near the virus assembly site.

Auteurs : Erik Lontok [États-Unis] ; Emily Corse ; Carolyn E. Machamer

Source :

Journal of virology [ 0022-538X ] ; 2004.

RBID : pubmed:15140989

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Motifs, Amino Acid Sequence, Dipeptides, Endoplasmic Reticulum (physiology), Golgi Apparatus (physiology), HeLa Cells, Humans, Infectious bronchitis virus (physiology), Membrane Glycoproteins (chemistry), Membrane Glycoproteins (physiology), Molecular Sequence Data, Protein Transport, Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (physiology), Virus Assembly.
MESH :
- chemical , chemistry : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , physiology : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical : Dipeptides, Spike Glycoprotein, Coronavirus.
- physiology : Endoplasmic Reticulum, Golgi Apparatus, Infectious bronchitis virus.
- Amino Acid Motifs, Amino Acid Sequence, HeLa Cells, Humans, Molecular Sequence Data, Protein Transport, Virus Assembly.

Abstract

Coronavirus budding at the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) requires accumulation of the viral envelope proteins at this point in the secretory pathway. Here we demonstrate that the spike (S) protein from the group 3 coronavirus infectious bronchitis virus (IBV) contains a canonical dilysine endoplasmic reticulum retrieval signal (-KKXX-COOH) in its cytoplasmic tail. This signal can retain a chimeric reporter protein in the ERGIC and when mutated allows transport of the full-length S protein as well as the chimera to the plasma membrane. Interestingly, the IBV S protein also contains a tyrosine-based endocytosis signal in its cytoplasmic tail, suggesting that any S protein that escapes the ERGIC will be rapidly endocytosed when it reaches the plasma membrane. We also identified a novel dibasic motif (-KXHXX-COOH) in the cytoplasmic tails of S proteins from group 1 coronaviruses and from the newly identified coronavirus implicated in severe acute respiratory syndrome. This dibasic motif also retained a reporter protein in the ERGIC, similar to the dilysine motif in IBV S. The cytoplasmic tails of S proteins from group 2 coronaviruses lack an intracellular localization signal. The inherent differences in S-protein trafficking could point to interesting variations in pathogenesis of coronaviruses, since increased levels of surface S protein could promote syncytium formation and direct cell-to-cell spread of the infection.

DOI: 10.1128/JVI.78.11.5913-5922.2004
PubMed: 15140989

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Le document en format XML

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<term>Glycoprotéines membranaires ()</term>
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<front><div type="abstract" xml:lang="en">Coronavirus budding at the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) requires accumulation of the viral envelope proteins at this point in the secretory pathway. Here we demonstrate that the spike (S) protein from the group 3 coronavirus infectious bronchitis virus (IBV) contains a canonical dilysine endoplasmic reticulum retrieval signal (-KKXX-COOH) in its cytoplasmic tail. This signal can retain a chimeric reporter protein in the ERGIC and when mutated allows transport of the full-length S protein as well as the chimera to the plasma membrane. Interestingly, the IBV S protein also contains a tyrosine-based endocytosis signal in its cytoplasmic tail, suggesting that any S protein that escapes the ERGIC will be rapidly endocytosed when it reaches the plasma membrane. We also identified a novel dibasic motif (-KXHXX-COOH) in the cytoplasmic tails of S proteins from group 1 coronaviruses and from the newly identified coronavirus implicated in severe acute respiratory syndrome. This dibasic motif also retained a reporter protein in the ERGIC, similar to the dilysine motif in IBV S. The cytoplasmic tails of S proteins from group 2 coronaviruses lack an intracellular localization signal. The inherent differences in S-protein trafficking could point to interesting variations in pathogenesis of coronaviruses, since increased levels of surface S protein could promote syncytium formation and direct cell-to-cell spread of the infection.</div>
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Intracellular targeting signals contribute to localization of coronavirus spike proteins near the virus assembly site.

Intracellular targeting signals contribute to localization of coronavirus spike proteins near the virus assembly site.

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