Two palmitylated cysteine residues of the severe acute respiratory syndrome coronavirus spike (S) protein are critical for S incorporation into virus-like particles, but not for M-S co-localization.
Identifieur interne : 001C30 ( Main/Exploration ); précédent : 001C29; suivant : 001C31Two palmitylated cysteine residues of the severe acute respiratory syndrome coronavirus spike (S) protein are critical for S incorporation into virus-like particles, but not for M-S co-localization.
Auteurs : Makoto Ujike [Japon] ; Cheng Huang [États-Unis] ; Kazuya Shirato [Japon] ; Shutoku Matsuyama [Japon] ; Shinji Makino [États-Unis] ; Fumihiro Taguchi [Japon]Source :
- The Journal of general virology [ 1465-2099 ] ; 2012.
Descripteurs français
- KwdFr :
- Acide palmitique (métabolisme), Animaux, Assemblage viral (physiologie), Cellules COS, Cystéine (métabolisme), Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (métabolisme), Protéines de l'enveloppe virale (métabolisme), Protéines de la matrice virale (métabolisme), Souris, Syndrome respiratoire aigu sévère (virologie), Virion (métabolisme), Virion (physiologie), Virus du SRAS (métabolisme), Virus du SRAS (physiologie).
- MESH :
- métabolisme : Acide palmitique, Cystéine, Glycoprotéines membranaires, Protéines de l'enveloppe virale, Protéines de la matrice virale, Virion, Virus du SRAS.
- physiologie : Assemblage viral, Virion, Virus du SRAS.
- virologie : Syndrome respiratoire aigu sévère.
- Animaux, Cellules COS, Glycoprotéine de spicule des coronavirus, Souris.
English descriptors
- KwdEn :
- Animals, COS Cells, Chlorocebus aethiops, Cysteine (metabolism), Membrane Glycoproteins (metabolism), Mice, Palmitic Acid (metabolism), SARS Virus (metabolism), SARS Virus (physiology), Severe Acute Respiratory Syndrome (virology), Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (metabolism), Viral Matrix Proteins (metabolism), Virion (metabolism), Virion (physiology), Virus Assembly (physiology).
- MESH :
- chemical , metabolism : Cysteine, Membrane Glycoproteins, Palmitic Acid, Viral Envelope Proteins, Viral Matrix Proteins.
- metabolism : SARS Virus, Virion.
- physiology : SARS Virus, Virion, Virus Assembly.
- virology : Severe Acute Respiratory Syndrome.
- Animals, COS Cells, Chlorocebus aethiops, Mice, Spike Glycoprotein, Coronavirus.
Abstract
The endodomain of several coronavirus (CoV) spike (S) proteins contains palmitylated cysteine residues and enables co-localization and interaction with the CoV membrane (M) protein. Depalmitylation of mouse hepatitis virus S proteins abolished this interaction, resulting in the failure of S incorporation into virions. In contrast, an immunofluorescence assay (IFA) showed that depalmitylated severe acute respiratory syndrome coronavirus (SCoV) S proteins still co-localized with the M protein in the budding site. Here, we determined the ability of depalmitylated SCoV S mutants to incorporate S into virus-like particles (VLPs). IFA confirmed that all SCoV S mutants co-localized with the M protein intracellularly. However, the mutants lacking two cysteine residues (C(1234/1235)) failed to incorporate S into VLPs. This indicated that these palmitylated cysteines are essential for S incorporation, but are not involved in S co-localization mediated by the M protein. Our findings suggest that M-S co-localization and S incorporation occur independently of one another in SCoV virion assembly.
DOI: 10.1099/vir.0.038091-0
PubMed: 22238235
Affiliations:
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Le document en format XML
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<term>Mice</term>
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<front><div type="abstract" xml:lang="en">The endodomain of several coronavirus (CoV) spike (S) proteins contains palmitylated cysteine residues and enables co-localization and interaction with the CoV membrane (M) protein. Depalmitylation of mouse hepatitis virus S proteins abolished this interaction, resulting in the failure of S incorporation into virions. In contrast, an immunofluorescence assay (IFA) showed that depalmitylated severe acute respiratory syndrome coronavirus (SCoV) S proteins still co-localized with the M protein in the budding site. Here, we determined the ability of depalmitylated SCoV S mutants to incorporate S into virus-like particles (VLPs). IFA confirmed that all SCoV S mutants co-localized with the M protein intracellularly. However, the mutants lacking two cysteine residues (C(1234/1235)) failed to incorporate S into VLPs. This indicated that these palmitylated cysteines are essential for S incorporation, but are not involved in S co-localization mediated by the M protein. Our findings suggest that M-S co-localization and S incorporation occur independently of one another in SCoV virion assembly.</div>
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