Severe acute respiratory syndrome coronavirus nucleocapsid protein confers ability to efficiently produce virus-like particles when substituted for the human immunodeficiency virus nucleocapsid domain.
Identifieur interne : 003019 ( Main/Exploration ); précédent : 003018; suivant : 003020Severe acute respiratory syndrome coronavirus nucleocapsid protein confers ability to efficiently produce virus-like particles when substituted for the human immunodeficiency virus nucleocapsid domain.
Auteurs : Shui-Mei Wang [République populaire de Chine] ; Yu-Fen Chang ; Yi-Ming Arthur Chen ; Chin-Tien WangSource :
- Journal of biomedical science [ 1423-0127 ] ; 2008.
Descripteurs français
- KwdFr :
- Cartographie peptidique, Centrifugation en gradient de densité, Humains, Lignée cellulaire, Protéines de fusion recombinantes (métabolisme), Protéines nucléocapside (génétique), Protéines nucléocapside (métabolisme), Saccharose (), VIH (Virus de l'Immunodéficience Humaine) (génétique), VIH (Virus de l'Immunodéficience Humaine) (métabolisme), Virion (métabolisme), Virus du SRAS (génétique), Virus du SRAS (métabolisme), Virus du SRAS (physiologie).
- MESH :
- génétique : Protéines nucléocapside, VIH (Virus de l'Immunodéficience Humaine), Virus du SRAS.
- métabolisme : Protéines de fusion recombinantes, Protéines nucléocapside, VIH (Virus de l'Immunodéficience Humaine), Virion, Virus du SRAS.
- physiologie : Virus du SRAS.
- Cartographie peptidique, Centrifugation en gradient de densité, Humains, Lignée cellulaire, Saccharose.
English descriptors
- KwdEn :
- Cell Line, Centrifugation, Density Gradient, HIV (genetics), HIV (metabolism), Humans, Nucleocapsid Proteins (genetics), Nucleocapsid Proteins (metabolism), Peptide Mapping, Recombinant Fusion Proteins (metabolism), SARS Virus (genetics), SARS Virus (metabolism), SARS Virus (physiology), Sucrose (chemistry), Virion (metabolism).
- MESH :
- chemical , chemistry : Sucrose.
- chemical , genetics : Nucleocapsid Proteins.
- genetics : HIV, SARS Virus.
- metabolism : HIV, Nucleocapsid Proteins, Recombinant Fusion Proteins, SARS Virus, Virion.
- physiology : SARS Virus.
- Cell Line, Centrifugation, Density Gradient, Humans, Peptide Mapping.
Abstract
We replaced the HIV-1 nucleocapsid (NC) domain with different N-coding sequences to test SARS-CoV nucleocapsid (N) self-interaction capacity, and determined the capabilities of each chimera to direct virus-like particle (VLP) assembly. Analysis results indicate that the replacement of NC with the carboxyl-terminal half of the SARS-CoV N resulted in the production of wild type (wt)-level virus-like particles (VLPs) with the density of a wt HIV-1 particle. When co-expressed with SARS-CoV N, chimeras containing the N carboxyl-terminal half sequence efficiently packaged N. However, the same was not true for the chimera bearing the N amino-terminal half sequence, despite its production of substantial amounts of VLPs. According to further analysis, HIV-1 NC replacement with N residues 2-213, 215-421, or 234-421 resulted in efficient VLP production at levels comparable to that of wt HIV-1, but replacement with residues 215-359, 302-421, 2-168, or 2-86 failed to restore VLP production to wild-type levels. The results suggest that the domain conferring the ability to direct VLP assembly and release in SARS-CoV N is largely contained between residues 168 and 421.
DOI: 10.1007/s11373-008-9265-8
PubMed: 18592403
Affiliations:
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Le document en format XML
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<front><div type="abstract" xml:lang="en">We replaced the HIV-1 nucleocapsid (NC) domain with different N-coding sequences to test SARS-CoV nucleocapsid (N) self-interaction capacity, and determined the capabilities of each chimera to direct virus-like particle (VLP) assembly. Analysis results indicate that the replacement of NC with the carboxyl-terminal half of the SARS-CoV N resulted in the production of wild type (wt)-level virus-like particles (VLPs) with the density of a wt HIV-1 particle. When co-expressed with SARS-CoV N, chimeras containing the N carboxyl-terminal half sequence efficiently packaged N. However, the same was not true for the chimera bearing the N amino-terminal half sequence, despite its production of substantial amounts of VLPs. According to further analysis, HIV-1 NC replacement with N residues 2-213, 215-421, or 234-421 resulted in efficient VLP production at levels comparable to that of wt HIV-1, but replacement with residues 215-359, 302-421, 2-168, or 2-86 failed to restore VLP production to wild-type levels. The results suggest that the domain conferring the ability to direct VLP assembly and release in SARS-CoV N is largely contained between residues 168 and 421.</div>
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