The SR-rich motif in SARS-CoV nucleocapsid protein is important for virus replication.
Identifieur interne : 001E91 ( Ncbi/Curation ); précédent : 001E90; suivant : 001E92The SR-rich motif in SARS-CoV nucleocapsid protein is important for virus replication.
Auteurs : Shaun Tylor [Canada] ; Anton Andonov ; Todd Cutts ; Jingxin Cao ; Elsey Grudesky ; Gary Van Domselaar ; Xuguang Li ; Runtao HeSource :
- Canadian journal of microbiology [ 0008-4166 ] ; 2009.
Descripteurs français
- KwdFr :
- Animaux, Arginine (), Cellules Vero, Données de séquences moléculaires, Humains, Motifs d'acides aminés (génétique), Protéines nucléocapside (), Protéines nucléocapside (génétique), Protéines nucléocapside (métabolisme), Réplication virale, Séquence d'acides aminés, Sérine (), Transfection, Virus du SRAS (génétique), Virus du SRAS (métabolisme), Virus du SRAS (physiologie).
- MESH :
- génétique : Motifs d'acides aminés, Protéines nucléocapside, Virus du SRAS.
- métabolisme : Protéines nucléocapside, Virus du SRAS.
- physiologie : Virus du SRAS.
- Animaux, Arginine, Cellules Vero, Données de séquences moléculaires, Humains, Protéines nucléocapside, Réplication virale, Séquence d'acides aminés, Sérine, Transfection.
English descriptors
- KwdEn :
- Amino Acid Motifs (genetics), Amino Acid Sequence, Animals, Arginine (chemistry), Chlorocebus aethiops, Humans, Molecular Sequence Data, Nucleocapsid Proteins (chemistry), Nucleocapsid Proteins (genetics), Nucleocapsid Proteins (metabolism), SARS Virus (genetics), SARS Virus (metabolism), SARS Virus (physiology), Serine (chemistry), Transfection, Vero Cells, Virus Replication.
- MESH :
- chemical , chemistry : Arginine, Nucleocapsid Proteins, Serine.
- genetics : Amino Acid Motifs, Nucleocapsid Proteins, SARS Virus.
- chemical , metabolism : Nucleocapsid Proteins, SARS Virus.
- physiology : SARS Virus.
- Amino Acid Sequence, Animals, Chlorocebus aethiops, Humans, Molecular Sequence Data, Transfection, Vero Cells, Virus Replication.
Abstract
The multimerization/self-interaction of viral proteins is an important step in the process of viral assembly and maturation. Our previous study indicated that the severe acute respiratory syndrome-associated coronavirus (SARS-CoV) nucleocapsid protein forms self-multimers through a serine-arginine (SR)-rich motif (SSRSSSRSRGNSR) by using a mammalian two-hybrid system. To determine the biological relevance of this motif, we constructed a SARS-CoV reverse genetic construct by using a bacterial artificial chromosome (BAC)-based vector controlled by a T7 promoter; and subsequently deleted the SR-rich motif from the N gene. The mutated infectious clone showed reduced level of genome transcription and significantly reduced levels of the infectious virions. These results strongly suggest that the SR-rich motif is critical for effective virus replication.
DOI: 10.1139/w08-139
PubMed: 19370068
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Our previous study indicated that the severe acute respiratory syndrome-associated coronavirus (SARS-CoV) nucleocapsid protein forms self-multimers through a serine-arginine (SR)-rich motif (SSRSSSRSRGNSR) by using a mammalian two-hybrid system. To determine the biological relevance of this motif, we constructed a SARS-CoV reverse genetic construct by using a bacterial artificial chromosome (BAC)-based vector controlled by a T7 promoter; and subsequently deleted the SR-rich motif from the N gene. The mutated infectious clone showed reduced level of genome transcription and significantly reduced levels of the infectious virions. These results strongly suggest that the SR-rich motif is critical for effective virus replication.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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