Analyses of Coronavirus Assembly Interactions with Interspecies Membrane and Nucleocapsid Protein Chimeras.
Identifieur interne : 001082 ( Main/Exploration ); précédent : 001081; suivant : 001083Analyses of Coronavirus Assembly Interactions with Interspecies Membrane and Nucleocapsid Protein Chimeras.
Auteurs : Lili Kuo [États-Unis] ; Kelley R. Hurst-Hess [États-Unis] ; Cheri A. Koetzner [États-Unis] ; Paul S. MastersSource :
- Journal of virology [ 1098-5514 ] ; 2016.
Descripteurs français
- KwdFr :
- Alignement de séquences, Animaux, Assemblage viral, Coronavirus (physiologie), Données de séquences moléculaires, Infections à coronavirus (virologie), Liaison aux protéines, Lignée cellulaire, Motifs et domaines d'intéraction protéique, Mutation, Protéines de la matrice virale (), Protéines de la matrice virale (génétique), Protéines de la matrice virale (métabolisme), Protéines nucléocapside (), Protéines nucléocapside (génétique), Protéines nucléocapside (métabolisme), Réplication virale, Souris, Séquence d'acides aminés, Vecteurs génétiques (génétique), Virion, Virus de l'hépatite murine (physiologie).
- MESH :
- génétique : Protéines de la matrice virale, Protéines nucléocapside, Vecteurs génétiques.
- métabolisme : Protéines de la matrice virale, Protéines nucléocapside.
- physiologie : Coronavirus, Virus de l'hépatite murine.
- virologie : Infections à coronavirus.
- Alignement de séquences, Animaux, Assemblage viral, Données de séquences moléculaires, Liaison aux protéines, Lignée cellulaire, Motifs et domaines d'intéraction protéique, Mutation, Protéines de la matrice virale, Protéines nucléocapside, Réplication virale, Souris, Séquence d'acides aminés, Virion.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Cell Line, Coronavirus (physiology), Coronavirus Infections (virology), Genetic Vectors (genetics), Mice, Molecular Sequence Data, Murine hepatitis virus (physiology), Mutation, Nucleocapsid Proteins (chemistry), Nucleocapsid Proteins (genetics), Nucleocapsid Proteins (metabolism), Protein Binding, Protein Interaction Domains and Motifs, Sequence Alignment, Viral Matrix Proteins (chemistry), Viral Matrix Proteins (genetics), Viral Matrix Proteins (metabolism), Virion, Virus Assembly, Virus Replication.
- MESH :
- chemical , chemistry : Nucleocapsid Proteins, Viral Matrix Proteins.
- genetics : Genetic Vectors, Nucleocapsid Proteins, Viral Matrix Proteins.
- chemical , metabolism : Nucleocapsid Proteins, Viral Matrix Proteins.
- physiology : Coronavirus, Murine hepatitis virus.
- virology : Coronavirus Infections.
- Amino Acid Sequence, Animals, Cell Line, Mice, Molecular Sequence Data, Mutation, Protein Binding, Protein Interaction Domains and Motifs, Sequence Alignment, Virion, Virus Assembly, Virus Replication.
Abstract
The coronavirus membrane (M) protein is the central actor in virion morphogenesis. M organizes the components of the viral membrane, and interactions of M with itself and with the nucleocapsid (N) protein drive virus assembly and budding. In order to further define M-M and M-N interactions, we constructed mutants of the model coronavirus mouse hepatitis virus (MHV) in which all or part of the M protein was replaced by its phylogenetically divergent counterpart from severe acute respiratory syndrome coronavirus (SARS-CoV). We were able to obtain viable chimeras containing the entire SARS-CoV M protein as well as mutants with intramolecular substitutions that partitioned M protein at the boundaries between the ectodomain, transmembrane domains, or endodomain. Our results show that the carboxy-terminal domain of N protein, N3, is necessary and sufficient for interaction with M protein. However, despite some previous genetic and biochemical evidence that mapped interactions with N to the carboxy terminus of M, it was not possible to define a short linear region of M protein sufficient for assembly with N. Thus, interactions with N protein likely involve multiple linearly discontiguous regions of the M endodomain. The SARS-CoV M chimera exhibited a conditional growth defect that was partially suppressed by mutations in the envelope (E) protein. Moreover, virions of the M chimera were markedly deficient in spike (S) protein incorporation. These findings suggest that the interactions of M protein with both E and S protein are more complex than previously thought.
DOI: 10.1128/JVI.03212-15
PubMed: 26889024
Affiliations:
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Masters</name><affiliation><nlm:affiliation>Wadsworth Center, New York State Department of Health, Albany, New York, USA Paul.Masters@health.ny.gov.</nlm:affiliation><wicri:noCountry code="subField">USA Paul.Masters@health.ny.gov.</wicri:noCountry></affiliation></author></analytic><series><title level="j">Journal of virology</title><idno type="eISSN">1098-5514</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Cell Line</term><term>Coronavirus (physiology)</term><term>Coronavirus Infections (virology)</term><term>Genetic Vectors (genetics)</term><term>Mice</term><term>Molecular Sequence Data</term><term>Murine hepatitis virus (physiology)</term><term>Mutation</term><term>Nucleocapsid Proteins (chemistry)</term><term>Nucleocapsid Proteins (genetics)</term><term>Nucleocapsid Proteins (metabolism)</term><term>Protein Binding</term><term>Protein Interaction Domains and Motifs</term><term>Sequence Alignment</term><term>Viral Matrix Proteins (chemistry)</term><term>Viral Matrix Proteins (genetics)</term><term>Viral Matrix Proteins (metabolism)</term><term>Virion</term><term>Virus Assembly</term><term>Virus Replication</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences</term><term>Animaux</term><term>Assemblage viral</term><term>Coronavirus (physiologie)</term><term>Données de séquences moléculaires</term><term>Infections à coronavirus (virologie)</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Motifs et domaines d'intéraction protéique</term><term>Mutation</term><term>Protéines de la matrice virale ()</term><term>Protéines de la matrice virale (génétique)</term><term>Protéines de la matrice virale (métabolisme)</term><term>Protéines nucléocapside ()</term><term>Protéines nucléocapside (génétique)</term><term>Protéines nucléocapside (métabolisme)</term><term>Réplication virale</term><term>Souris</term><term>Séquence d'acides aminés</term><term>Vecteurs génétiques (génétique)</term><term>Virion</term><term>Virus de l'hépatite murine (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Nucleocapsid Proteins</term><term>Viral Matrix Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Genetic Vectors</term><term>Nucleocapsid Proteins</term><term>Viral Matrix Proteins</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Protéines de la matrice virale</term><term>Protéines nucléocapside</term><term>Vecteurs génétiques</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Nucleocapsid Proteins</term><term>Viral Matrix Proteins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Protéines de la matrice virale</term><term>Protéines nucléocapside</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Coronavirus</term><term>Virus de l'hépatite murine</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Coronavirus</term><term>Murine hepatitis virus</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Infections à coronavirus</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Coronavirus Infections</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Cell Line</term><term>Mice</term><term>Molecular Sequence Data</term><term>Mutation</term><term>Protein Binding</term><term>Protein Interaction Domains and Motifs</term><term>Sequence Alignment</term><term>Virion</term><term>Virus Assembly</term><term>Virus Replication</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term><term>Animaux</term><term>Assemblage viral</term><term>Données de séquences moléculaires</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Motifs et domaines d'intéraction protéique</term><term>Mutation</term><term>Protéines de la matrice virale</term><term>Protéines nucléocapside</term><term>Réplication virale</term><term>Souris</term><term>Séquence d'acides aminés</term><term>Virion</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The coronavirus membrane (M) protein is the central actor in virion morphogenesis. M organizes the components of the viral membrane, and interactions of M with itself and with the nucleocapsid (N) protein drive virus assembly and budding. In order to further define M-M and M-N interactions, we constructed mutants of the model coronavirus mouse hepatitis virus (MHV) in which all or part of the M protein was replaced by its phylogenetically divergent counterpart from severe acute respiratory syndrome coronavirus (SARS-CoV). We were able to obtain viable chimeras containing the entire SARS-CoV M protein as well as mutants with intramolecular substitutions that partitioned M protein at the boundaries between the ectodomain, transmembrane domains, or endodomain. Our results show that the carboxy-terminal domain of N protein, N3, is necessary and sufficient for interaction with M protein. However, despite some previous genetic and biochemical evidence that mapped interactions with N to the carboxy terminus of M, it was not possible to define a short linear region of M protein sufficient for assembly with N. Thus, interactions with N protein likely involve multiple linearly discontiguous regions of the M endodomain. The SARS-CoV M chimera exhibited a conditional growth defect that was partially suppressed by mutations in the envelope (E) protein. Moreover, virions of the M chimera were markedly deficient in spike (S) protein incorporation. These findings suggest that the interactions of M protein with both E and S protein are more complex than previously thought.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>État de New York</li></region></list><tree><noCountry><name sortKey="Masters, Paul S" sort="Masters, Paul S" uniqKey="Masters P" first="Paul S" last="Masters">Paul S. Masters</name></noCountry><country name="États-Unis"><region name="État de New York"><name sortKey="Kuo, Lili" sort="Kuo, Lili" uniqKey="Kuo L" first="Lili" last="Kuo">Lili Kuo</name></region><name sortKey="Hurst Hess, Kelley R" sort="Hurst Hess, Kelley R" uniqKey="Hurst Hess K" first="Kelley R" last="Hurst-Hess">Kelley R. Hurst-Hess</name><name sortKey="Koetzner, Cheri A" sort="Koetzner, Cheri A" uniqKey="Koetzner C" first="Cheri A" last="Koetzner">Cheri A. Koetzner</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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