Palmitoylation of virus proteins
Identifieur interne : 001E50 ( Main/Exploration ); précédent : 001E49; suivant : 001E51Palmitoylation of virus proteins
Auteurs : Michael Veit [Allemagne]Source :
- Biology of the Cell [ 0248-4900 ] ; 2012-09.
English descriptors
- Teeft :
- Acad, Acid, Acyl, Acyl chain, Acylated, Acylated cysteine, Acylation, Acylation site, Acylation sites, Amino, Amino acids, Amphiphilic helix, Bilayer, Biochem, Biol, Biologie, Biologie cellulaire, Cell attachment, Cell biol, Cell surface, Cellulaire, Cellular, Cellular proteins, Chem, Core protein, Coronavirus, Covs, Cysteine, Cysteine residues, Cytoplasmic, Cytoplasmic cysteines, Cytoplasmic domain, Cytoplasmic tail, Deletion, Dhhc, Dhhc proteins, Drms, Escrt, Exocytic pathway, Fatty, Fatty acid, Fatty acids, Febs lett, Fusion, Fusion pore formation, Fusion process, Fusion protein, Genome, Glycoprotein, Golgi, Hairpin topology, Helix, Hemagglutinin, Hemifusion, Herrmann, Hydrophobic, Infectivity, Insect cells, Internal components, Intracellular, Kordyukova, Linder, Lipid, Lipid rafts, Localisation, Machamer, Membrane, Membrane binding, Membrane fusion, Membrane proteins, Membrane rafts, Membrane topology, Murine, Mutation, Myristate, Natl, Nsp1, Palmitate, Palmitic acid, Palmitoylated, Palmitoylated proteins, Palmitoylation, Palmitoylation site, Palmitoylation sites, Pathway, Peptide, Peripheral membrane proteins, Plasma membrane, Proc, Protein, Protein palmitoylation, Raft, Raft association, Rafts, Receptor, Replication, Respiratory syndrome, Retrovirus, Review palmitoylation, Roth, Sars, Schmidt, Scission, Semliki, Semliki forest virus, Sindbis, Sindbis virus, Societe, Societe francaise, Spike, Spike protein, Spike proteins, Stearate, Stearic, Stearic acid, Structural proteins, Subunit, Syncytium formation, Thaa, Togaviruses, Topology, Transmembrane, Transmembrane cysteine, Transmembrane domain, Transmembrane protein, Transmembrane proteins, Transmembrane region, Trimeric, Uorescent protein, Veit, Vesicular, Viral, Viral envelope, Viral genome, Viral glycoproteins, Viral proteins, Viral spike proteins, Virion, Virol, Virology, Viroporins, Virus, Virus assembly, Virus entry, Virus hemagglutinin, Virus infectivity, Virus particle, Virus particles, Virus proteins, Virus release, Virus replication.
Abstract
The article summarises the results of more than 30 years of research on palmitoylation (S‐acylation) of viral proteins, the post‐translational attachment of fatty acids to cysteine residues of integral and peripheral membrane proteins. Analysing viral proteins is not only important to characterise the cellular pathogens but also instrumental to decipher the palmitoylation machinery of cells. This comprehensive review describes methods to identify S‐acylated proteins and covers the fundamental biochemistry of palmitoylation: the location of palmitoylation sites in viral proteins, the fatty acid species found in S‐acylated proteins, the intracellular site of palmitoylation and the enzymology of the reaction. Finally, the functional consequences of palmitoylation are discussed regarding binding of proteins to membranes or membrane rafts, entry of enveloped viruses into target cells by spike‐mediated membrane fusion as well as assembly and release of virus particles from infected cells. The topics are described mainly for palmitoylated proteins of influenza virus, but proteins of other important pathogens, such as the causative agents of AIDS and severe acute respiratory syndrome, and of model viruses are discussed.
The article covers the biochemistry, cell biology and functional role of palmitoylation of viral proteins, especially of spike proteins. The transmembrane and cytoplasmic domains of influenza virus hemagglutinin are shown, which contains three fatty acids covalently linked to conserved cysteines. The cysteine at the beginning of the transmembrane region is acylated with stearic acid (yellow zigzag line), whereas the two cytoplasmic cysteines contain palmitic acid (red zigzag line). The model was created by Oliver Ernst (Biochemiezentrum, Heidelberg) using BallView 1.3.
Url:
DOI: 10.1111/boc.201200006
Affiliations:
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acids</term><term>Febs lett</term><term>Fusion</term><term>Fusion pore formation</term><term>Fusion process</term><term>Fusion protein</term><term>Genome</term><term>Glycoprotein</term><term>Golgi</term><term>Hairpin topology</term><term>Helix</term><term>Hemagglutinin</term><term>Hemifusion</term><term>Herrmann</term><term>Hydrophobic</term><term>Infectivity</term><term>Insect cells</term><term>Internal components</term><term>Intracellular</term><term>Kordyukova</term><term>Linder</term><term>Lipid</term><term>Lipid rafts</term><term>Localisation</term><term>Machamer</term><term>Membrane</term><term>Membrane binding</term><term>Membrane fusion</term><term>Membrane proteins</term><term>Membrane rafts</term><term>Membrane topology</term><term>Murine</term><term>Mutation</term><term>Myristate</term><term>Natl</term><term>Nsp1</term><term>Palmitate</term><term>Palmitic acid</term><term>Palmitoylated</term><term>Palmitoylated proteins</term><term>Palmitoylation</term><term>Palmitoylation site</term><term>Palmitoylation sites</term><term>Pathway</term><term>Peptide</term><term>Peripheral membrane proteins</term><term>Plasma membrane</term><term>Proc</term><term>Protein</term><term>Protein palmitoylation</term><term>Raft</term><term>Raft association</term><term>Rafts</term><term>Receptor</term><term>Replication</term><term>Respiratory syndrome</term><term>Retrovirus</term><term>Review palmitoylation</term><term>Roth</term><term>Sars</term><term>Schmidt</term><term>Scission</term><term>Semliki</term><term>Semliki forest virus</term><term>Sindbis</term><term>Sindbis virus</term><term>Societe</term><term>Societe francaise</term><term>Spike</term><term>Spike protein</term><term>Spike proteins</term><term>Stearate</term><term>Stearic</term><term>Stearic acid</term><term>Structural proteins</term><term>Subunit</term><term>Syncytium formation</term><term>Thaa</term><term>Togaviruses</term><term>Topology</term><term>Transmembrane</term><term>Transmembrane cysteine</term><term>Transmembrane domain</term><term>Transmembrane protein</term><term>Transmembrane proteins</term><term>Transmembrane region</term><term>Trimeric</term><term>Uorescent protein</term><term>Veit</term><term>Vesicular</term><term>Viral</term><term>Viral envelope</term><term>Viral genome</term><term>Viral glycoproteins</term><term>Viral proteins</term><term>Viral spike proteins</term><term>Virion</term><term>Virol</term><term>Virology</term><term>Viroporins</term><term>Virus</term><term>Virus assembly</term><term>Virus entry</term><term>Virus hemagglutinin</term><term>Virus infectivity</term><term>Virus particle</term><term>Virus particles</term><term>Virus proteins</term><term>Virus release</term><term>Virus replication</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The article summarises the results of more than 30 years of research on palmitoylation (S‐acylation) of viral proteins, the post‐translational attachment of fatty acids to cysteine residues of integral and peripheral membrane proteins. Analysing viral proteins is not only important to characterise the cellular pathogens but also instrumental to decipher the palmitoylation machinery of cells. This comprehensive review describes methods to identify S‐acylated proteins and covers the fundamental biochemistry of palmitoylation: the location of palmitoylation sites in viral proteins, the fatty acid species found in S‐acylated proteins, the intracellular site of palmitoylation and the enzymology of the reaction. Finally, the functional consequences of palmitoylation are discussed regarding binding of proteins to membranes or membrane rafts, entry of enveloped viruses into target cells by spike‐mediated membrane fusion as well as assembly and release of virus particles from infected cells. The topics are described mainly for palmitoylated proteins of influenza virus, but proteins of other important pathogens, such as the causative agents of AIDS and severe acute respiratory syndrome, and of model viruses are discussed.</div><div type="abstract" xml:lang="en">The article covers the biochemistry, cell biology and functional role of palmitoylation of viral proteins, especially of spike proteins. The transmembrane and cytoplasmic domains of influenza virus hemagglutinin are shown, which contains three fatty acids covalently linked to conserved cysteines. The cysteine at the beginning of the transmembrane region is acylated with stearic acid (yellow zigzag line), whereas the two cytoplasmic cysteines contain palmitic acid (red zigzag line). The model was created by Oliver Ernst (Biochemiezentrum, Heidelberg) using BallView 1.3.</div></front></TEI><affiliations><list><country><li>Allemagne</li></country><region><li>Berlin</li></region><settlement><li>Berlin</li></settlement></list><tree><country name="Allemagne"><region name="Berlin"><name sortKey="Veit, Michael" sort="Veit, Michael" uniqKey="Veit M" first="Michael" last="Veit">Michael Veit</name></region><name sortKey="Veit, Michael" sort="Veit, Michael" uniqKey="Veit M" first="Michael" last="Veit">Michael Veit</name><name sortKey="Veit, Michael" sort="Veit, Michael" uniqKey="Veit M" first="Michael" last="Veit">Michael Veit</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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