NMR structures and localization of the potential fusion peptides and the pre-transmembrane region of SARS-CoV: Implications in membrane fusion.
Identifieur interne : 001276 ( Main/Exploration ); précédent : 001275; suivant : 001277NMR structures and localization of the potential fusion peptides and the pre-transmembrane region of SARS-CoV: Implications in membrane fusion.
Auteurs : Mukesh Mahajan [Singapour] ; Surajit Bhattacharjya [Singapour]Source :
- Biochimica et biophysica acta [ 0006-3002 ] ; 2015.
Descripteurs français
- KwdFr :
- Données de séquences moléculaires, Détergents (), Fusion membranaire (physiologie), Humains, Micelles, Modèles moléculaires, Motifs et domaines d'intéraction protéique, Protéines de fusion virale (), Protéines de fusion virale (synthèse chimique), Résonance magnétique nucléaire biomoléculaire, Structure secondaire des protéines, Séquence d'acides aminés, Thermodynamique, Virus du SRAS ().
- MESH :
- physiologie : Fusion membranaire.
- synthèse chimique : Protéines de fusion virale.
- Données de séquences moléculaires, Détergents, Humains, Micelles, Modèles moléculaires, Motifs et domaines d'intéraction protéique, Protéines de fusion virale, Résonance magnétique nucléaire biomoléculaire, Structure secondaire des protéines, Séquence d'acides aminés, Thermodynamique, Virus du SRAS.
English descriptors
- KwdEn :
- Amino Acid Sequence, Detergents (chemistry), Humans, Membrane Fusion (physiology), Micelles, Models, Molecular, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Protein Interaction Domains and Motifs, Protein Structure, Secondary, SARS Virus (chemistry), Thermodynamics, Viral Fusion Proteins (chemical synthesis), Viral Fusion Proteins (chemistry).
- MESH :
- chemical , chemical synthesis : Viral Fusion Proteins.
- chemical , chemistry : Detergents, Viral Fusion Proteins.
- chemistry : SARS Virus.
- physiology : Membrane Fusion.
- Amino Acid Sequence, Humans, Micelles, Models, Molecular, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Protein Interaction Domains and Motifs, Protein Structure, Secondary, Thermodynamics.
Abstract
Severe acute respiratory syndrome-associated coronavirus (SARS-CoV) poses a serious public health hazard. The S2 subunit of the S glycoprotein of SARS-CoV carries out fusion between the virus and the host cells. However, the exact mechanism of the cell fusion process is not well understood. Current model suggests that a conformational transition, upon receptor recognition, of the two heptad core regions of S2 may expose the hydrophobic fusogenic peptide or fusion peptide for membrane insertion. Three regions of the S2 subunit have been proposed to be involved in cell-cell fusion. The N-terminal fusion peptide (FP, residues 770-788), an internal fusion peptide (IFP, residues 873-888) and the pre-transmembrane region (PTM, residues 1185-1202) demonstrated interactions with model lipid membranes and potentially involved in the fusion process. Here, we have determined atomic resolution structures of these three peptides in DPC detergent micelles by solution NMR. FP assumes α-helical conformation with significant distortion at the central Gly residues; enabling a close packing among sidechains of aromatic residues including W, Y and F. The 3-D structure of PMT is characterized by a helix-loop-helix with extensive aromatic interactions within the helices. IFP adopts a rather straight α-helical conformation defined by packing among sidechains of aromatic and aliphatic residues. Paramagnetic spin labeled NMR has demonstrated surface localization of PMT whereas FP and IFP inserted into the micelles. Collectively, data presented in this study will aid in understanding fusion mechanism of SARS-CoV.
DOI: 10.1016/j.bbamem.2014.11.025
PubMed: 25475644
Affiliations:
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Electronic address: surajit@ntu.edu.sg.</nlm:affiliation><country xml:lang="fr">Singapour</country><wicri:regionArea>School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551</wicri:regionArea><wicri:noRegion>Singapore 637551</wicri:noRegion></affiliation></author></analytic><series><title level="j">Biochimica et biophysica acta</title><idno type="ISSN">0006-3002</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Detergents (chemistry)</term><term>Humans</term><term>Membrane Fusion (physiology)</term><term>Micelles</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Nuclear Magnetic Resonance, Biomolecular</term><term>Protein Interaction Domains and Motifs</term><term>Protein Structure, Secondary</term><term>SARS Virus (chemistry)</term><term>Thermodynamics</term><term>Viral Fusion Proteins (chemical synthesis)</term><term>Viral Fusion Proteins (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Données de séquences moléculaires</term><term>Détergents ()</term><term>Fusion membranaire (physiologie)</term><term>Humains</term><term>Micelles</term><term>Modèles moléculaires</term><term>Motifs et domaines d'intéraction protéique</term><term>Protéines de fusion virale ()</term><term>Protéines de fusion virale (synthèse chimique)</term><term>Résonance magnétique nucléaire biomoléculaire</term><term>Structure secondaire des protéines</term><term>Séquence d'acides aminés</term><term>Thermodynamique</term><term>Virus du SRAS ()</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemical synthesis" xml:lang="en"><term>Viral Fusion Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Detergents</term><term>Viral Fusion Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Fusion membranaire</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Membrane Fusion</term></keywords><keywords scheme="MESH" qualifier="synthèse chimique" xml:lang="fr"><term>Protéines de fusion virale</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Humans</term><term>Micelles</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Nuclear Magnetic Resonance, Biomolecular</term><term>Protein Interaction Domains and Motifs</term><term>Protein Structure, Secondary</term><term>Thermodynamics</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Données de séquences moléculaires</term><term>Détergents</term><term>Humains</term><term>Micelles</term><term>Modèles moléculaires</term><term>Motifs et domaines d'intéraction protéique</term><term>Protéines de fusion virale</term><term>Résonance magnétique nucléaire biomoléculaire</term><term>Structure secondaire des protéines</term><term>Séquence d'acides aminés</term><term>Thermodynamique</term><term>Virus du SRAS</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Severe acute respiratory syndrome-associated coronavirus (SARS-CoV) poses a serious public health hazard. The S2 subunit of the S glycoprotein of SARS-CoV carries out fusion between the virus and the host cells. However, the exact mechanism of the cell fusion process is not well understood. Current model suggests that a conformational transition, upon receptor recognition, of the two heptad core regions of S2 may expose the hydrophobic fusogenic peptide or fusion peptide for membrane insertion. Three regions of the S2 subunit have been proposed to be involved in cell-cell fusion. The N-terminal fusion peptide (FP, residues 770-788), an internal fusion peptide (IFP, residues 873-888) and the pre-transmembrane region (PTM, residues 1185-1202) demonstrated interactions with model lipid membranes and potentially involved in the fusion process. Here, we have determined atomic resolution structures of these three peptides in DPC detergent micelles by solution NMR. FP assumes α-helical conformation with significant distortion at the central Gly residues; enabling a close packing among sidechains of aromatic residues including W, Y and F. The 3-D structure of PMT is characterized by a helix-loop-helix with extensive aromatic interactions within the helices. IFP adopts a rather straight α-helical conformation defined by packing among sidechains of aromatic and aliphatic residues. Paramagnetic spin labeled NMR has demonstrated surface localization of PMT whereas FP and IFP inserted into the micelles. Collectively, data presented in this study will aid in understanding fusion mechanism of SARS-CoV. </div></front></TEI><affiliations><list><country><li>Singapour</li></country></list><tree><country name="Singapour"><noRegion><name sortKey="Mahajan, Mukesh" sort="Mahajan, Mukesh" uniqKey="Mahajan M" first="Mukesh" last="Mahajan">Mukesh Mahajan</name></noRegion><name sortKey="Bhattacharjya, Surajit" sort="Bhattacharjya, Surajit" uniqKey="Bhattacharjya S" first="Surajit" last="Bhattacharjya">Surajit Bhattacharjya</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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