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Structural and biochemical investigation of heptad repeat derived peptides of human SARS corona virus (hSARS-CoV) spike protein.

Identifieur interne : 001580 ( Main/Exploration ); précédent : 001579; suivant : 001581

Structural and biochemical investigation of heptad repeat derived peptides of human SARS corona virus (hSARS-CoV) spike protein.

Auteurs : Sarmistha Basak [Canada] ; Xiaolei Hao ; Andrew Chen ; Michel Chrétien ; Ajoy Basak

Source :

RBID : pubmed:18991761

Descripteurs français

English descriptors

Abstract

hSARS-CoV is the causative agent for SARS infection. Its spike glycoprotein (S) is processed by host furin enzyme to produce S1 and S2 fragments, the latter being crucial for fusion with the host membrane. This takes place via formation of a coiled coil 6-helix bundle involving N and C-terminal heptad repeat domains (HR-N and HR-C) of S2. Several fluorescent and non-fluorescent peptides from these domains were synthesized to examine their interactions by circular dichroism, thermal denaturation, native-page, mass spectrometry and fluorescence spectroscopy studies. Data revealed that HR-C domains (1153-1189), (1153-1172) and (1164-1184) all exhibit potent binding interactions with HR-N(892-931) domain. These peptides may find useful therapeutic applications in SARS intervention.

DOI: 10.2174/092986608785849173
PubMed: 18991761


Affiliations:


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Le document en format XML

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<term>Amino Acid Sequence</term>
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<term>Circular Dichroism</term>
<term>Electrophoresis, Polyacrylamide Gel</term>
<term>Mass Spectrometry</term>
<term>Membrane Fusion Proteins</term>
<term>Membrane Glycoproteins (chemistry)</term>
<term>Membrane Glycoproteins (genetics)</term>
<term>Membrane Glycoproteins (metabolism)</term>
<term>Peptides (chemical synthesis)</term>
<term>Peptides (chemistry)</term>
<term>Peptides (metabolism)</term>
<term>Protein Binding</term>
<term>Protein Denaturation</term>
<term>Protein Structure, Secondary</term>
<term>Protein Structure, Tertiary</term>
<term>SARS Virus (chemistry)</term>
<term>SARS Virus (metabolism)</term>
<term>Sequence Analysis, Protein</term>
<term>Spectrometry, Fluorescence</term>
<term>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</term>
<term>Spike Glycoprotein, Coronavirus</term>
<term>Viral Envelope Proteins (chemistry)</term>
<term>Viral Envelope Proteins (genetics)</term>
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<term>Analyse de séquence de protéine</term>
<term>Chromatographie en phase liquide à haute performance</term>
<term>Dichroïsme circulaire</term>
<term>Dénaturation des protéines</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires ()</term>
<term>Glycoprotéines membranaires (génétique)</term>
<term>Glycoprotéines membranaires (métabolisme)</term>
<term>Liaison aux protéines</term>
<term>Peptides ()</term>
<term>Peptides (métabolisme)</term>
<term>Peptides (synthèse chimique)</term>
<term>Protéines de fusion membranaire</term>
<term>Protéines de l'enveloppe virale ()</term>
<term>Protéines de l'enveloppe virale (génétique)</term>
<term>Protéines de l'enveloppe virale (métabolisme)</term>
<term>Spectrométrie de fluorescence</term>
<term>Spectrométrie de masse</term>
<term>Spectrométrie de masse MALDI</term>
<term>Structure secondaire des protéines</term>
<term>Structure tertiaire des protéines</term>
<term>Séquence d'acides aminés</term>
<term>Virus du SRAS ()</term>
<term>Virus du SRAS (métabolisme)</term>
<term>Électrophorèse sur gel de polyacrylamide</term>
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<term>Peptides</term>
<term>Viral Envelope Proteins</term>
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<term>Chromatography, High Pressure Liquid</term>
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<term>Protein Structure, Tertiary</term>
<term>Sequence Analysis, Protein</term>
<term>Spectrometry, Fluorescence</term>
<term>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</term>
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<term>Analyse de séquence de protéine</term>
<term>Chromatographie en phase liquide à haute performance</term>
<term>Dichroïsme circulaire</term>
<term>Dénaturation des protéines</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires</term>
<term>Liaison aux protéines</term>
<term>Peptides</term>
<term>Protéines de fusion membranaire</term>
<term>Protéines de l'enveloppe virale</term>
<term>Spectrométrie de fluorescence</term>
<term>Spectrométrie de masse</term>
<term>Spectrométrie de masse MALDI</term>
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<term>Structure tertiaire des protéines</term>
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<div type="abstract" xml:lang="en">hSARS-CoV is the causative agent for SARS infection. Its spike glycoprotein (S) is processed by host furin enzyme to produce S1 and S2 fragments, the latter being crucial for fusion with the host membrane. This takes place via formation of a coiled coil 6-helix bundle involving N and C-terminal heptad repeat domains (HR-N and HR-C) of S2. Several fluorescent and non-fluorescent peptides from these domains were synthesized to examine their interactions by circular dichroism, thermal denaturation, native-page, mass spectrometry and fluorescence spectroscopy studies. Data revealed that HR-C domains (1153-1189), (1153-1172) and (1164-1184) all exhibit potent binding interactions with HR-N(892-931) domain. These peptides may find useful therapeutic applications in SARS intervention.</div>
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