SrasV1, Main, Exploration, bibRecord, 004990

Folding of the SARS Coronavirus Spike Glycoprotein Immunological Fragment (SARS_S1B): Thermodynamic and Kinetic Investigation Correlating with Three-Dimensional Structural Modeling†

Identifieur interne : 004990 ( Main/Exploration ); précédent : 004989; suivant : 004991

Folding of the SARS Coronavirus Spike Glycoprotein Immunological Fragment (SARS_S1B): Thermodynamic and Kinetic Investigation Correlating with Three-Dimensional Structural Modeling†

Source :

Biochemistry [ 0006-2960 ] ; 2005.

RBID : ISTEX:1B3B857EECDEE18BE6E04BE4F62B875F5C8F7052

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence, Circular Dichroism, Computer Simulation, Guanidine (chemistry), Hot Temperature, Kinetics, Membrane Glycoproteins (chemistry), Membrane Glycoproteins (immunology), Models, Chemical, Models, Molecular, Molecular Sequence Data, Peptide Fragments (chemistry), Peptide Fragments (immunology), Protein Denaturation, Protein Folding, Protein Structure, Secondary, SARS Virus (chemistry), Spectrometry, Fluorescence, Spike Glycoprotein, Coronavirus, Structural Homology, Protein, Thermodynamics, Tryptophan (chemistry), Viral Envelope Proteins (chemistry), Viral Envelope Proteins (immunology).
MESH :
- chemical , chemistry : Guanidine, Membrane Glycoproteins, Peptide Fragments, Tryptophan, Viral Envelope Proteins.
- chemical , immunology : Membrane Glycoproteins, Peptide Fragments, Viral Envelope Proteins.
- chemistry : SARS Virus.
- Amino Acid Sequence, Circular Dichroism, Computer Simulation, Hot Temperature, Kinetics, Models, Chemical, Models, Molecular, Molecular Sequence Data, Protein Denaturation, Protein Folding, Protein Structure, Secondary, Spectrometry, Fluorescence, Spike Glycoprotein, Coronavirus, Structural Homology, Protein, Thermodynamics.

Abstract

Spike glycoprotein of SARS coronavirus (S protein) plays a pivotal role in SARS coronavirus (SARS_CoV) infection. The immunological fragment of the S protein (Ala251−His641, SARS_S1b) is believed to be essential for SARS_CoV entering the host cell through S protein−ACE-2 interaction. We have quantitatively characterized the thermally induced and GuHCl-induced unfolding features of SARS_S1b using circular dichroism (CD), tryptophan fluorescence, and stopped-flow spectral techniques. For the thermally induced unfolding at pH 7.4, the apparent activation energy (Eapp) and transition midpoint temperature (Tm) were determined to be 16.3 ± 0.2 kcal/mol and 52.5 ± 0.4 °C, respectively. The CD spectra are not dependent on temperature, suggesting that the secondary structure of SARS_S1b has a relatively high thermal stability. GuHCl strongly affected SARS_S1b structure. Both the CD and fluorescent spectra resulted in consistent values of the transition middle concentration of the denaturant (Cm, ranging from 2.30 to 2.45 M) and the standard free energy change (ΔG°, ranging from 2.1 to 2.5 kcal/mol) for the SARS_S1b unfolding reaction. Moreover, the kinetic features of the chemical unfolding and refolding of SARS_S1b were also characterized using a stopped-flow CD spectral technique. The obvious unfolding reaction rates and relaxation times were determined at various GuHCl concentrations, and the Cm value was obtained, which is very close to the data that resulted from CD and fluorescent spectral determinations. Secondary and three-dimensional structural predictions by homology modeling indicated that SARS_S1b folded as a globular-like structure by β-sheets and loops; two of the four tryptophans are located on the protein surface, which is in agreement with the tryptophan fluorescence result. The three-dimensional model was also used to explain the recently published experimental results of S1−ACE-2 binding and immunizations.

Url:

https://api.istex.fr/ark:/67375/TPS-NZ5V5XNP-C/fulltext.pdf

DOI: 10.1021/bi0482396

Affiliations:

République populaire de Chine

Le document en format XML

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<term>Circular Dichroism</term>
<term>Computer Simulation</term>
<term>Guanidine (chemistry)</term>
<term>Hot Temperature</term>
<term>Kinetics</term>
<term>Membrane Glycoproteins (chemistry)</term>
<term>Membrane Glycoproteins (immunology)</term>
<term>Models, Chemical</term>
<term>Models, Molecular</term>
<term>Molecular Sequence Data</term>
<term>Peptide Fragments (chemistry)</term>
<term>Peptide Fragments (immunology)</term>
<term>Protein Denaturation</term>
<term>Protein Folding</term>
<term>Protein Structure, Secondary</term>
<term>SARS Virus (chemistry)</term>
<term>Spectrometry, Fluorescence</term>
<term>Spike Glycoprotein, Coronavirus</term>
<term>Structural Homology, Protein</term>
<term>Thermodynamics</term>
<term>Tryptophan (chemistry)</term>
<term>Viral Envelope Proteins (chemistry)</term>
<term>Viral Envelope Proteins (immunology)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Cinétique</term>
<term>Dichroïsme circulaire</term>
<term>Données de séquences moléculaires</term>
<term>Dénaturation des protéines</term>
<term>Fragments peptidiques ()</term>
<term>Fragments peptidiques (immunologie)</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires ()</term>
<term>Glycoprotéines membranaires (immunologie)</term>
<term>Guanidine ()</term>
<term>Modèles chimiques</term>
<term>Modèles moléculaires</term>
<term>Pliage des protéines</term>
<term>Protéines de l'enveloppe virale ()</term>
<term>Protéines de l'enveloppe virale (immunologie)</term>
<term>Similitude structurale de protéines</term>
<term>Simulation numérique</term>
<term>Spectrométrie de fluorescence</term>
<term>Structure secondaire des protéines</term>
<term>Séquence d'acides aminés</term>
<term>Température élevée</term>
<term>Thermodynamique</term>
<term>Tryptophane ()</term>
<term>Virus du SRAS ()</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Guanidine</term>
<term>Membrane Glycoproteins</term>
<term>Peptide Fragments</term>
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<term>Viral Envelope Proteins</term>
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<term>Viral Envelope Proteins</term>
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</keywords>
<keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Fragments peptidiques</term>
<term>Glycoprotéines membranaires</term>
<term>Protéines de l'enveloppe virale</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Circular Dichroism</term>
<term>Computer Simulation</term>
<term>Hot Temperature</term>
<term>Kinetics</term>
<term>Models, Chemical</term>
<term>Models, Molecular</term>
<term>Molecular Sequence Data</term>
<term>Protein Denaturation</term>
<term>Protein Folding</term>
<term>Protein Structure, Secondary</term>
<term>Spectrometry, Fluorescence</term>
<term>Spike Glycoprotein, Coronavirus</term>
<term>Structural Homology, Protein</term>
<term>Thermodynamics</term>
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<keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term>
<term>Dichroïsme circulaire</term>
<term>Données de séquences moléculaires</term>
<term>Dénaturation des protéines</term>
<term>Fragments peptidiques</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires</term>
<term>Guanidine</term>
<term>Modèles chimiques</term>
<term>Modèles moléculaires</term>
<term>Pliage des protéines</term>
<term>Protéines de l'enveloppe virale</term>
<term>Similitude structurale de protéines</term>
<term>Simulation numérique</term>
<term>Spectrométrie de fluorescence</term>
<term>Structure secondaire des protéines</term>
<term>Séquence d'acides aminés</term>
<term>Température élevée</term>
<term>Thermodynamique</term>
<term>Tryptophane</term>
<term>Virus du SRAS</term>
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<front><div type="abstract">Spike glycoprotein of SARS coronavirus (S protein) plays a pivotal role in SARS coronavirus (SARS_CoV) infection. The immunological fragment of the S protein (Ala251−His641, SARS_S1b) is believed to be essential for SARS_CoV entering the host cell through S protein−ACE-2 interaction. We have quantitatively characterized the thermally induced and GuHCl-induced unfolding features of SARS_S1b using circular dichroism (CD), tryptophan fluorescence, and stopped-flow spectral techniques. For the thermally induced unfolding at pH 7.4, the apparent activation energy (Eapp) and transition midpoint temperature (Tm) were determined to be 16.3 ± 0.2 kcal/mol and 52.5 ± 0.4 °C, respectively. The CD spectra are not dependent on temperature, suggesting that the secondary structure of SARS_S1b has a relatively high thermal stability. GuHCl strongly affected SARS_S1b structure. Both the CD and fluorescent spectra resulted in consistent values of the transition middle concentration of the denaturant (Cm, ranging from 2.30 to 2.45 M) and the standard free energy change (ΔG°, ranging from 2.1 to 2.5 kcal/mol) for the SARS_S1b unfolding reaction. Moreover, the kinetic features of the chemical unfolding and refolding of SARS_S1b were also characterized using a stopped-flow CD spectral technique. The obvious unfolding reaction rates and relaxation times were determined at various GuHCl concentrations, and the Cm value was obtained, which is very close to the data that resulted from CD and fluorescent spectral determinations. Secondary and three-dimensional structural predictions by homology modeling indicated that SARS_S1b folded as a globular-like structure by β-sheets and loops; two of the four tryptophans are located on the protein surface, which is in agreement with the tryptophan fluorescence result. The three-dimensional model was also used to explain the recently published experimental results of S1−ACE-2 binding and immunizations.</div>
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<tree><country name="République populaire de Chine"><noRegion><name sortKey="Yu, Changying" sort="Yu, Changying" uniqKey="Yu C" first="Changying" last="Yu">Changying Yu</name>
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<name sortKey="Yu, Hao" sort="Yu, Hao" uniqKey="Yu H" first="Hao" last="Yu">Hao Yu</name>
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   |flux=    Main
   |étape=   Exploration
   |type=    RBID
   |clé=     ISTEX:1B3B857EECDEE18BE6E04BE4F62B875F5C8F7052
   |texte=   Folding of the SARS Coronavirus Spike Glycoprotein Immunological Fragment (SARS_S1B):  Thermodynamic and Kinetic Investigation Correlating with Three-Dimensional Structural Modeling†
}}

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Folding of the SARS Coronavirus Spike Glycoprotein Immunological Fragment (SARS_S1B): Thermodynamic and Kinetic Investigation Correlating with Three-Dimensional Structural Modeling†

Folding of the SARS Coronavirus Spike Glycoprotein Immunological Fragment (SARS_S1B): Thermodynamic and Kinetic Investigation Correlating with Three-Dimensional Structural Modeling†

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