Importance of SARS-CoV spike protein Trp-rich region in viral infectivity.
Identifieur interne : 003093 ( Main/Exploration ); précédent : 003092; suivant : 003094Importance of SARS-CoV spike protein Trp-rich region in viral infectivity.
Auteurs : Yanning Lu [Singapour] ; Tuan Ling Neo ; Ding Xiang Liu ; James P. TamSource :
- Biochemical and biophysical research communications [ 1090-2104 ] ; 2008.
Descripteurs français
- KwdFr :
- Animaux, Cellules Vero, Données de séquences moléculaires, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (), Glycoprotéines membranaires (génétique), Humains, Motifs d'acides aminés, Mutation, Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (génétique), Pénétration virale, Substitution d'acide aminé, Séquence conservée, Séquence d'acides aminés, Tryptophane (), Tryptophane (génétique), Virus du SRAS (génétique), Virus du SRAS (physiologie).
- MESH :
- génétique : Glycoprotéines membranaires, Protéines de l'enveloppe virale, Tryptophane, Virus du SRAS.
- physiologie : Virus du SRAS.
- Animaux, Cellules Vero, Données de séquences moléculaires, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Humains, Motifs d'acides aminés, Mutation, Protéines de l'enveloppe virale, Pénétration virale, Substitution d'acide aminé, Séquence conservée, Séquence d'acides aminés, Tryptophane.
English descriptors
- KwdEn :
- Amino Acid Motifs, Amino Acid Sequence, Amino Acid Substitution, Animals, Chlorocebus aethiops, Conserved Sequence, Humans, Membrane Glycoproteins (chemistry), Membrane Glycoproteins (genetics), Molecular Sequence Data, Mutation, SARS Virus (genetics), SARS Virus (physiology), Spike Glycoprotein, Coronavirus, Tryptophan (chemistry), Tryptophan (genetics), Vero Cells, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics), Virus Internalization.
- MESH :
- chemical , chemistry : Membrane Glycoproteins, Tryptophan, Viral Envelope Proteins.
- chemical , genetics : Membrane Glycoproteins, Tryptophan, Viral Envelope Proteins.
- genetics : SARS Virus.
- physiology : SARS Virus.
- Amino Acid Motifs, Amino Acid Sequence, Amino Acid Substitution, Animals, Chlorocebus aethiops, Conserved Sequence, Humans, Molecular Sequence Data, Mutation, Spike Glycoprotein, Coronavirus, Vero Cells, Virus Internalization.
Abstract
SARS-CoV entry is mediated by spike glycoprotein. During the viral and host cellular membrane fusion, HR1 and HR2 form 6-helix bundle, positioning the fusion peptide closely to the C-terminal region of ectodomain to drive apposition and subsequent membrane fusion. Connecting to the HR2 region is a Trp-rich region which is absolutely conserved in members of coronaviruses. To investigate the importance of Trp-rich region in SARS-CoV entry, we produced different mutated S proteins using Alanine scan strategy. SARS-CoV pseudotyped with mutated S protein was used to measure viral infectivity. To restore the aromaticity of Ala-mutants, we performed rescue experiments using phenylalanine substitutions. Our results show that individually substituted Ala-mutants substantially decrease infectivity by >90%, global Ala-mutants totally abrogated infectivity. In contrast, Phe-substituted mutants are able to restore 10-25% infectivity comparing to the wild-type. The results suggest that the Trp-rich region of S protein is essential for SARS-CoV infectivity.
DOI: 10.1016/j.bbrc.2008.04.044
PubMed: 18424264
Affiliations:
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Tam</name></author></analytic><series><title level="j">Biochemical and biophysical research communications</title><idno type="eISSN">1090-2104</idno><imprint><date when="2008" type="published">2008</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Motifs</term><term>Amino Acid Sequence</term><term>Amino Acid Substitution</term><term>Animals</term><term>Chlorocebus aethiops</term><term>Conserved Sequence</term><term>Humans</term><term>Membrane Glycoproteins (chemistry)</term><term>Membrane Glycoproteins (genetics)</term><term>Molecular Sequence Data</term><term>Mutation</term><term>SARS Virus (genetics)</term><term>SARS Virus (physiology)</term><term>Spike Glycoprotein, Coronavirus</term><term>Tryptophan (chemistry)</term><term>Tryptophan (genetics)</term><term>Vero Cells</term><term>Viral Envelope Proteins (chemistry)</term><term>Viral Envelope Proteins (genetics)</term><term>Virus Internalization</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Cellules Vero</term><term>Données de séquences moléculaires</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires ()</term><term>Glycoprotéines membranaires (génétique)</term><term>Humains</term><term>Motifs d'acides aminés</term><term>Mutation</term><term>Protéines de l'enveloppe virale ()</term><term>Protéines de l'enveloppe virale (génétique)</term><term>Pénétration virale</term><term>Substitution d'acide aminé</term><term>Séquence conservée</term><term>Séquence d'acides aminés</term><term>Tryptophane ()</term><term>Tryptophane (génétique)</term><term>Virus du SRAS (génétique)</term><term>Virus du SRAS (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Membrane Glycoproteins</term><term>Tryptophan</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Membrane Glycoproteins</term><term>Tryptophan</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glycoprotéines membranaires</term><term>Protéines de l'enveloppe virale</term><term>Tryptophane</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Motifs</term><term>Amino Acid Sequence</term><term>Amino Acid Substitution</term><term>Animals</term><term>Chlorocebus aethiops</term><term>Conserved Sequence</term><term>Humans</term><term>Molecular Sequence Data</term><term>Mutation</term><term>Spike Glycoprotein, Coronavirus</term><term>Vero Cells</term><term>Virus Internalization</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cellules Vero</term><term>Données de séquences moléculaires</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires</term><term>Humains</term><term>Motifs d'acides aminés</term><term>Mutation</term><term>Protéines de l'enveloppe virale</term><term>Pénétration virale</term><term>Substitution d'acide aminé</term><term>Séquence conservée</term><term>Séquence d'acides aminés</term><term>Tryptophane</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">SARS-CoV entry is mediated by spike glycoprotein. During the viral and host cellular membrane fusion, HR1 and HR2 form 6-helix bundle, positioning the fusion peptide closely to the C-terminal region of ectodomain to drive apposition and subsequent membrane fusion. Connecting to the HR2 region is a Trp-rich region which is absolutely conserved in members of coronaviruses. To investigate the importance of Trp-rich region in SARS-CoV entry, we produced different mutated S proteins using Alanine scan strategy. SARS-CoV pseudotyped with mutated S protein was used to measure viral infectivity. To restore the aromaticity of Ala-mutants, we performed rescue experiments using phenylalanine substitutions. Our results show that individually substituted Ala-mutants substantially decrease infectivity by >90%, global Ala-mutants totally abrogated infectivity. In contrast, Phe-substituted mutants are able to restore 10-25% infectivity comparing to the wild-type. The results suggest that the Trp-rich region of S protein is essential for SARS-CoV infectivity.</div></front></TEI><affiliations><list><country><li>Singapour</li></country></list><tree><noCountry><name sortKey="Liu, Ding Xiang" sort="Liu, Ding Xiang" uniqKey="Liu D" first="Ding Xiang" last="Liu">Ding Xiang Liu</name><name sortKey="Neo, Tuan Ling" sort="Neo, Tuan Ling" uniqKey="Neo T" first="Tuan Ling" last="Neo">Tuan Ling Neo</name><name sortKey="Tam, James P" sort="Tam, James P" uniqKey="Tam J" first="James P" last="Tam">James P. Tam</name></noCountry><country name="Singapour"><noRegion><name sortKey="Lu, Yanning" sort="Lu, Yanning" uniqKey="Lu Y" first="Yanning" last="Lu">Yanning Lu</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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