Identification of two critical amino acid residues of the severe acute respiratory syndrome coronavirus spike protein for its variation in zoonotic tropism transition via a double substitution strategy.
Identifieur interne : 004803 ( Main/Curation ); précédent : 004802; suivant : 004804Identification of two critical amino acid residues of the severe acute respiratory syndrome coronavirus spike protein for its variation in zoonotic tropism transition via a double substitution strategy.
Auteurs : Xiu-Xia Qu [République populaire de Chine] ; Pei Hao ; Xi-Jun Song ; Si-Ming Jiang ; Yan-Xia Liu ; Pei-Gang Wang ; Xi Rao ; Huai-Dong Song ; Sheng-Yue Wang ; Yu Zuo ; Ai-Hua Zheng ; Min Luo ; Hua-Lin Wang ; Fei Deng ; Han-Zhong Wang ; Zhi-Hong Hu ; Ming-Xiao Ding ; Guo-Ping Zhao ; Hong-Kui DengSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2005.
Descripteurs français
- KwdFr :
- Carboxypeptidases (métabolisme), Données de séquences moléculaires, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (), Glycoprotéines membranaires (physiologie), Humains, Peptidyl-Dipeptidase A, Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (physiologie), Relation structure-activité, Sites de fixation, Substitution d'acide aminé, Syndrome respiratoire aigu sévère (transmission), Séquence d'acides aminés, Tropisme, Virus du SRAS (), Virus du SRAS (pathogénicité), Zoonoses.
- MESH :
- métabolisme : Carboxypeptidases.
- pathogénicité : Virus du SRAS.
- physiologie : Glycoprotéines membranaires, Protéines de l'enveloppe virale.
- Données de séquences moléculaires, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Humains, Peptidyl-Dipeptidase A, Protéines de l'enveloppe virale, Relation structure-activité, Sites de fixation, Substitution d'acide aminé, Syndrome respiratoire aigu sévère, Séquence d'acides aminés, Tropisme, Virus du SRAS, Zoonoses.
English descriptors
- KwdEn :
- Amino Acid Sequence, Amino Acid Substitution, Binding Sites, Carboxypeptidases (metabolism), Humans, Membrane Glycoproteins (chemistry), Membrane Glycoproteins (physiology), Molecular Sequence Data, Peptidyl-Dipeptidase A, SARS Virus (chemistry), SARS Virus (pathogenicity), Severe Acute Respiratory Syndrome (transmission), Spike Glycoprotein, Coronavirus, Structure-Activity Relationship, Tropism, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (physiology), Zoonoses.
- MESH :
- chemical , chemistry : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , metabolism : Carboxypeptidases.
- chemical , physiology : Membrane Glycoproteins, Viral Envelope Proteins.
- chemistry : SARS Virus.
- pathogenicity : SARS Virus.
- transmission : Severe Acute Respiratory Syndrome.
- Amino Acid Sequence, Amino Acid Substitution, Binding Sites, Humans, Molecular Sequence Data, Peptidyl-Dipeptidase A, Spike Glycoprotein, Coronavirus, Structure-Activity Relationship, Tropism, Zoonoses.
Abstract
Severe acute respiratory syndrome coronavirus (SARS-CoV) is a recently identified human coronavirus. The extremely high homology of the viral genomic sequences between the viruses isolated from human (huSARS-CoV) and those of palm civet origin (pcSARS-CoV) suggested possible palm civet-to-human transmission. Genetic analysis revealed that the spike (S) protein of pcSARS-CoV and huSARS-CoV was subjected to the strongest positive selection pressure during transmission, and there were six amino acid residues within the receptor-binding domain of the S protein being potentially important for SARS progression and tropism. Using the single-round infection assay, we found that a two-amino acid substitution (N479K/T487S) of a huSARS-CoV for those of pcSARS-CoV almost abolished its infection of human cells expressing the SARS-CoV receptor ACE2 but no effect upon the infection of mouse ACE2 cells. Although single substitution of these two residues had no effects on the infectivity of huSARS-CoV, these recombinant S proteins bound to human ACE2 with different levels of reduced affinity, and the two-amino acid-substituted S protein showed extremely low affinity. On the contrary, substitution of these two amino acid residues of pcSARS-CoV for those of huSRAS-CoV made pcSARS-CoV capable of infecting human ACE2-expressing cells. These results suggest that amino acid residues at position 479 and 487 of the S protein are important determinants for SARS-CoV tropism and animal-to-human transmission.
DOI: 10.1074/jbc.M500662200
PubMed: 15980414
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pubmed:15980414Le document en format XML
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<term>Amino Acid Substitution</term>
<term>Binding Sites</term>
<term>Carboxypeptidases (metabolism)</term>
<term>Humans</term>
<term>Membrane Glycoproteins (chemistry)</term>
<term>Membrane Glycoproteins (physiology)</term>
<term>Molecular Sequence Data</term>
<term>Peptidyl-Dipeptidase A</term>
<term>SARS Virus (chemistry)</term>
<term>SARS Virus (pathogenicity)</term>
<term>Severe Acute Respiratory Syndrome (transmission)</term>
<term>Spike Glycoprotein, Coronavirus</term>
<term>Structure-Activity Relationship</term>
<term>Tropism</term>
<term>Viral Envelope Proteins (chemistry)</term>
<term>Viral Envelope Proteins (physiology)</term>
<term>Zoonoses</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Carboxypeptidases (métabolisme)</term>
<term>Données de séquences moléculaires</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires ()</term>
<term>Glycoprotéines membranaires (physiologie)</term>
<term>Humains</term>
<term>Peptidyl-Dipeptidase A</term>
<term>Protéines de l'enveloppe virale ()</term>
<term>Protéines de l'enveloppe virale (physiologie)</term>
<term>Relation structure-activité</term>
<term>Sites de fixation</term>
<term>Substitution d'acide aminé</term>
<term>Syndrome respiratoire aigu sévère (transmission)</term>
<term>Séquence d'acides aminés</term>
<term>Tropisme</term>
<term>Virus du SRAS ()</term>
<term>Virus du SRAS (pathogénicité)</term>
<term>Zoonoses</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Membrane Glycoproteins</term>
<term>Viral Envelope Proteins</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Carboxypeptidases</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Membrane Glycoproteins</term>
<term>Viral Envelope Proteins</term>
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<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>SARS Virus</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Carboxypeptidases</term>
</keywords>
<keywords scheme="MESH" qualifier="pathogenicity" xml:lang="en"><term>SARS Virus</term>
</keywords>
<keywords scheme="MESH" qualifier="pathogénicité" xml:lang="fr"><term>Virus du SRAS</term>
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<keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Glycoprotéines membranaires</term>
<term>Protéines de l'enveloppe virale</term>
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<keywords scheme="MESH" qualifier="transmission" xml:lang="en"><term>Severe Acute Respiratory Syndrome</term>
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<term>Amino Acid Substitution</term>
<term>Binding Sites</term>
<term>Humans</term>
<term>Molecular Sequence Data</term>
<term>Peptidyl-Dipeptidase A</term>
<term>Spike Glycoprotein, Coronavirus</term>
<term>Structure-Activity Relationship</term>
<term>Tropism</term>
<term>Zoonoses</term>
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<term>Glycoprotéines membranaires</term>
<term>Humains</term>
<term>Peptidyl-Dipeptidase A</term>
<term>Protéines de l'enveloppe virale</term>
<term>Relation structure-activité</term>
<term>Sites de fixation</term>
<term>Substitution d'acide aminé</term>
<term>Syndrome respiratoire aigu sévère</term>
<term>Séquence d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">Severe acute respiratory syndrome coronavirus (SARS-CoV) is a recently identified human coronavirus. The extremely high homology of the viral genomic sequences between the viruses isolated from human (huSARS-CoV) and those of palm civet origin (pcSARS-CoV) suggested possible palm civet-to-human transmission. Genetic analysis revealed that the spike (S) protein of pcSARS-CoV and huSARS-CoV was subjected to the strongest positive selection pressure during transmission, and there were six amino acid residues within the receptor-binding domain of the S protein being potentially important for SARS progression and tropism. Using the single-round infection assay, we found that a two-amino acid substitution (N479K/T487S) of a huSARS-CoV for those of pcSARS-CoV almost abolished its infection of human cells expressing the SARS-CoV receptor ACE2 but no effect upon the infection of mouse ACE2 cells. Although single substitution of these two residues had no effects on the infectivity of huSARS-CoV, these recombinant S proteins bound to human ACE2 with different levels of reduced affinity, and the two-amino acid-substituted S protein showed extremely low affinity. On the contrary, substitution of these two amino acid residues of pcSARS-CoV for those of huSRAS-CoV made pcSARS-CoV capable of infecting human ACE2-expressing cells. These results suggest that amino acid residues at position 479 and 487 of the S protein are important determinants for SARS-CoV tropism and animal-to-human transmission.</div>
</front>
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