A single amino acid substitution (R441A) in the receptor-binding domain of SARS coronavirus spike protein disrupts the antigenic structure and binding activity
Identifieur interne : 001457 ( Ncbi/Curation ); précédent : 001456; suivant : 001458A single amino acid substitution (R441A) in the receptor-binding domain of SARS coronavirus spike protein disrupts the antigenic structure and binding activity
Auteurs : Yuxian He ; Jingjing Li ; Shibo JiangSource :
- Biochemical and Biophysical Research Communications [ 0006-291X ] ; 2006.
Descripteurs français
- KwdFr :
- Animaux, Anticorps monoclonaux (immunologie), Antigènes viraux (génétique), Antigènes viraux (immunologie), Arginine (génétique), Arginine (immunologie), Femelle, Fragments Fc des immunoglobulines (génétique), Fragments Fc des immunoglobulines (immunologie), Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (génétique), Glycoprotéines membranaires (immunologie), Glycoprotéines membranaires (métabolisme), Lapins, Mutation ponctuelle, Peptidyl-Dipeptidase A (métabolisme), Protéines de fusion recombinantes (), Protéines de fusion recombinantes (génétique), Protéines de fusion recombinantes (immunologie), Protéines de l'enveloppe virale (génétique), Protéines de l'enveloppe virale (immunologie), Protéines de l'enveloppe virale (métabolisme), Souris, Souris de lignée BALB C, Structure tertiaire des protéines (génétique), Substitution d'acide aminé (immunologie), Vaccins antiviraux (génétique), Vaccins antiviraux (immunologie).
- MESH :
- génétique : Antigènes viraux, Arginine, Fragments Fc des immunoglobulines, Glycoprotéines membranaires, Protéines de fusion recombinantes, Protéines de l'enveloppe virale, Structure tertiaire des protéines, Vaccins antiviraux.
- immunologie : Anticorps monoclonaux, Antigènes viraux, Arginine, Fragments Fc des immunoglobulines, Glycoprotéines membranaires, Protéines de fusion recombinantes, Protéines de l'enveloppe virale, Substitution d'acide aminé, Vaccins antiviraux.
- métabolisme : Glycoprotéines membranaires, Peptidyl-Dipeptidase A, Protéines de l'enveloppe virale.
- Animaux, Femelle, Glycoprotéine de spicule des coronavirus, Lapins, Mutation ponctuelle, Protéines de fusion recombinantes, Souris, Souris de lignée BALB C.
English descriptors
- KwdEn :
- Amino Acid Substitution (immunology), Animals, Antibodies, Monoclonal (immunology), Antigens, Viral (genetics), Antigens, Viral (immunology), Arginine (genetics), Arginine (immunology), Female, Immunoglobulin Fc Fragments (genetics), Immunoglobulin Fc Fragments (immunology), Membrane Glycoproteins (genetics), Membrane Glycoproteins (immunology), Membrane Glycoproteins (metabolism), Mice, Mice, Inbred BALB C, Peptidyl-Dipeptidase A (metabolism), Point Mutation, Protein Structure, Tertiary (genetics), Rabbits, Recombinant Fusion Proteins (chemistry), Recombinant Fusion Proteins (genetics), Recombinant Fusion Proteins (immunology), Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (genetics), Viral Envelope Proteins (immunology), Viral Envelope Proteins (metabolism), Viral Vaccines (genetics), Viral Vaccines (immunology).
- MESH :
- chemical , chemistry : Recombinant Fusion Proteins.
- chemical , genetics : Antigens, Viral, Arginine, Immunoglobulin Fc Fragments, Membrane Glycoproteins, Recombinant Fusion Proteins, Viral Envelope Proteins, Viral Vaccines.
- chemical , immunology : Antibodies, Monoclonal, Antigens, Viral, Arginine, Immunoglobulin Fc Fragments, Membrane Glycoproteins, Recombinant Fusion Proteins, Viral Envelope Proteins, Viral Vaccines.
- genetics : Protein Structure, Tertiary.
- immunology : Amino Acid Substitution.
- chemical , metabolism : Membrane Glycoproteins, Peptidyl-Dipeptidase A, Viral Envelope Proteins.
- Animals, Female, Mice, Mice, Inbred BALB C, Point Mutation, Rabbits, Spike Glycoprotein, Coronavirus.
Abstract
The spike (S) protein of severe acute respiratory syndrome coronavirus (SARS-CoV) has two major functions: interacting with the receptor to mediate virus entry and inducing protective immunity. Coincidently, the receptor-binding domain (RBD, residues 318–510) of SAR-CoV S protein is a major antigenic site to induce neutralizing antibodies. Here, we used RBD-Fc, a fusion protein containing the RBD and human IgG1 Fc, as a model in the studies and found that a single amino acid substitution in the RBD (R441A) could abolish the immunogenicity of RBD to induce neutralizing antibodies in immunized mice and rabbits. With a panel of anti-RBD mAbs as probes, we observed that R441A substitution was able to disrupt the majority of neutralizing epitopes in the RBD, suggesting that this residue is critical for the antigenic structure responsible for inducing protective immune responses. We also demonstrated that the RBD-Fc bearing R441A mutation could not bind to soluble and cell-associated angiotensin-converting enzyme 2 (ACE2), the functional receptor for SARS-CoV and failed to block S protein-mediated pseudovirus entry, indicating that this point mutation also disrupted the receptor-binding motif (RBM) in the RBD. Taken together, these data provide direct evidence to show that a single amino acid residue at key position in the RBD can determine the major function of SARS-CoV S protein and imply for designing SARS vaccines and therapeutics.
Url:
DOI: 10.1016/j.bbrc.2006.03.139
PubMed: 16615996
PubMed Central: 7092835
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PMC:7092835Le document en format XML
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xml:lang="en"><term>Amino Acid Substitution (immunology)</term><term>Animals</term><term>Antibodies, Monoclonal (immunology)</term><term>Antigens, Viral (genetics)</term><term>Antigens, Viral (immunology)</term><term>Arginine (genetics)</term><term>Arginine (immunology)</term><term>Female</term><term>Immunoglobulin Fc Fragments (genetics)</term><term>Immunoglobulin Fc Fragments (immunology)</term><term>Membrane Glycoproteins (genetics)</term><term>Membrane Glycoproteins (immunology)</term><term>Membrane Glycoproteins (metabolism)</term><term>Mice</term><term>Mice, Inbred BALB C</term><term>Peptidyl-Dipeptidase A (metabolism)</term><term>Point Mutation</term><term>Protein Structure, Tertiary (genetics)</term><term>Rabbits</term><term>Recombinant Fusion Proteins (chemistry)</term><term>Recombinant Fusion Proteins (genetics)</term><term>Recombinant Fusion Proteins (immunology)</term><term>Spike Glycoprotein, Coronavirus</term><term>Viral Envelope Proteins (genetics)</term><term>Viral Envelope Proteins (immunology)</term><term>Viral Envelope Proteins (metabolism)</term><term>Viral Vaccines (genetics)</term><term>Viral Vaccines (immunology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Anticorps monoclonaux (immunologie)</term><term>Antigènes viraux (génétique)</term><term>Antigènes viraux (immunologie)</term><term>Arginine (génétique)</term><term>Arginine (immunologie)</term><term>Femelle</term><term>Fragments Fc des immunoglobulines (génétique)</term><term>Fragments Fc des immunoglobulines (immunologie)</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires (génétique)</term><term>Glycoprotéines membranaires (immunologie)</term><term>Glycoprotéines membranaires (métabolisme)</term><term>Lapins</term><term>Mutation ponctuelle</term><term>Peptidyl-Dipeptidase A (métabolisme)</term><term>Protéines de fusion recombinantes ()</term><term>Protéines de fusion recombinantes (génétique)</term><term>Protéines de fusion recombinantes (immunologie)</term><term>Protéines de l'enveloppe virale (génétique)</term><term>Protéines de l'enveloppe virale (immunologie)</term><term>Protéines de l'enveloppe virale (métabolisme)</term><term>Souris</term><term>Souris de lignée BALB C</term><term>Structure tertiaire des protéines (génétique)</term><term>Substitution d'acide aminé (immunologie)</term><term>Vaccins antiviraux (génétique)</term><term>Vaccins antiviraux (immunologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Recombinant Fusion Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Antigens, Viral</term><term>Arginine</term><term>Immunoglobulin Fc Fragments</term><term>Membrane Glycoproteins</term><term>Recombinant Fusion Proteins</term><term>Viral Envelope Proteins</term><term>Viral Vaccines</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Antibodies, Monoclonal</term><term>Antigens, Viral</term><term>Arginine</term><term>Immunoglobulin Fc Fragments</term><term>Membrane Glycoproteins</term><term>Recombinant Fusion Proteins</term><term>Viral Envelope Proteins</term><term>Viral Vaccines</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Protein Structure, Tertiary</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Antigènes viraux</term><term>Arginine</term><term>Fragments Fc des immunoglobulines</term><term>Glycoprotéines membranaires</term><term>Protéines de fusion recombinantes</term><term>Protéines de l'enveloppe virale</term><term>Structure tertiaire des protéines</term><term>Vaccins antiviraux</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Anticorps monoclonaux</term><term>Antigènes viraux</term><term>Arginine</term><term>Fragments Fc des 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xml:lang="fr"><term>Animaux</term><term>Femelle</term><term>Glycoprotéine de spicule des coronavirus</term><term>Lapins</term><term>Mutation ponctuelle</term><term>Protéines de fusion recombinantes</term><term>Souris</term><term>Souris de lignée BALB C</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>The spike (S) protein of severe acute respiratory syndrome coronavirus (SARS-CoV) has two major functions: interacting with the receptor to mediate virus entry and inducing protective immunity. Coincidently, the receptor-binding domain (RBD, residues 318–510) of SAR-CoV S protein is a major antigenic site to induce neutralizing antibodies. Here, we used RBD-Fc, a fusion protein containing the RBD and human IgG1 Fc, as a model in the studies and found that a single amino acid substitution in the RBD (R441A) could abolish the immunogenicity of RBD to induce neutralizing antibodies in immunized mice and rabbits. With a panel of anti-RBD mAbs as probes, we observed that R441A substitution was able to disrupt the majority of neutralizing epitopes in the RBD, suggesting that this residue is critical for the antigenic structure responsible for inducing protective immune responses. We also demonstrated that the RBD-Fc bearing R441A mutation could not bind to soluble and cell-associated angiotensin-converting enzyme 2 (ACE2), the functional receptor for SARS-CoV and failed to block S protein-mediated pseudovirus entry, indicating that this point mutation also disrupted the receptor-binding motif (RBM) in the RBD. Taken together, these data provide direct evidence to show that a single amino acid residue at key position in the RBD can determine the major function of SARS-CoV S protein and imply for designing SARS vaccines and therapeutics.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Marra, M A" uniqKey="Marra M">M.A. Marra</name></author><author><name sortKey="Jones, S J" uniqKey="Jones S">S.J. Jones</name></author><author><name sortKey="Astell, C R" uniqKey="Astell C">C.R. Astell</name></author><author><name sortKey="Holt, R A" uniqKey="Holt R">R.A. 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