SrasV1, Ncbi, Checkpoint, bibRecord, 001145

Single Amino Acid Substitutions in the Severe Acute Respiratory Syndrome Coronavirus Spike Glycoprotein Determine Viral Entry and Immunogenicity of a Major Neutralizing Domain

Identifieur interne : 001145 ( Ncbi/Checkpoint ); précédent : 001144; suivant : 001146

Single Amino Acid Substitutions in the Severe Acute Respiratory Syndrome Coronavirus Spike Glycoprotein Determine Viral Entry and Immunogenicity of a Major Neutralizing Domain

Auteurs : Christopher E. Yi [États-Unis] ; Lei Ba [États-Unis] ; Linqi Zhang [États-Unis] ; David D. Ho [États-Unis] ; Zhiwei Chen [États-Unis]

Source :

Journal of Virology [ 0022-538X ] ; 2005.

RBID : PMC:1212612

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence, Amino Acid Substitution, Animals, Antibodies, Viral (biosynthesis), Antigens, Viral (chemistry), Antigens, Viral (genetics), Cell Line, Female, Humans, Membrane Glycoproteins (chemistry), Membrane Glycoproteins (genetics), Membrane Glycoproteins (immunology), Membrane Glycoproteins (physiology), Mice, Mice, Inbred BALB C, Microscopy, Electron, Mutagenesis, Site-Directed, Neutralization Tests, Protein Structure, Tertiary, SARS Virus (genetics), SARS Virus (immunology), SARS Virus (pathogenicity), SARS Virus (physiology), Sequence Deletion, Spike Glycoprotein, Coronavirus, Vaccines, DNA (administration & dosage), Vaccines, DNA (genetics), Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics), Viral Envelope Proteins (immunology), Viral Envelope Proteins (physiology), Viral Vaccines (administration & dosage), Viral Vaccines (genetics), Virulence (genetics), Virulence (immunology), Virulence (physiology).
MESH :
- chemical , administration & dosage : Vaccines, DNA, Viral Vaccines.
- chemical , biosynthesis : Antibodies, Viral.
- chemical , chemistry : Antigens, Viral, Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , genetics : Antigens, Viral, Membrane Glycoproteins, Vaccines, DNA, Viral Envelope Proteins, Viral Vaccines.
- chemical , immunology : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , physiology : Membrane Glycoproteins, Viral Envelope Proteins.
- genetics : SARS Virus, Virulence.
- immunology : SARS Virus, Virulence.
- pathogenicity : SARS Virus.
- physiology : SARS Virus, Virulence.
- Amino Acid Sequence, Amino Acid Substitution, Animals, Cell Line, Female, Humans, Mice, Mice, Inbred BALB C, Microscopy, Electron, Mutagenesis, Site-Directed, Neutralization Tests, Protein Structure, Tertiary, Sequence Deletion, Spike Glycoprotein, Coronavirus.

Abstract

Neutralizing antibodies (NAbs) against severe acute respiratory syndrome (SARS) coronavirus (SARS-CoV) spike (S) glycoprotein confer protection to animals experimentally infected with the pathogenic virus. We and others previously demonstrated that a major mechanism for neutralizing SARS-CoV was through blocking the interaction between the S glycoprotein and the cellular receptor angiotensin-converting enzyme 2 (ACE2). In this study, we used in vivo electroporation DNA immunization and a pseudovirus-based assay to functionally evaluate immunogenicity and viral entry. We characterized the neutralization and viral entry determinants within the ACE2-binding domain of the S glycoprotein. The deletion of a positively charged region SΔ(422-463) abolished the capacity of the S glycoprotein to induce NAbs in mice vaccinated by in vivo DNA electroporation. Moreover, the SΔ(422-463) pseudovirus was unable to infect HEK293T-ACE2 cells. To determine the specific residues that contribute to related phenotypes, we replaced eight basic amino acids with alanine. We found that a single amino acid substitution (R441A) in the full-length S DNA vaccine failed to induce NAbs and abolished viral entry when pseudoviruses were generated. However, another substitution (R453A) abolished viral entry while retaining the capacity for inducing NAbs. The difference between R441A and R453A suggests that the determinants for immunogenicity and viral entry may not be identical. Our findings provide direct evidence that these basic residues are essential for immunogenicity of the major neutralizing domain and for viral entry. Our data have implications for the rational design of vaccine and antiviral agents as well as for understanding viral tropism.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1212612

DOI: 10.1128/JVI.79.18.11638-11646.2005
PubMed: 16140741
PubMed Central: 1212612

Affiliations:

Links to Exploration step

PMC:1212612

Le document en format XML

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<term>Amino Acid Substitution</term>
<term>Animals</term>
<term>Antibodies, Viral (biosynthesis)</term>
<term>Antigens, Viral (chemistry)</term>
<term>Antigens, Viral (genetics)</term>
<term>Cell Line</term>
<term>Female</term>
<term>Humans</term>
<term>Membrane Glycoproteins (chemistry)</term>
<term>Membrane Glycoproteins (genetics)</term>
<term>Membrane Glycoproteins (immunology)</term>
<term>Membrane Glycoproteins (physiology)</term>
<term>Mice</term>
<term>Mice, Inbred BALB C</term>
<term>Microscopy, Electron</term>
<term>Mutagenesis, Site-Directed</term>
<term>Neutralization Tests</term>
<term>Protein Structure, Tertiary</term>
<term>SARS Virus (genetics)</term>
<term>SARS Virus (immunology)</term>
<term>SARS Virus (pathogenicity)</term>
<term>SARS Virus (physiology)</term>
<term>Sequence Deletion</term>
<term>Spike Glycoprotein, Coronavirus</term>
<term>Vaccines, DNA (administration & dosage)</term>
<term>Vaccines, DNA (genetics)</term>
<term>Viral Envelope Proteins (chemistry)</term>
<term>Viral Envelope Proteins (genetics)</term>
<term>Viral Envelope Proteins (immunology)</term>
<term>Viral Envelope Proteins (physiology)</term>
<term>Viral Vaccines (administration & dosage)</term>
<term>Viral Vaccines (genetics)</term>
<term>Virulence (genetics)</term>
<term>Virulence (immunology)</term>
<term>Virulence (physiology)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term>
<term>Anticorps antiviraux (biosynthèse)</term>
<term>Antigènes viraux ()</term>
<term>Antigènes viraux (génétique)</term>
<term>Délétion de séquence</term>
<term>Femelle</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires ()</term>
<term>Glycoprotéines membranaires (génétique)</term>
<term>Glycoprotéines membranaires (immunologie)</term>
<term>Glycoprotéines membranaires (physiologie)</term>
<term>Humains</term>
<term>Lignée cellulaire</term>
<term>Microscopie électronique</term>
<term>Mutagenèse dirigée</term>
<term>Protéines de l'enveloppe virale ()</term>
<term>Protéines de l'enveloppe virale (génétique)</term>
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<term>Protéines de l'enveloppe virale (physiologie)</term>
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<term>Souris de lignée BALB C</term>
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<term>Séquence d'acides aminés</term>
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<term>Vaccins antiviraux (génétique)</term>
<term>Vaccins à ADN (administration et posologie)</term>
<term>Vaccins à ADN (génétique)</term>
<term>Virulence (génétique)</term>
<term>Virulence (immunologie)</term>
<term>Virulence (physiologie)</term>
<term>Virus du SRAS (génétique)</term>
<term>Virus du SRAS (immunologie)</term>
<term>Virus du SRAS (pathogénicité)</term>
<term>Virus du SRAS (physiologie)</term>
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<keywords scheme="MESH" type="chemical" qualifier="administration & dosage" xml:lang="en"><term>Vaccines, DNA</term>
<term>Viral Vaccines</term>
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<term>Membrane Glycoproteins</term>
<term>Viral Envelope Proteins</term>
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<term>Membrane Glycoproteins</term>
<term>Vaccines, DNA</term>
<term>Viral Envelope Proteins</term>
<term>Viral Vaccines</term>
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<term>Viral Envelope Proteins</term>
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<term>Vaccins à ADN</term>
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<term>Vaccins antiviraux</term>
<term>Vaccins à ADN</term>
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<term>Virus du SRAS</term>
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<keywords scheme="MESH" qualifier="pathogénicité" xml:lang="fr"><term>Virus du SRAS</term>
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<term>Protéines de l'enveloppe virale</term>
<term>Virulence</term>
<term>Virus du SRAS</term>
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<keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>SARS Virus</term>
<term>Virulence</term>
</keywords>
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<term>Amino Acid Substitution</term>
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<term>Cell Line</term>
<term>Female</term>
<term>Humans</term>
<term>Mice</term>
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<term>Neutralization Tests</term>
<term>Protein Structure, Tertiary</term>
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<term>Délétion de séquence</term>
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<term>Microscopie électronique</term>
<term>Mutagenèse dirigée</term>
<term>Protéines de l'enveloppe virale</term>
<term>Souris</term>
<term>Souris de lignée BALB C</term>
<term>Structure tertiaire des protéines</term>
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<front><div type="abstract" xml:lang="en"><p>Neutralizing antibodies (NAbs) against severe acute respiratory syndrome (SARS) coronavirus (SARS-CoV) spike (S) glycoprotein confer protection to animals experimentally infected with the pathogenic virus. We and others previously demonstrated that a major mechanism for neutralizing SARS-CoV was through blocking the interaction between the S glycoprotein and the cellular receptor angiotensin-converting enzyme 2 (ACE2). In this study, we used in vivo electroporation DNA immunization and a pseudovirus-based assay to functionally evaluate immunogenicity and viral entry. We characterized the neutralization and viral entry determinants within the ACE2-binding domain of the S glycoprotein. The deletion of a positively charged region SΔ(422-463) abolished the capacity of the S glycoprotein to induce NAbs in mice vaccinated by in vivo DNA electroporation. Moreover, the SΔ(422-463) pseudovirus was unable to infect HEK293T-ACE2 cells. To determine the specific residues that contribute to related phenotypes, we replaced eight basic amino acids with alanine. We found that a single amino acid substitution (R441A) in the full-length S DNA vaccine failed to induce NAbs and abolished viral entry when pseudoviruses were generated. However, another substitution (R453A) abolished viral entry while retaining the capacity for inducing NAbs. The difference between R441A and R453A suggests that the determinants for immunogenicity and viral entry may not be identical. Our findings provide direct evidence that these basic residues are essential for immunogenicity of the major neutralizing domain and for viral entry. Our data have implications for the rational design of vaccine and antiviral agents as well as for understanding viral tropism.</p>
</div>
</front>
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<name sortKey="Ho, David D" sort="Ho, David D" uniqKey="Ho D" first="David D." last="Ho">David D. Ho</name>
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Single Amino Acid Substitutions in the Severe Acute Respiratory Syndrome Coronavirus Spike Glycoprotein Determine Viral Entry and Immunogenicity of a Major Neutralizing Domain

Single Amino Acid Substitutions in the Severe Acute Respiratory Syndrome Coronavirus Spike Glycoprotein Determine Viral Entry and Immunogenicity of a Major Neutralizing Domain

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