Effects of Human Anti-Spike Protein Receptor Binding Domain Antibodies on Severe Acute Respiratory Syndrome Coronavirus Neutralization Escape and Fitness
Identifieur interne : 001656 ( Main/Curation ); précédent : 001655; suivant : 001657Effects of Human Anti-Spike Protein Receptor Binding Domain Antibodies on Severe Acute Respiratory Syndrome Coronavirus Neutralization Escape and Fitness
Auteurs : Jianhua Sui [États-Unis] ; Meagan Deming [États-Unis] ; Barry Rockx [États-Unis] ; Robert C. Liddington [États-Unis] ; Quan Karen Zhu [États-Unis] ; Ralph S. Baric [États-Unis] ; Wayne A. Marasco [États-Unis]Source :
- Journal of Virology [ 0022-538X ] ; 2014.
Descripteurs français
- KwdFr :
- Animaux, Anticorps antiviraux (immunologie), Femelle, Glycoprotéine de spicule des coronavirus (immunologie), Humains, Mutation, Peptidyl-Dipeptidase A (métabolisme), Récepteurs viraux (métabolisme), Souris, Souris de lignée BALB C, Tests de neutralisation, Virulence, Virus du SRAS (immunologie), Virus du SRAS (pathogénicité), Virus du SRAS (physiologie), Échappement immunitaire.
- MESH :
- immunologie : Anticorps antiviraux, Glycoprotéine de spicule des coronavirus, Virus du SRAS.
- métabolisme : Peptidyl-Dipeptidase A, Récepteurs viraux.
- pathogénicité : Virus du SRAS.
- physiologie : Virus du SRAS.
- Animaux, Femelle, Humains, Mutation, Souris, Souris de lignée BALB C, Tests de neutralisation, Virulence, Échappement immunitaire.
English descriptors
- KwdEn :
- Animals, Antibodies, Viral (immunology), Female, Humans, Immune Evasion, Mice, Mice, Inbred BALB C, Mutation, Neutralization Tests, Peptidyl-Dipeptidase A (metabolism), Receptors, Virus (metabolism), SARS Virus (immunology), SARS Virus (pathogenicity), SARS Virus (physiology), Spike Glycoprotein, Coronavirus (immunology), Virulence.
- MESH :
- chemical , immunology : Antibodies, Viral, Spike Glycoprotein, Coronavirus.
- chemical , metabolism : Peptidyl-Dipeptidase A, Receptors, Virus.
- immunology : SARS Virus.
- pathogenicity : SARS Virus.
- physiology : SARS Virus.
- Animals, Female, Humans, Immune Evasion, Mice, Mice, Inbred BALB C, Mutation, Neutralization Tests, Virulence.
Abstract
The receptor binding domain (RBD) of the spike (S) glycoprotein of severe acute respiratory syndrome coronavirus (SARS-CoV) is a major target of protective immunity
Url:
DOI: 10.1128/JVI.02232-14
PubMed: 25231316
PubMed Central: 4248992
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PMC:4248992Le document en format XML
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<series><title level="j">Journal of Virology</title>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term>
<term>Antibodies, Viral (immunology)</term>
<term>Female</term>
<term>Humans</term>
<term>Immune Evasion</term>
<term>Mice</term>
<term>Mice, Inbred BALB C</term>
<term>Mutation</term>
<term>Neutralization Tests</term>
<term>Peptidyl-Dipeptidase A (metabolism)</term>
<term>Receptors, Virus (metabolism)</term>
<term>SARS Virus (immunology)</term>
<term>SARS Virus (pathogenicity)</term>
<term>SARS Virus (physiology)</term>
<term>Spike Glycoprotein, Coronavirus (immunology)</term>
<term>Virulence</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term>
<term>Anticorps antiviraux (immunologie)</term>
<term>Femelle</term>
<term>Glycoprotéine de spicule des coronavirus (immunologie)</term>
<term>Humains</term>
<term>Mutation</term>
<term>Peptidyl-Dipeptidase A (métabolisme)</term>
<term>Récepteurs viraux (métabolisme)</term>
<term>Souris</term>
<term>Souris de lignée BALB C</term>
<term>Tests de neutralisation</term>
<term>Virulence</term>
<term>Virus du SRAS (immunologie)</term>
<term>Virus du SRAS (pathogénicité)</term>
<term>Virus du SRAS (physiologie)</term>
<term>Échappement immunitaire</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Antibodies, Viral</term>
<term>Spike Glycoprotein, Coronavirus</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Peptidyl-Dipeptidase A</term>
<term>Receptors, Virus</term>
</keywords>
<keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Anticorps antiviraux</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Virus du SRAS</term>
</keywords>
<keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>SARS Virus</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Peptidyl-Dipeptidase A</term>
<term>Récepteurs viraux</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>
</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>Animals</term>
<term>Female</term>
<term>Humans</term>
<term>Immune Evasion</term>
<term>Mice</term>
<term>Mice, Inbred BALB C</term>
<term>Mutation</term>
<term>Neutralization Tests</term>
<term>Virulence</term>
</keywords>
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<term>Femelle</term>
<term>Humains</term>
<term>Mutation</term>
<term>Souris</term>
<term>Souris de lignée BALB C</term>
<term>Tests de neutralisation</term>
<term>Virulence</term>
<term>Échappement immunitaire</term>
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<front><div type="abstract" xml:lang="en"><title>ABSTRACT</title>
<p>The receptor binding domain (RBD) of the spike (S) glycoprotein of severe acute respiratory syndrome coronavirus (SARS-CoV) is a major target of protective immunity <italic>in vivo</italic>
. Although a large number of neutralizing antibodies (nAbs) have been developed, it remains unclear if a single RBD-targeting nAb or two in combination can prevent neutralization escape and, if not, attenuate viral virulence <italic>in vivo</italic>
. In this study, we used a large panel of human nAbs against an epitope that overlaps the interface between the RBD and its receptor, angiotensin-converting enzyme 2 (ACE2), to assess their cross-neutralization activities against a panel of human and zoonotic SARS-CoVs and neutralization escape mutants. We also investigated the neutralization escape profiles of these nAbs and evaluated their effects on receptor binding and virus fitness <italic>in vitro</italic>
and in mice. We found that some nAbs had great potency and breadth in neutralizing multiple viral strains, including neutralization escape viruses derived from other nAbs; however, no single nAb or combination of two blocked neutralization escape. Interestingly, in mice the neutralization escape mutant viruses showed either attenuation (Urbani background) or increased virulence (GD03 background) consistent with the different binding affinities between their RBDs and the mouse ACE2. We conclude that using either single nAbs or dual nAb combinations to target a SARS-CoV RBD epitope that shows plasticity may have limitations for preventing neutralization escape during <italic>in vivo</italic>
immunotherapy. However, RBD-directed nAbs may be useful for providing broad neutralization and prevention of escape variants when combined with other nAbs that target a second conserved epitope with less plasticity and more structural constraint.</p>
<p><bold>IMPORTANCE</bold>
The emergence of severe acute respiratory syndrome coronavirus (SARS-CoV) in 2002 and Middle East respiratory syndrome coronavirus (MERS-CoV) in 2012 has resulted in severe human respiratory disease with high death rates. Their zoonotic origins highlight the likelihood of reemergence or further evolution into novel human coronavirus pathogens. Broadly neutralizing antibodies (nAbs) that prevent infection of related viruses represent an important immunostrategy for combating coronavirus infections; however, for this strategy to succeed, it is essential to uncover nAb-mediated escape pathways and to pioneer strategies that prevent escape. Here, we used SARS-CoV as a research model and examined the escape pathways of broad nAbs that target the receptor binding domain (RBD) of the virus. We found that neither single nAbs nor two nAbs in combination blocked escape. Our results suggest that targeting conserved regions with less plasticity and more structural constraint rather than the SARS-CoV RBD-like region(s) should have broader utility for antibody-based immunotherapy.</p>
</div>
</front>
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