Generation of Chicken IgY against SARS-COV-2 Spike Protein and Epitope Mapping.
Administration, Intranasal
Animals
Antibodies, Neutralizing
/ administration & dosage
Antibodies, Viral
/ administration & dosage
Betacoronavirus
/ immunology
COVID-19
Chickens
Coronavirus Infections
/ epidemiology
Cross Reactions
Epitope Mapping
Feasibility Studies
Humans
Immunization, Passive
/ methods
Immunoglobulins
/ administration & dosage
Pandemics
Pneumonia, Viral
/ epidemiology
SARS-CoV-2
Spike Glycoprotein, Coronavirus
/ immunology
COVID-19 Serotherapy
Journal
Journal of immunology research
ISSN: 2314-7156
Titre abrégé: J Immunol Res
Pays: Egypt
ID NLM: 101627166
Informations de publication
Date de publication:
2020
2020
Historique:
received:
19
06
2020
revised:
16
09
2020
accepted:
25
09
2020
entrez:
2
11
2020
pubmed:
3
11
2020
medline:
11
11
2020
Statut:
epublish
Résumé
This new decade has started with a global pandemic of COVID-19 caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), precipitating a worldwide health crisis and economic downturn. Scientists and clinicians have been racing against time to find therapies for COVID-19. Repurposing approved drugs, developing vaccines and employing passive immunization are three major therapeutic approaches to fighting COVID-19. Chicken immunoglobulin Y (IgY) has the potential to be used as neutralizing antibody against respiratory infections, and its advantages include high avidity, low risk of adverse immune responses, and easy local delivery by intranasal administration. In this study, we raised antibody against the spike (S) protein of SARS-CoV-2 in chickens and extracted IgY (called IgY-S) from egg yolk. IgY-S exhibited high immunoreactivity against SARS-CoV-2 S, and by epitope mapping, we found five linear epitopes of IgY-S in SARS-CoV-2 S, two of which are cross-reactive with SARS-CoV S. Notably, epitope SIIAYTMSL, one of the identified epitopes, partially overlaps the S1/S2 cleavage region in SARS-CoV-2 S and is located on the surface of S trimer in 3D structure, close to the S1/S2 cleavage site. Thus, antibody binding at this location could physically block the access of proteolytic enzymes to S1/S2 cleavage site and thereby impede S1/S2 proteolytic cleavage, which is crucial to subsequent virus-cell membrane fusion and viral cell entry. Therefore, the feasibility of using IgY-S or epitope SIIAYTMS-specific IgY as neutralizing antibody for preventing or treating SARS-CoV-2 infection is worth exploring.
Identifiants
pubmed: 33134398
doi: 10.1155/2020/9465398
pmc: PMC7568776
doi:
Substances chimiques
Antibodies, Neutralizing
0
Antibodies, Viral
0
IgY
0
Immunoglobulins
0
Spike Glycoprotein, Coronavirus
0
spike protein, SARS-CoV-2
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
9465398Informations de copyright
Copyright © 2020 Yan Lu et al.
Déclaration de conflit d'intérêts
All authors declare no conflict of interest.
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