Built-in RNA-mediated chaperone (chaperna) for antigen folding tailored to immunized hosts.
Animals
Antibodies, Monoclonal
/ biosynthesis
Antibodies, Viral
/ biosynthesis
Antigens, Viral
/ chemistry
Coronavirus Infections
/ blood
Enzyme-Linked Immunosorbent Assay
Female
Hemagglutinin Glycoproteins, Influenza Virus
/ chemistry
Humans
Hybridomas
/ immunology
Immunization
Influenza Vaccines
Lysine-tRNA Ligase
/ chemistry
Mice
Mice, Inbred BALB C
Middle East Respiratory Syndrome Coronavirus
/ immunology
Molecular Chaperones
Protein Conformation
Protein Domains
Protein Folding
Recombinant Fusion Proteins
/ chemistry
Serologic Tests
Solubility
MERS-CoV
chaperna
chaperone
influenza virus
monoclonal antibody
Journal
Biotechnology and bioengineering
ISSN: 1097-0290
Titre abrégé: Biotechnol Bioeng
Pays: United States
ID NLM: 7502021
Informations de publication
Date de publication:
07 2020
07 2020
Historique:
received:
24
11
2019
revised:
12
04
2020
accepted:
13
04
2020
pubmed:
17
4
2020
medline:
12
9
2020
entrez:
17
4
2020
Statut:
ppublish
Résumé
High-quality antibody (Ab) production depends on the availability of immunologically relevant antigens. We present a potentially universal platform for generating soluble antigens from bacterial hosts, tailored to immunized animals for Ab production. A novel RNA-dependent chaperone, in which the target antigen is genetically fused with an RNA-interacting domain (RID) docking tag derived from the immunized host, promotes the solubility and robust folding of the target antigen. We selected the N-terminal tRNA-binding domain of lysyl-tRNA synthetase (LysRS) as the RID for fusion with viral proteins and demonstrated the expression of the RID fusion proteins in their soluble and native conformations; immunization predominantly elicited Ab responses to the target antigen, whereas the "self" RID tag remained nonimmunogenic. Differential immunogenicity of the fusion proteins greatly enriched and simplified the screening of hybridoma clones of monoclonal antibodies (mAbs), enabling specific and sensitive serodiagnosis of MERS-CoV infection. Moreover, mAbs against the consensus influenza hemagglutinin stalk domain enabled a novel assay for trivalent seasonal influenza vaccines. The Fc-mediated effector function was demonstrated, which could be harnessed for the design of next-generation "universal" influenza vaccines. The nonimmunogenic built-in antigen folding module tailored to a repertoire of immunized animal hosts will drive immunochemical diagnostics, therapeutics, and designer vaccines.
Identifiants
pubmed: 32297972
doi: 10.1002/bit.27355
pmc: PMC7262357
doi:
Substances chimiques
Antibodies, Monoclonal
0
Antibodies, Viral
0
Antigens, Viral
0
H1N1 virus hemagglutinin
0
Hemagglutinin Glycoproteins, Influenza Virus
0
Influenza Vaccines
0
Molecular Chaperones
0
Recombinant Fusion Proteins
0
Lysine-tRNA Ligase
EC 6.1.1.6
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1990-2007Subventions
Organisme : National Research Foundation of Korea
ID : NRF-2018M3A9H4079358
Pays : International
Organisme : Graduate School of YONSEI University Research Scholarship Grants
Pays : International
Organisme : Ministry of Food and Drug Safety of the Republic of Korea
ID : 16172MFDS199
Pays : International
Organisme : Ministry of Food and Drug Safety of the Republic of Korea
ID : 16172MFDS268
Pays : International
Organisme : Ministry of Food and Drug Safety of the Republic of Korea
ID : 16172MFDS363
Pays : International
Organisme : Ministry of Food and Drug Safety of the Republic of Korea
ID : 18172MFDS252
Pays : International
Informations de copyright
© 2020 The Authors. Biotechnology and Bioengineering published by Wiley Periodicals, Inc.
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