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About:
Harnessing an RNA-mediated chaperone for the assembly of influenza hemagglutinin in an immunologically relevant conformation
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schema:ScholarlyArticle
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wasabi.inria.fr
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Type:
Academic Article
research paper
schema:ScholarlyArticle
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type
Academic Article
research paper
schema:ScholarlyArticle
isDefinedBy
Covid-on-the-Web dataset
has title
Harnessing an RNA-mediated chaperone for the assembly of influenza hemagglutinin in an immunologically relevant conformation
Creator
Park, Chan
Kim, Paul
Lee, S
Lee, C
Chae, Wonil
Choi, Y
Choi, Seong
Jang, Yo
Kim, Choon
Kim, Y
Kim, Young
Kwon, Soon
Lee, Yoon
Lee, Young
Seong, Baik
Yang, Seung
Chae, Y
Ho Byun, Young
Jang, W
Kim, C
Kwon, Y
Park, P
Source
PMC
abstract
A novel protein-folding function of RNA has been recognized, which can outperform previously known molecular chaperone proteins. The RNA as a molecular chaperone (chaperna) activity is intrinsic to some ribozymes and is operational during viral infections. Our purpose was to test whether influenza hemagglutinin (HA) can be assembled in a soluble, trimeric, and immunologically activating conformation by means of an RNA molecular chaperone (chaperna) activity. An RNA-interacting domain (RID) from the host being immunized was selected as a docking tag for RNA binding, which served as a transducer for the chaperna function for de novo folding and trimeric assembly of RID-HA1. Mutations that affect tRNA binding greatly increased the soluble aggregation defective in trimer assembly, suggesting that RNA interaction critically controls the kinetic network in the folding/assembly pathway. Immunization of mice resulted in strong hemagglutination inhibition and high titers of a neutralizing antibody, providing sterile protection against a lethal challenge and confirming the immunologically relevant HA conformation. The results may be translated into a rapid response to a new influenza pandemic. The harnessing of the novel chaperna described herein with immunologically tailored antigen-folding functions should serve as a robust prophylactic and diagnostic tool for viral infections.—Yang, S. W., Jang, Y. H., Kwon, S. B., Lee, Y. J., Chae, W., Byun, Y. H., Kim, P., Park, C., Lee, Y. J., Kim, C. K., Kim, Y. S., Choi, S. I., Seong, B. L. Harnessing an RNA-mediated chaperone for the assembly of influenza hemagglutinin in an immunologically relevant conformation.
has issue date
2018-01-08
(
xsd:dateTime
)
bibo:doi
10.1096/fj.201700747rr
bibo:pmid
29295864
has license
cc-by-nc
sha1sum (hex)
73d22ae218e1b28a39ac87844927cc56f164cbc2
schema:url
https://doi.org/10.1096/fj.201700747rr
resource representing a document's title
Harnessing an RNA-mediated chaperone for the assembly of influenza hemagglutinin in an immunologically relevant conformation
has PubMed Central identifier
PMC5901386
has PubMed identifier
29295864
schema:publication
FASEB J
resource representing a document's body
covid:73d22ae218e1b28a39ac87844927cc56f164cbc2#body_text
is
schema:about
of
named entity 'docking'
named entity 'operational'
named entity 'activity'
covid:arg/73d22ae218e1b28a39ac87844927cc56f164cbc2
named entity 'trimeric'
named entity 'molecular chaperone'
named entity 'assembled'
named entity 'titers'
named entity 'aggregation'
named entity 'tag'
named entity 'high'
named entity 'influenza'
named entity 'Our'
named entity 'soluble'
named entity 'translated'
named entity 'influenza'
named entity 'rapid response'
named entity 'conformation'
named entity 'influenza hemagglutinin'
named entity 'RNA'
named entity 'Triton X-100'
named entity 'foldase'
named entity 'viruses'
named entity 'solubility'
named entity 'GE Healthcare'
named entity 'mice'
named entity 'RNA'
named entity 'influenza infection'
named entity 'conformation'
named entity 'mice'
named entity 'PVDF'
named entity 'solubilization'
named entity 'Recombinant'
named entity 'virus'
named entity 'refolding'
named entity 'PBS'
named entity 'affinity purification'
named entity 'substrate'
named entity 'mice'
named entity 'mice'
named entity 'RNA'
named entity 'IACUC'
named entity 'total protein'
named entity 'antisera'
named entity 'antibody'
named entity 'serum'
named entity 'mice'
named entity 'antisera'
named entity 'influenza virus'
named entity 'antiserum'
named entity 'virus'
named entity 'hemagglutination inhibition'
named entity 'virus'
named entity 'St. Louis'
named entity 'conformation'
named entity 'tRNAs'
named entity 'mice'
named entity 'infection'
named entity 'LysRS'
named entity 'mice'
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