Recombinant Soluble Henipavirus Glycoprotein Preparation.
Cedar virus
Cross-linking
Expression
F glycoprotein
G glycoprotein
Ghana virus
Hendra virus
Henipaviruses
Multiplex microsphere immunoassay
Mòjiāng virus
Nipah virus
Purification
Journal
Methods in molecular biology (Clifton, N.J.)
ISSN: 1940-6029
Titre abrégé: Methods Mol Biol
Pays: United States
ID NLM: 9214969
Informations de publication
Date de publication:
2023
2023
Historique:
medline:
24
8
2023
pubmed:
23
8
2023
entrez:
23
8
2023
Statut:
ppublish
Résumé
Henipaviruses possess two envelope glycoproteins, the attachment (G) and the fusion (F) proteins that mediate cellular entry and are the major targets of virus-neutralizing antibody responses. Recombinant expression technologies have been used to produce soluble G and F proteins (sG and sF) that retain native-like oligomeric conformations and epitopes, which are advantageous for the development and characterization of vaccines and antiviral antibody therapeutics. In addition to Hendra virus and Nipah virus tetrameric sG and trimeric sF production, we also describe the expression and purification of Cedar virus tetrameric sG and Ghana virus trimeric sF glycoproteins. These henipavirus glycoproteins were also used as immunizing antigens to generate monoclonal antibodies, and binding was demonstrated with a pan-henipavirus multiplex microsphere immunoassay.
Identifiants
pubmed: 37610572
doi: 10.1007/978-1-0716-3283-3_3
doi:
Substances chimiques
Antibodies, Blocking
0
Antibodies, Monoclonal
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
33-58Subventions
Organisme : NIAID NIH HHS
ID : U19 AI142764
Pays : United States
Organisme : NIAID NIH HHS
ID : U01 AI077995
Pays : United States
Organisme : NIAID NIH HHS
ID : R01 AI054715
Pays : United States
Informations de copyright
© 2023. Springer Science+Business Media, LLC, part of Springer Nature.
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