@inbook{5c1da0289d3a483d9dca3b9011fad693,
title = "Recombinant Soluble Henipavirus Glycoprotein Preparation",
abstract = "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.",
keywords = "Cedar virus, Cross-linking, Expression, F glycoprotein, G glycoprotein, Ghana virus, Hendra virus, Henipaviruses, Multiplex microsphere immunoassay, M{\`o}jiāng virus, Nipah virus, Purification",
author = "Lianying Yan and Sterling, {Spencer L.} and Fusco, {Deborah L.} and Chan, {Yee Peng} and Kai Xu and Laing, {Eric D.} and Broder, {Christopher C.}",
note = "Publisher Copyright: {\textcopyright} 2023, Springer Science+Business Media, LLC, part of Springer Nature.",
year = "2023",
doi = "10.1007/978-1-0716-3283-3_3",
language = "English",
series = "Methods in Molecular Biology",
publisher = "Humana Press Inc.",
pages = "33--58",
booktitle = "Methods in Molecular Biology",
}