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Recombinant Soluble Henipavirus Glycoprotein Preparation.
Methods Mol Biol. 2023; 2682:33-58.MM

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.

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Publisher Full Text (DOI)

Authors+Show Affiliations

Department of Microbiology and Immunology, Uniformed Services University, Bethesda, MD, USA.

Department of Microbiology and Immunology, Uniformed Services University, Bethesda, MD, USA.

Department of Microbiology and Immunology, Uniformed Services University, Bethesda, MD, USA.

Department of Microbiology and Immunology, Uniformed Services University, Bethesda, MD, USA.

Department of Veterinary Biosciences, College of Veterinary Medicine, The Ohio State University, Columbus, OH, USA. Center for Retrovirus Research, The Ohio State University, Columbus, OH, USA.

Department of Microbiology and Immunology, Uniformed Services University, Bethesda, MD, USA.

Department of Microbiology and Immunology, Uniformed Services University, Bethesda, MD, USA. christopher.broder@usuhs.edu.

MeSH

HenipavirusAntibodies, BlockingAntibodies, Monoclonal

Pub Type(s)

Journal Article

Research Support, N.I.H., Extramural

Language

eng

PubMed ID

37610572

Citation

Yan, Lianying, et al. "Recombinant Soluble Henipavirus Glycoprotein Preparation." Methods in Molecular Biology (Clifton, N.J.), vol. 2682, 2023, pp. 33-58.

Yan L, Sterling SL, Fusco DL, et al. Recombinant Soluble Henipavirus Glycoprotein Preparation. Methods Mol Biol. 2023;2682:33-58.

Yan, L., Sterling, S. L., Fusco, D. L., Chan, Y. P., Xu, K., Laing, E. D., & Broder, C. C. (2023). Recombinant Soluble Henipavirus Glycoprotein Preparation. Methods in Molecular Biology (Clifton, N.J.), 2682, 33-58. https://doi.org/10.1007/978-1-0716-3283-3_3

Yan L, et al. Recombinant Soluble Henipavirus Glycoprotein Preparation. Methods Mol Biol. 2023;2682:33-58. PubMed PMID: 37610572.

* Article titles in AMA citation format should be in sentence-case

TY - JOUR T1 - Recombinant Soluble Henipavirus Glycoprotein Preparation. AU - Yan,Lianying, AU - Sterling,Spencer L, AU - Fusco,Deborah L, AU - Chan,Yee-Peng, AU - Xu,Kai, AU - Laing,Eric D, AU - Broder,Christopher C, PY - 2023/8/24/medline PY - 2023/8/23/pubmed PY - 2023/8/23/entrez KW - Cedar virus KW - Cross-linking KW - Expression KW - F glycoprotein KW - G glycoprotein KW - Ghana virus KW - Hendra virus KW - Henipaviruses KW - Multiplex microsphere immunoassay KW - Mòjiāng virus KW - Nipah virus KW - Purification SP - 33 EP - 58 JF - Methods in molecular biology (Clifton, N.J.) JO - Methods Mol Biol VL - 2682 N2 - 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. SN - 1940-6029 UR - https://www.unboundmedicine.com/medline/citation/37610572/Recombinant_Soluble_Henipavirus_Glycoprotein_Preparation_ DB - PRIME DP - Unbound Medicine ER -