Antigen-adjuvant interactions, stability, and immunogenicity profiles of a SARS-CoV-2 receptor-binding domain (RBD) antigen formulated with aluminum salt and CpG adjuvants

Autor: Sakshi Bajoria, Kawaljit Kaur, Ozan S. Kumru, Greta Van Slyke, Jennifer Doering, Hayley Novak, Sergio A. Rodriguez Aponte, Neil C. Dalvie, Christopher A. Naranjo, Ryan S. Johnston, Judith Maxwell Silverman, Harry Kleanthous, J. Christopher Love, Nicholas J. Mantis, Sangeeta B. Joshi, David B. Volkin
Jazyk: angličtina
Rok vydání: 2022
Předmět:
Zdroj: Human Vaccines & Immunotherapeutics, Vol 18, Iss 5 (2022)
Druh dokumentu: article
ISSN: 2164-5515
2164-554X
21645515
DOI: 10.1080/21645515.2022.2079346
Popis: Low-cost, refrigerator-stable COVID-19 vaccines will facilitate global access and improve vaccine coverage in low- and middle-income countries. To this end, subunit-based approaches targeting the receptor-binding domain (RBD) of SARS-CoV-2 Spike protein remain attractive. Antibodies against RBD neutralize SARS-CoV-2 by blocking viral attachment to the host cell receptor, ACE2. Here, a yeast-produced recombinant RBD antigen (RBD-L452K-F490W or RBD-J) was formulated with various combinations of aluminum-salt (Alhydrogel®, AH; AdjuPhos®, AP) and CpG 1018 adjuvants. We assessed the effect of antigen-adjuvant interactions on the stability and mouse immunogenicity of various RBD-J preparations. While RBD-J was 50% adsorbed to AH and
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