{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,4,11]],"date-time":"2025-04-11T18:42:42Z","timestamp":1744396962728,"version":"3.37.3"},"reference-count":39,"publisher":"Oxford University Press (OUP)","issue":"6","license":[{"start":{"date-parts":[[2023,9,1]],"date-time":"2023-09-01T00:00:00Z","timestamp":1693526400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/pages\/standard-publication-reuse-rights"}],"funder":[{"DOI":"10.13039\/501100000046","name":"National Research Council of Canada","doi-asserted-by":"crossref","award":["AWD-019441"],"award-info":[{"award-number":["AWD-019441"]}],"id":[{"id":"10.13039\/501100000046","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2023,9,15]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Current vaccine efforts to combat SARS-CoV-2 are focused on the whole spike protein administered as mRNA, viral vector, or protein subunit. However, the SARS-CoV-2 receptor-binding domain (RBD) is the immunodominant portion of the spike protein, accounting for 90% of serum neutralizing activity. In this study, we constructed several versions of RBD and together with aluminum hydroxide or DDA (dimethyldioctadecylammonium bromide)\/TDB (d-(+)-trehalose 6,6\u2032-dibehenate) adjuvant evaluated immunogenicity in mice. We generated human angiotensin-converting enzyme 2 knock-in mice to evaluate vaccine efficacy in vivo following viral challenge. We found that 1) subdomain (SD)1 was essential for the RBD to elicit maximal immunogenicity; 2) RBDSD1 produced in mammalian HEK cells elicited better immunogenicity than did protein produced in insect or yeast cells; 3) RBDSD1 combined with the CD4 Th1 adjuvant DDA\/TDB produced higher neutralizing Ab responses and stronger CD4 T cell responses than did aluminum hydroxide; 4) addition of monomeric human Fc receptor to RBDSD1 (RBDSD1Fc) significantly enhanced immunogenicity and neutralizing Ab titers; 5) the Beta version of RBDSD1Fc provided a broad range of cross-neutralization to multiple antigenic variants of concern, including Omicron; and 6) the Beta version of RBDSD1Fc with DDA\/TDB provided complete protection against virus challenge in the knock-in mouse model. Thus, we have identified an optimized RBD-based subunit vaccine suitable for clinical trials.<\/jats:p>","DOI":"10.4049\/jimmunol.2300282","type":"journal-article","created":{"date-parts":[[2023,7,26]],"date-time":"2023-07-26T13:14:23Z","timestamp":1690377263000},"page":"981-993","source":"Crossref","is-referenced-by-count":1,"title":["Identification of an Optimized Receptor-Binding Domain Subunit Vaccine against SARS-CoV-2"],"prefix":"10.1093","volume":"211","author":[{"given":"Hong","family":"Yu","sequence":"first","affiliation":[{"name":"British Columbia Centre for Disease Control, University of British Columbia, Vancouver , British Columbia ,","place":["Canada"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4966-7175","authenticated-orcid":false,"given":"Liam J","family":"Worrall","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, Centre for Blood Research, University of British Columbia 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