{
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      "official_url": "https:\/\/pmc.ncbi.nlm.nih.gov\/articles\/PMC12797234\/",
      "rev_number": 7,
      "creators": [
        {
          "name": {
            "lineage": null,
            "given": "Simran",
            "honourific": null,
            "family": "Srivastava"
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        {
          "name": {
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            "given": "Sahil",
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            "family": "Kumar"
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        {
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            "family": "Mishra"
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        {
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            "given": "Raju S",
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            "family": "Rajmani"
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        {
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            "given": "Randhir",
            "honourific": null,
            "family": "Singh"
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        },
        {
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            "given": "Somnath",
            "honourific": null,
            "family": "Dutta"
          }
        },
        {
          "name": {
            "lineage": null,
            "given": "Rajesh Prakash",
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            "family": "Ringe"
          }
        },
        {
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            "given": "Raghavan",
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      "dir": "disk0\/00\/00\/34\/87",
      "keywords": "SARS-CoV-2; coronavirus; efficacy; lyophilized; preparedness; protein-subunit; thermostability; yield",
      "lastmod": "2026-07-22 01:03:53",
      "ispublished": "pub",
      "pagerange": "104-118",
      "publisher": "American Chemical Society (ACS)",
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      "uri": "http:\/\/crdd.osdd.net\/open\/id\/eprint\/3487",
      "note": "Copyright of this article belongs to American Chemical Society (ACS)",
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      "contact_email": "kps.sengar@csir.res.in",
      "publication": "ACS Infect. Dis.",
      "abstract": "Zoonotic spillover of sarbecoviruses to humans resulted in the SARS-CoV-1 outbreak in 2003 and the current COVID-19 pandemic caused by SARS-CoV-2. In both cases, the viral spike protein (S) is the principal target of neutralizing antibodies that prevent infection. Within the spike, the immunodominant receptor-binding domain (RBD) is the primary target of neutralizing antibodies in COVID-19 convalescent sera and vaccine recipients. We have constructed stabilized RBD derivatives of different sarbecoviruses: SARS-CoV-1 (Clade 1a), WIV-1 (Clade 1a), RaTG13 (Clade 1b), RmYN02 (Clade 2), and BtKY72 (Clade 3). Stabilization enhanced yield by 3-23-fold. The RBD derivatives were conformationally intact, as assayed by binding to multiple broadly neutralizing antibodies. The stabilized RBDs show significant enhancement in apparent Tm, exhibit resistance to a 2-h incubation at temperatures up to 60 °C in PBS in contrast to the corresponding WT RBDs, and show prolonged stability of over 15 days at 37 °C after lyophilization. In mice immunizations, both stabilization and trimerization significantly enhanced elicited neutralization titers by �100-fold. The stabilized RBD cocktail elicited highly neutralizing titers against both homologous and heterologous pseudoviruses. The immunogenicity of the vaccine formulation was assessed in both na\\\"\\ive and SARS-CoV-2 preimmunized mice, revealing an absence of immune imprinting, thus indicating its suitability for use in future sarbecovirus-origin epidemics or pandemics.",
      "type": "article",
      "title": "Development of a thermostable and broadly neutralizing pan-sarbecovirus vaccine candidate"
    }