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**CoV RBD219-N1** is a yeast-expressed recombinant protein vaccine candidate consisting of the receptor-binding domain (RBD, residues 218-436) of the SARS-CoV spike protein, engineered in *Pichia pastoris* with deletion of the first N-glycosylation site (Asn331) for improved stability and yield. Developed by researchers at Texas Children's Hospital Center for Vaccine Development, it binds the ACE2 receptor and, when formulated with **Alhydrogel®** adjuvant at a 1:25 ratio, elicits high titers of neutralizing antibodies, providing 100% protection against lethal SARS-CoV challenge in mice with minimal pulmonary infiltrates and no detectable viral loads. It outperforms full-length spike protein and other RBD constructs in preclinical studies by minimizing eosinophilic immunopathology and enhancing Th2-biased immunity, positioning it as a scalable, safe candidate for SARS coronavirus vaccines.[1][5]
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