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SARS-CoV-2 LP.8.1 spike protein RBD fusion homodimer is a recombinant protein subunit vaccine candidate developed by the Finnish Institute for Health and Welfare (THL) in collaboration with the University of Helsinki. The vaccine construct consists of the receptor-binding domain (RBD) of the SARS-CoV-2 spike protein fused to a dimerization domain, typically a human IgG1 Fc fragment, which facilitates the formation of a stable homodimer. This dimeric structure is designed to enhance the immunogenicity of the RBD by increasing its size and mimicking the multivalent display of antigens, thereby promoting a more robust B-cell response and the production of high-titer neutralizing antibodies. LP.8.1 is intended for the prevention of COVID-19 infection and has demonstrated potent neutralizing activity against multiple SARS-CoV-2 variants in preclinical studies.
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