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Vaccines, Volume 13, Issue 1
January 2025 - 96 articles
Cover Story: Norovirus (NoV) protruding (P) domains that bind to receptors self-assemble into a 24-meric nanoparticle (P24 NP). By inserting the receptor-binding αTSR domain of the circumsporozoite protein of Plasmodium sporozoite into a surface loop of the P domain, we generated a self-assembling, chimeric P24-αTSR NP. The structural model, the P24-αTSR NP, was constructed, indicating that each P24-αTSR NP consists of a P24 NP core with 24 surface-exposed αTSR domains that retained authentic conformation and receptor binding function. The P24-αTSR NP elicited high antibody titers in mice toward both the NoV P domain and the αTSR domain of Plasmodium. The resulting antibodies bind to Plasmodium sporozoites and block NoV VLP binding to its receptors. Thus, the P24-αTSR NP may serve as a combination vaccine against both NoV and Plasmodium parasites. View this paper
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Vaccines - ISSN 2076-393X