Please use this identifier to cite or link to this item: http://localhost:80/xmlui/handle/123456789/1485
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dc.contributor.authorBiswal, Bichitra Kumar
dc.contributor.authorSrichandan, Sudeepa
dc.contributor.authorMeena, Jairam
dc.contributor.authorPanda, Amulya K
dc.contributor.authorAhuja, Rahul
dc.date.accessioned2025-01-29T10:49:02Z
dc.date.accessioned2025-01-29T10:50:11Z
dc.date.available2025-01-29T10:49:02Z
dc.date.available2025-01-29T10:50:11Z
dc.date.issued2023
dc.identifier.urihttp://hdl.handle.net/123456789/1485
dc.description.abstractReceptor binding domain (RBD) of SARS-CoV-2 is a prime vaccine target against which neutralizing antibody responses are directed. Purified RBD as a vaccine candidate warrants administration of multiple doses along with adjuvants and use of delivery systems to improve its immunogenicity. The present investigation examines the immunogenicity of RBD delivered by biodegradable polymer particles from single dose administration. Mice upon single point immunization of RBD entrapped microparticles generated improved antibody response. The polymer microparticles showed better temperature stability and could be stored at 37 degrees for one month without any considerable loss of immunogenicity. Further, immunization with microparticles could elicit memory antibody response upon challenge after four months of single dose administration. Thus, using microparticles entrapping RBD as a vaccine candidate confer improved immunogenicity, temperature stability and recall response. These thermostable microparticles seem to be a potentially cost-effective approach which can help in dose reduction, provide a wider access of vaccines and accelerate the end of global pandemic.en_US
dc.language.isoenen_US
dc.publisherElsevier Incen_US
dc.subjecten_US
dc.titleImmunogenicity Evaluation of Thermostable Microparticles Entrapping Receptor Binding Domain of SARS-CoV-2 by Single Point Administrationen_US
dc.typeArticleen_US
dc.journalJ Pharm Scien_US
dc.volumeno112en_US
dc.issueno(6)en_US
dc.pages1664-1670en_US
Appears in Collections:Protein Crystallography, Publications

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