2026-09-23T17:12:29Zhttps://ubir.buffalo.edu/oai/request

oai:ubir.buffalo.edu:10477/867242025-02-22T08:05:21Zcom_10477_77914col_10477_86252

Lyophilized, Antigen-Bound Liposomes with Reduced MPLA and Enhanced Thermostability Mabrouk, Moustafa Lovell, Jonathan Biomedical Engineering pharmaceutical sciences parasitology M.S. Improved thermostability and decreased component costs are desirable features for adjuvanted, recombinant vaccines. We previously showed that a model malaria transmission-blocking vaccine candidate antigen, Pfs25, can be rendered more immunogenic when mixed with liposomes containing cobalt porphyrin–phospholipid "CoPoP" and a synthetic monophosphoryl lipid A (MPLA) variant. CoPoP induces stable particle formation of recombinant antigen-based on interaction with the histidine tag. In the present work, different synthetic MPLA variants and concentrations were assessed in CoPoP liposomes. Long-term biophysical stability and immunogenicity were not adversely impacted by a 60 % reduction in MPLA content. When admixed with Pfs25, the adjuvant formulations effectively induced functional antibodies in immunized mice and rabbits. Lyophilized, antigen-bound liposome particles were formed using sucrose and trehalose cryoprotectants, which improved vaccine reconstitution for a variety of model antigens. Compared to liquid storage, the lyophilized Pfs25 and CoPoP liposomes exhibited thermostability with respect to size, biochemical integrity, binding capacity, protein folding and immunogenicity. Following six weeks of storage at 60 °C (the most extended storage period assessed), the lyophilized formulation induced functional antibodies in mice after immunization. **To request an accessible version of the file(s) associated with this item, contact library@buffalo.edu. Please include the item's persistent URL [http://hdl.handle.net/. . .] in your request.** 2025-02-21T21:36:52Z 2025-02-21T21:36:52Z 2020 Text Thesis http://hdl.handle.net/10477/86724 eng Users of works found in University at Buffalo Institutional Repository (UBIR) are responsible for identifying and contacting the copyright owner for permission to reuse. University at Buffalo Libraries do not manage rights for copyright-protected works and cannot assist with permissions. Copyright retained by author. application/pdf State University of New York at Buffalo