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Immunogenicity of the Lyme disease antigen OspA, particleized by cobalt porphyrin-phospholipid liposomes

Vaccine. 2020; 
Federizon J, Frye A, Huang WC, Hart TM, He X, Beltran C, Marcinkiewicz AL, Mainprize IL, Wills MKB, Lin YP, Lovell JF.
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ORF cDNA Clones/MolecularCloud … 22 Protein expression and purification The DNA sequence encoding for non-lipidated OspA (B burgdorferi B31, Supplementary Fig S1) was synthesized into a pET21a plasmid by Genscript, which was transformed into BL21 (DE3) competent Escherichia coli cells … Get A Quote

摘要

Outer surface protein A (OspA) is a Borrelia lipoprotein and an established Lyme disease vaccine target. Admixing non-lipidated, recombinant B. burgdorferi OspA with liposomes containing cobalt porphyrin-phospholipid (CoPoP) resulted in rapid, particulate surface display of the conformationally intact antigen. Particleization was serum-stable and led to enhanced antigen uptake in murine macrophages in vitro. Mouse immunization using CoPoP liposomes that also contained a synthetic monophosphoryl lipid A (PHAD) elicited a Th1-biased OspA antibody response with higher IgG production compared to other vaccine adjuvants. Antibodies were reactive with intact B. burgdorferi spirochetes and Borrelia lysates, and induce... More

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