Immunogenicity of the Lyme disease antigen OspA, particleized by cobalt porphyrin-phospholipid liposomes. Issue 4 (22nd January 2020)

• Record Type: Journal Article
• Authors: Federizon, Jasmin; Frye, Amber; Huang, Wei-Chiao; Hart, Thomas M.; He, Xuedan; Beltran, Christopher; Marcinkiewicz, Ashley L.; Mainprize, Iain L.; Wills, Melanie K.B.; Lin, Yi-Pin; Lovell, Jonathan F.
• Is Part Of: Vaccine. Volume 38:Issue 4(2020)
• Page Start: 942
• Page End: 950
• Publication Date: 2020-01-22
• Subjects: Liposomes -- Adjuvant -- Particle vaccine -- Lyme disease -- OspA; Vaccines -- Periodicals; 615.372
• DOI: 10.1016/j.vaccine.2019.10.073
• Languages: English
• ISSNs: 0264-410X

Abstract

Highlights: Recombinant OspA spontaneously and stably binds to liposomes containing cobalt porphyrin-phospolipid (CoPoP). Particleized OspA is effectively taken by macrophages in vitro . In mice, OspA is more immunogenic when admixed with CoPoP liposomes, relative to other adjuvants. Induced antibodies recognize spirochetes and have complement-mediated borreliacidal activity. A year after immunization, mice retain antibodies that block spirochete transmission in a feeding chamber. Abstract: 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 induced complement-mediated borreliacidal activity in vitro . One year after initial immunization, mice maintained high levels of circulating borreliacidal antibodies capable of blocking B. burgdorferi transmission from infected ticks to human blood in a feeding chamber.