OUTER SURFACE PROTEIN-C (OSPC), BUT NOT P39, IS A PROTECTIVE IMMUNOGEN AGAINST A TICK-TRANSMITTED BORRELIA-BURGDORFERI CHALLENGE - EVIDENCEFOR A CONFORMATIONAL PROTECTIVE EPITOPE IN OSPC
Rd. Gilmore et al., OUTER SURFACE PROTEIN-C (OSPC), BUT NOT P39, IS A PROTECTIVE IMMUNOGEN AGAINST A TICK-TRANSMITTED BORRELIA-BURGDORFERI CHALLENGE - EVIDENCEFOR A CONFORMATIONAL PROTECTIVE EPITOPE IN OSPC, Infection and immunity, 64(6), 1996, pp. 2234-2239
Outbred mice were immunized with the soluble fraction of a crude Esche
richia coli lysate containing either recombinant outer surface protein
C (OspC) or P39 of Borrelia burgdorferi B31 (low passage). Following
seroconversion, the mice were challenged with an infections dose of B.
burgdorferi B31 via the natural transmission mode of tick bite. Three
mice immunized with P39 were not protected; however, all 12 of the re
combinant OspC-immunized mice were protected from infection as assayed
by culture and serology. Although OspC has been shown to be a protect
ive immunogen against challenge with in vitro-cultured borrelia admini
stered by needle, this study is the first to demonstrate OspC effectiv
eness against tick-borne spirochetes. Following feeding, all ticks sti
ll harbored B. burgdorferi, suggesting that the mechanism of protectio
n is not linked to destruction of the infectious spirochete within the
tick. In a separate experiment, groups of four mice were immunized wi
th protein fractions from B. burgdorferi B31 purified by preparative g
el electrophoresis in an attempt to identify potential protective anti
gens. Many of these mice developed high-titer-antibody responses again
st OspC, but curiously the mice were susceptible to B. burgdorferi inf
ection via tick bite. These results suggest that the protective epitop
e(s) on OspC is heat sensitive/conformational, a finding which has imp
lications in vaccine development.