Borrelia burgdorferi outer surface protein (Osp) A has been used as a Lyme
disease vaccine that blocks transmission: OspA antibodies of immune hosts e
nter ticks during blood feeding and destroy spirochetes before transmission
to the host can occur. B. burgdorferi produce OspA in the gut of unfed Ixo
des scapularis ticks, and many spirochetes repress OspA production during t
he feeding process. This preferential expression suggests that OspA may hav
e an important function in the vector. Here we show that OspA mediates spir
ochete attachment to the tick gut by binding to an I. scapularis protein. T
he binding domains reside in the central region and COOH-terminus of OspA.
OspA also binds to itself, suggesting that spirochete-spirochete interactio
ns may further facilitate adherence in the gut. OspA-mediated attachment in
the tick provides a possible mechanism for how stage-specific protein expr
ession can contribute to pathogenesis during the B. burgdorferi natural cyc
le.