A tick mannose-binding lectin inhibitor interferes with the vertebrate
complement cascade to enhance transmission of the lyme disease agent.
Schuijt TJ, Coumou J, Narasimhan S, Dai J, Deponte K, Wouters D,
Brouwer M, Oei A, Roelofs JJ, van Dam AP, van der Poll T, Van't Veer C,
Hovius JW, Fikrig E
Cell Host Microbe 2011 08 18; 10 (2): 136-46
The Lyme disease agent Borrelia burgdorferi is primarily transmitted to
vertebrates by Ixodes ticks. The classical and alternative complement
pathways are important in Borrelia eradication by the vertebrate host.
We recently identified a tick salivary protein, designated P8, which
reduced complement-mediated killing of Borrelia. We now discover that P8
interferes with the human lectin complement cascade, resulting in
impaired neutrophil phagocytosis and chemotaxis and diminished Borrelia
lysis. Therefore, P8 was renamed the tick salivary lectin pathway
inhibitor (TSLPI). TSLPI-silenced ticks, or ticks exposed to
TSLPI-immune mice, were hampered in Borrelia transmission. Moreover,
Borrelia acquisition and persistence in tick midguts was impaired in
ticks feeding on TSLPI-immunized, B. burgdorferi-infected mice.
Together, our findings suggest an essential role for the lectin
complement cascade in Borrelia eradication and demonstrate how a
vector-borne pathogen co-opts a vector protein to facilitate early
mammalian infection and vector colonization.
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