Journal
INSECT MOLECULAR BIOLOGY
Volume 16, Issue 4, Pages 469-479Publisher
BLACKWELL PUBLISHING
DOI: 10.1111/j.1365-2583.2007.00742.x
Keywords
Ixodes scapularis; tick salivary proteins; Salp20; anti-complement proteins; Borrelia burgdorferi
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Funding
- NIAID NIH HHS [5U01AI058263-04] Funding Source: Medline
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Ixodes ticks are vectors of several pathogens including Borrelia burgdorferi. Tick saliva contains numerous molecules that facilitate blood feeding without host immune recognition and rejection. We have expressed, purified, and characterized Ixodes scapularis salivary protein 20 (Salp20), a potential inhibitor of the alternative complement pathway that shares homology with the Isac protein family. When analysed by SDS-PAGE and size exclusion chromatography, Salp20 was approximately 48 kDa, more than double its predicted mass, primarily due N- and O-linked glycosylations. Recombinant Salp20 inhibited the alternative complement pathway by dissociating the C3 convertase, and partially protected a serum sensitive species of Borrelia from lysis by normal human serum. We propose that Salp20 facilitates tick feeding and possibly protects tick-borne pathogens from complement components.
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