A high affinity serotonin- and histamine-binding lipocalin from tick saliva
Sangamnatdej, S.; Paesen, G.C.; Slovak, M.; Nuttall, P.A.. 2002 A high affinity serotonin- and histamine-binding lipocalin from tick saliva. Insect Molecular Biology, 11 (1). 79-86. 10.1046/j.0962-1075.2001.00311.xFull text not available from this repository.
To overcome the inflammatory response in its host, the cattle-feeding, brown ear tick secretes histamine-binding proteins into the feeding site. These proteins are β-barrels with two internal binding sites: a high-affinity (H) site for histamine and a site (L) for which the natural ligand is unknown. Here we report a related protein (SHBP), secreted by a rodent- and cattle-feeding tick, that traps both histamine and serotonin. The histamine-binding H site is well conserved in SHBP, whereas residue changes in the L-like site are consistent with binding of the bulkier serotonin molecule. As histamine is a key inflammatory mediator in cattle, while serotonin takes on this role in rodents, the diversification of these tick proteins may reflect host adaptation
|Programmes:||CEH Programmes pre-2009 publications > Other|
|CEH Sections:||_ Molecular Virology & Parasitology|
|NORA Subject Terms:||Biology and Microbiology|
|Date made live:||04 Oct 2012 09:22|
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