A high affinity serotonin- and histamine-binding lipocalin from tick saliva.
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 beta-barrels with two internal binding sites: a high-affinity (H) site for histamine and a site (L) for which the natural ligand is unkn...
| Main Authors: | , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
2002
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| _version_ | 1826263269568937984 |
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| author | Sangamnatdej, S Paesen, G Slovak, M Nuttall, P |
| author_facet | Sangamnatdej, S Paesen, G Slovak, M Nuttall, P |
| author_sort | Sangamnatdej, S |
| collection | OXFORD |
| description | 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 beta-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. |
| first_indexed | 2024-03-06T19:49:04Z |
| format | Journal article |
| id | oxford-uuid:23552aa1-79d3-4824-a89d-45bdf2f8fa58 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T19:49:04Z |
| publishDate | 2002 |
| record_format | dspace |
| spelling | oxford-uuid:23552aa1-79d3-4824-a89d-45bdf2f8fa582022-03-26T11:43:49ZA high affinity serotonin- and histamine-binding lipocalin from tick saliva.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:23552aa1-79d3-4824-a89d-45bdf2f8fa58EnglishSymplectic Elements at Oxford2002Sangamnatdej, SPaesen, GSlovak, MNuttall, PTo overcome the inflammatory response in its host, the cattle-feeding, brown ear tick secretes histamine-binding proteins into the feeding site. These proteins are beta-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. |
| spellingShingle | Sangamnatdej, S Paesen, G Slovak, M Nuttall, P A high affinity serotonin- and histamine-binding lipocalin from tick saliva. |
| title | A high affinity serotonin- and histamine-binding lipocalin from tick saliva. |
| title_full | A high affinity serotonin- and histamine-binding lipocalin from tick saliva. |
| title_fullStr | A high affinity serotonin- and histamine-binding lipocalin from tick saliva. |
| title_full_unstemmed | A high affinity serotonin- and histamine-binding lipocalin from tick saliva. |
| title_short | A high affinity serotonin- and histamine-binding lipocalin from tick saliva. |
| title_sort | high affinity serotonin and histamine binding lipocalin from tick saliva |
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