Tick Histamine-Binding Proteins

Paesen, Guido C.; Adams, Peter L.; Harlos, K.; Nuttall, Patricia A.; Stuart, David I.

doi:10.1016/s1097-2765(00)80359-7

Cited by 289 publications

(139 citation statements)

References 39 publications

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“…In addition, preliminary experiments using affinity chromatography with histamine-bound agarose gel suggested that Equ c 1 may bind histamine, 2 a mediator released by basophils and mast cells, which plays a crucial role in allergy. Such a ligand has been described for other lipocalins like those found in the saliva of the blood-feeding insect Rhodnius prolixus (37) and Rhipicephalus appendiculatus ticks (38). However, the specificity of the horse allergen for histamine needs to be confirmed, because the hydrophilic nature of the ligand has no counterpart within the hydrophobic binding site of Equ c 1, and soaking trials of Equ c 1 crystals with various lipocalin ligands (including histamine) were inconclusive.…”

Section: Discussionmentioning

confidence: 99%

Crystal Structure of the Allergen Equ c 1

Lascombe¹,

Grégoire²,

Poncet³

et al. 2000

Journal of Biological Chemistry

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The three-dimensional structure of the major horse allergen Equ c 1 has been determined at 2.3 Å resolution by x-ray crystallography. Equ c 1 displays the typical fold of lipocalins, a ␤-barrel flanked by a C-terminal ␣-helix. The space between the two ␤-sheets of the barrel defines an internal cavity that could serve, as in other lipocalins, for the binding and transport of small hydrophobic ligands. Equ c 1 crystallizes in a novel dimeric form, which is distinct from that observed in other lipocalin dimers and corresponds to the functional form of the allergen. Binding studies of point mutants of the allergen with specific monoclonal antibodies raised in mouse and IgE serum from horse allergic patients allowed to identify putative B cell antigenic determinants. In addition, total inhibition of IgE serum recognition by a single specific monoclonal antibody revealed the restricted nature of the IgE binding target on the molecular surface of Equ c 1.The incidence of allergic diseases is increasing in developed countries resulting from growing exposure to allergens, altered stimulation of the immune system during development, and probably facilitating an adjuvant effect of the environment. Allergy to animals is distinguishable by its intensity and the possibility of sensitization by a limited contact with danders or hair. The animals responsible for allergy are obviously familiar domestic cats and dogs, but also the horse, which is often incriminated. Five main horse allergens have been isolated and purified (1, 2). Among these, the Equ c 1 protein (molecular mass 21.5 kDa, 187 amino acids, pI ϭ 4.5) has been defined as a major allergen, because it induces an IgE-mediated type I allergic reaction in a majority of the patients allergic to horses.Equ c 1 belongs to the lipocalin family (3, 4). Although members of this family display low sequence similarity (often lower than 20% of amino acid identities), all share a conserved folding pattern, an 8-stranded ␤-barrel flanked by an ␣-helix at the C-terminal end of the polypeptide chain. The lipocalin ␤-barrel often defines a central apolar cavity that serves for the binding and transport of small hydrophobic molecules such as retinol (retinol-binding protein (5, 6)), odorant molecules (bovine odorant-binding protein (7, 8)), or pheromones (mouse major urinary protein, mMUP 1 (9), and rat urinary ␣2-globulin (10)). Several lipocalins have been described as allergenic proteins, among which the mouse major urinary protein mMUP (11), rat urinary ␣2-globulin rat urinary ␣2-globulin (12), bovine ␤-lactoglobulin (13), cockroach allergen Bla g 4 (14), dog allergens Can f 1 and Can f 2 (15), and bovine allergen Bos d 2 (16).Whether a protein exhibits special structural characteristics that are responsible for its allergenic properties is an issue that remains poorly understood. Although the three-dimensional structures of some allergenic lipocalins are known (mMUP (9), rat urinary ␣2-globulin (10), bovine ␤-lactoglobulin (17, 18), and Bos d 2 (19)), little information is availa...

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Section: Discussionmentioning

confidence: 99%

Crystal Structure of the Allergen Equ c 1

Lascombe¹,

Grégoire²,

Poncet³

et al. 2000

Journal of Biological Chemistry

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“…At the time of crystallization of monomine, the closest related sequence for which a structure existed in the data base was that for female-specific histamine-binding protein (FS-HBP2) from the hard tick Rhipicephalus appendiculatus (3). Due to the low sequence similarity to FS-HBP2 (16% sequence identity) it was considered improbable that molecular replacement would work.…”

Section: Methodsmentioning

confidence: 99%

“…Thus far, scavengers of biogenic amines have evolved independently in assassin bugs, mosquitoes, and ticks, and this will probably hold for other bloodfeeders as well (2)(3)(4)(5). This is in part due to the myriad effects that biogenic amines have during host defenses against blood loss and parasite invasion.…”

mentioning

confidence: 99%

“…In some ticks, histamine and 5-HT are known to be scavenged by members of the lipocalin protein family (3,9). Lipocalins are highly abundant proteins in both hard and soft tick salivary glands with large numbers of paralogous genes in each lineage (10,11).…”

mentioning

confidence: 99%

“…It has been argued that because hard ticks remain attached to their hosts over a long period of feeding, anti-inflammatory mechanisms, such as histamine antagonism are necessary to prevent host rejection (3). However, blood-feeders with shorter feeding times also contain biogenic amine scavenging proteins, suggesting that this mechanism is generally essential for successful feeding (2,4,5).…”

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confidence: 99%

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Structure, Function, and Evolution of Biogenic Amine-binding Proteins in Soft Ticks

Mans

Ribeiro

Andersen

2008

Journal of Biological Chemistry

158

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Two highly abundant lipocalins, monomine and monotonin, have been isolated from the salivary gland of the soft tick Argas monolakensis and shown to bind histamine and 5-hydroxytryptamine (5-HT), respectively. The crystal structures of monomine and a paralog of monotonin were determined in the presence of ligands to compare the determinants of ligand binding. Both the structures and binding measurements indicate that the proteins have a single binding site rather than the two sites previously described for the female-specific histaminebinding protein (FS-HBP), the histamine-binding lipocalin of the tick Rhipicephalus appendiculatus. The binding sites of monomine and monotonin are similar to the lower, low affinity site of FS-HBP. The interaction of the protein with the aliphatic amine group of the ligand is very similar for the all of the proteins, whereas specificity is determined by interactions with the aromatic portion of the ligand. Interestingly, protein interaction with the imidazole ring of histamine differs significantly between the low affinity binding site of FS-HBP and monomine, suggesting that histamine binding has evolved independently in the two lineages. From the conserved features of these proteins, a tick lipocalin biogenic amine-binding motif could be derived that was used to predict biogenic amine-binding function in other tick lipocalins. Heterologous expression of genes from salivary gland libraries led to the discovery of biogenic amine-binding proteins in soft (Ornithodoros) and hard (Ixodes) tick genera. The data generated were used to reconstruct the most probable evolutionary pathway for the evolution of biogenic amine-binding in tick lipocalins.Hemostasis (blood clotting, platelet aggregation, and vasoconstriction) and immunity (inflammation, pain, and adaptive immunity) are the primary ways that the vertebrate host can respond against parasitic invasion and subsequent blood loss caused by blood-feeding arthropods. Hematophagous arthropods modulate these defenses by secreting a pharmacological mixture of bioactive components in their saliva during feeding. Most blood-feeders will have at least an anti-clotting, antiplatelet, and vasodilatory component in their salivary arsenal (1).This classic paradigm of blood-feeding strategy can be extended to include anti-inflammatory proteins that scavenge biogenic amines, as their presence in all blood-feeding arthropods is becoming apparent. Thus far, scavengers of biogenic amines have evolved independently in assassin bugs, mosquitoes, and ticks, and this will probably hold for other bloodfeeders as well (2)(3)(4)(5). This is in part due to the myriad effects that biogenic amines have during host defenses against blood loss and parasite invasion.5-Hydroxytryptamine (5-HT) 2 (or serotonin) is secreted by platelets and thrombocytes, as well as mast cells of many mammals, and functions to increase vascular permeability as well as inducing platelet aggregation and vasoconstriction (6). Histamine is released by activated mast cells and basophils and...

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Identification of putative proteins involved in granule biogenesis of tick salivary glands

et al. 2001

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Ticks secrete bioactive components during feeding that assist them in gaining a blood meal. Compounds secreted are stored in granules until a stimulus induces secretion during feeding. Biogenesis of tick secretory granules has not been investigated before. An adequate understanding of granule biogenesis could advance our understanding of tick salivary gland biology and could aid in the rational design of tick control methods. Putative tick salivary gland proteins 1-4 (TSGP1-4) involved in granule biogenesis were identified in this study based on their abundance in salivary gland extracts and granule preparations and their ability to aggregate under conditions of slight acidity and high calcium concentration. TSGP2 and TSGP3 have been identified as previously described toxic and nontoxic homologues, respectively, while toxicity was also associated with TSGP4.

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Tick Histamine-Binding Proteins

Cited by 289 publications

References 39 publications

Crystal Structure of the Allergen Equ c 1

Crystal Structure of the Allergen Equ c 1

Structure, Function, and Evolution of Biogenic Amine-binding Proteins in Soft Ticks

Identification of putative proteins involved in granule biogenesis of tick salivary glands

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