Abstract
Ticks (Acarina) are obligate blood-feeding arthopods that vector human and animal pathogens, causing typhus, Lyme disease, Rocky Mountain spotted fever, tick-borne relapsing fever, babesiosis, Q fever, arboviruses, anaplasmosis, and ehrlichiosis. Among the specializations required for this peculiar diet, tick saliva, a fluid once believed to be relevant only for lubrication of mouthparts and water balance, is now well known to be a cocktail of potent antihemostatic, anti-inflammatory, and immunomodulatory molecules that helps these arthropods obtain a blood meal from their vertebrate hosts. The repertoire of pharmacologically active components in this cocktail is impressive as well as the number of targets they specifically affect. These salivary components change the physiology of the host at the bite site, and, consequently, some pathogens transmitted by ticks take advantage of this change and become more infective. Tick salivary proteins have therefore become an attractive target to control tick-borne diseases. Recent advances in molecular biology, protein chemistry, and computational biology are accelerating the isolation, sequencing, and analysis of a large number of transcripts and proteins from the saliva of different ticks. Many of these newly isolated genes code for proteins with homology to known proteins allowing identification or prediction of their function. These and other molecules from genome and proteome sequences offer an exciting possibility to identify new vaccine antigens, potential biopharmaceuticals, antimicrobial peptides, and other novel human therapeutics.
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Notes
- 1.
The Viperidae (vipers) are a family of venomous snakes found all over the world, except in Antarctica, Australia, New Zealand, Ireland, Madagascar, Hawaii, various other isolated islands, and north of the Arctic Circle.
Abbreviations
- ADP:
-
Adenosine diphosphate
- APTT:
-
Activated partial thromboplastin time
- ATP:
-
Adenosine triphosphate
- BIP:
-
B-cell inhibitory proteins
- BmAP:
-
Boophilus microplus anticoagulant protein
- BmTI-A:
-
Rhipicephalus microplus trypsin inhibitor-A
- BPTI–Kunitz:
-
Basic protease inhibitor–Kunitz type
- cAMP:
-
Cyclic adenosine monophosphate
- Dc:
-
Dendritic cell
- ECM:
-
Extracellular matrix
- ETC:
-
Extrinsic tenase complex
- FIXa:
-
Factor IXa
- FVIII:
-
Factor VIII
- FX:
-
Factor X
- FXa:
-
Factor Xa
- GP IIb–IIIa:
-
Glycoprotein IIb–IIIa
- IC50 :
-
The concentration of an inhibitor where the response (or binding) is reduced by half
- IFN:
-
Interferon
- IL:
-
Interleukin
- Ir-CPI:
-
Ixodes ricinus contact phase inhibitor
- IRS-2:
-
I. ricinus serine proteinase inhibitor (serpin)
- Isac:
-
I. scapularis anticomplement
- ISL929:
-
Ixodes scapularis salivary proteins
- MIF:
-
Macrophage migration inhibitory factor
- NCBI:
-
National Center for Biotechnology Information
- NK:
-
Natural killer
- OmCI:
-
Ornithodoros moubata complement inhibitor
- PGE2:
-
Prostaglandin E2
- PGF2a:
-
Prostaglandin F2
- PT:
-
Prothrombin time
- RaHBP:
-
Rhipicephalus appendiculatus histamine-binding salivary protein
- Salp:
-
Salivary protein
- SAT:
-
Saliva-assisted transmission
- SG:
-
Salivary gland
- SGE:
-
Salivary gland extract
- SHBP:
-
serotonin- and histamine- binding protein
- TAI:
-
Tick adhesion inhibitor
- TAP:
-
Tick anticoagulant peptide
- TdPI:
-
Tick-derived protease inhibitor
- TF:
-
Tissue factor
- tHRF:
-
Tick histamine release factor
- TT:
-
Thrombin time
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M’ghirbi, Y. (2016). Exploring the Sialomes of Ticks. In: Raman, C., Goldsmith, M., Agunbiade, T. (eds) Short Views on Insect Genomics and Proteomics. Entomology in Focus, vol 4. Springer, Cham. https://doi.org/10.1007/978-3-319-24244-6_1
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