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Exploring the Sialomes of Ticks

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Short Views on Insect Genomics and Proteomics

Part of the book series: Entomology in Focus ((ENFO,volume 4))

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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. 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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