Exploring the Sialomes of Ticks

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

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.

Keywords

Sialomes Ticks Acarina Sialotranscriptome Sialoproteome Pharmacologically active components 

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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© Springer International Publishing Switzerland 2016

Authors and Affiliations

  1. 1.Laboratory of Veterinary Microbiology and Epidemiology, Service of Medical Entomology, Institute Pasteur of TunisUniversity of Tunis El-ManarTunisTunisia

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