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Ixodes Scapularis tick saliva proteins sequentially secreted every 24h during blood feeding

ABSTRACT: Ixodes scapularis is the most medically important tick species and transmits five of the 14 reportable human tick borne diseases (TBD) in the USA. This study describes LC-MS/MS identification of 582 tick- and 83 rabbit proteins in saliva of I. scapularis ticks that fed for 24, 48, 72, 96, and 120h, those that engorged but were not detached from the host (BD), and replete fed and detached (SD).

INSTRUMENT(S): Q Exactive

ORGANISM(S): Ixodes Scapularis (black-legged Tick) (deer Tick)

TISSUE(S): Saliva

SUBMITTER: Albert Mulenga

LAB HEAD: Albert Mulenga

PROVIDER: PXD003214 | Pride | 2015-12-11

REPOSITORIES: Pride

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			Action	DRS
	UniProt_Ixodes_Rabbit_patternlab_09-02-2014_reversed.fasta	Fasta
	YRC_Mulenga_20140418_1_Ixodes_24h_1.raw	Raw
	YRC_Mulenga_20140418_1_Ixodes_24h_1.sepr	Other
	YRC_Mulenga_20140418_1_Ixodes_24h_1.sqt	Other
	YRC_Mulenga_20140418_1_Ixodes_24h_1.txt	Txt

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Publications

Ixodes scapularis Tick Saliva Proteins Sequentially Secreted Every 24 h during Blood Feeding.

Kim Tae Kwon TK Tirloni Lucas L Pinto Antônio F M AF Moresco James J Yates John R JR da Silva Vaz Itabajara I Mulenga Albert A

PLoS neglected tropical diseases 20160111 1

Ixodes scapularis is the most medically important tick species and transmits five of the 14 reportable human tick borne disease (TBD) agents in the USA. This study describes LC-MS/MS identification of 582 tick- and 83 rabbit proteins in saliva of I. scapularis ticks that fed for 24, 48, 72, 96, and 120 h, as well as engorged but not detached (BD), and spontaneously detached (SD). The 582 tick proteins include proteases (5.7%), protease inhibitors (7.4%), unknown function proteins (22%), immunity ...[more]

PMID: 26751078

Publication: 1/2

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Borrelia burgdorferi infected Ixodes scapularis nymph saliva proteome

Project description:Lyme disease (LD) is one of the most important human vector-borne diseases in North America. Since transmission of Borrelia burgdorferi (Bb), the causative agent of LD, is influenced by yet unknown tick saliva proteins (TSP), the discovery and characterization of such TSPs are highly sought after for their potential as tick-antigen based vaccine targets. We validated a novel non-invasive approach of collecting sufficient amounts of saliva from unfed, partially fed (12, 24, 36, 48, 60, and 72h), and replete fed Ixodes scapularis nymphs for identification of tick saliva proteins using the LC-MS/MS approach. Our data has described TSPs that might be injected into the host within few hours of the tick starting to feed and are likely associated with manipulating host immunity to facilitate transmitted Bb to colonize the host. Thus, these data will serve as a source for Bb-infection associated TSPs that might be targeted in tick-antigen based vaccines to prevent LD. Equally important, the non-invasive method to collect nymph tick saliva is likely to provide transformative impact on research to understand transmission of other TBD agents.

2021-09-10 | PXD023940 | Pride

Tick host range adaptation: changes in protein profiles in Ixodes scapularis and Amblyomma americanum saliva during stimulation to feed on different hosts

Project description:Understanding the molecular basis of how the tick adapts to feed on different animal hosts is central to understanding tick and tick-borne disease (TBD) epidemiology. Tick adaptation to feed on vertebrate hosts is regulated by tick secretion of multiple tick saliva proteins (TSPs) and other molecules that regulate tick feeding. This study was initiated to determine if ticks such as Ixodes scapularis and Amblyomma americanum that are adapted to feed on multiple hosts utilized the same sets of proteins to accomplish feeding on all hosts. Our data suggest that ticks of the same species differentially express proteins when feeding on diffent hosts. SDS-PAGE and silver staining analysis revealed unique protein eletrophoretic profile in saliva of Ixodes scapularis and Amblyomma americanum that were stimulated to start feeding on different hosts: rabbits, humans, and dogs. LC-MS/MS sequencing and pairwise analysis of proteins in saliva of I. scapularis and A. americanum ticks that were non-stimulated and those that were stimulated to feed on rabbits, dogs, or humans identified TSPs that were unique to each treatment and those that were common. Overal, we identified a total of 276 and 340 non-redundant I. scapularis and A. americanum TSPs, which we have classified into 28 functional classes that include secreted conserved proteins (unknown functions), proteinase inhibitors, lipocalins, extracellular matrix/cell adhesion, heme/iron metabolism, signal transduction and immunity-related proteins being the most predominant in saliva of unfed ticks. With exception of Rhipicephalus microplus, anti-tick vaccine research relies on feeding lab animals. Data here suggest that lab animal data could result in prioritizing irrelevant targets as some tick genes are unique to ticks fed on lab animals. This study provides the platform that could be utilized to identify relevant target anti-tick vaccine antigens, and will facilitate early stage tick feeding research.

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Identification and characterization of proteins that form the inner core Ixodes scapularis tick attachment cement layer.

Project description:Ixodes scapularis and other hard ticks are long-term blood feeders. This feeding behavior is facilitated by a tick secreted bio adhesive (tick cement) that attaches tick mouthparts to skin tissue and prevents the host from dislodging the tick from its feeding site. Understanding tick cement formation is highly sought after as its disruption will prevent tick feeding. This study describes proteins that form the inner core layer of I. scapularis tick cement as disrupting these will stop formation of the outer cortical layer. As the inner core cement layer completes forming by 24 h of attachment, we used laser capture to isolate cement from cryosections of 6 h and 24 h tick attachment sites and to distinguish between early and late inner core cement proteins. LC-MS/MS analysis identified 138 tick cement proteins (TCPs) of which 37 and 35 were unique in cement of 6 and 24 h respectively, and 66 shared proteins. The 138 TCPs are classified in 14 functional categories: cuticular protein (16%), tick specific proteins of unknown function, cytoskeletal proteins, and enzymes (at 13% each), enzymes (10%), antioxidant, glycine rich, scaffolding, heat shock, histone, histamine binding, proteases and protease inhibitors, and miscellaneous (at 3-6% each). Gene ontology analysis confirm that TCPs are enriched for bio adhesive properties. Our data offer insights into yet unknown tick cement bonding patterns and set the foundation for understanding the molecular basis of I. scapularis tick cement formation.

2023-03-11 | PXD038685 | Pride

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