Strategies for new and improved vaccines against ticks and tick‐borne diseases

Fuente, José de la; Kopáček, Petr; Lew-Tabor, A.E.; Maritz-Olivier, Christine

doi:10.1111/pim.12339

Cited by 110 publications

(104 citation statements)

References 175 publications

(220 reference statements)

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“…More recently, new technologies have made tractable approaches based on a deeper understanding of complex tick-pathogen-host interactions (de la Fuente et al, 2016a; Kuleš et al, 2016). For example, SILK (a salivary gland-expressed flagelliform protein of unknown function) and TROSPA (tick receptor for OspA localized in the gut) facilitate transmission of cattle tick-borne pathogens, Anaplasma marginale and Babesia bigemina , respectively.…”

Section: Vaccinesmentioning

confidence: 99%

Tick-Borne Viruses and Biological Processes at the Tick-Host-Virus Interface

Kazimírová

Thangamani

Bartíková

et al. 2017

Front. Cell. Infect. Microbiol.

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Ticks are efficient vectors of arboviruses, although less than 10% of tick species are known to be virus vectors. Most tick-borne viruses (TBV) are RNA viruses some of which cause serious diseases in humans and animals world-wide. Several TBV impacting human or domesticated animal health have been found to emerge or re-emerge recently. In order to survive in nature, TBV must infect and replicate in both vertebrate and tick cells, representing very different physiological environments. Information on molecular mechanisms that allow TBV to switch between infecting and replicating in tick and vertebrate cells is scarce. In general, ticks succeed in completing their blood meal thanks to a plethora of biologically active molecules in their saliva that counteract and modulate different arms of the host defense responses (haemostasis, inflammation, innate and acquired immunity, and wound healing). The transmission of TBV occurs primarily during tick feeding and is a complex process, known to be promoted by tick saliva constituents. However, the underlying molecular mechanisms of TBV transmission are poorly understood. Immunomodulatory properties of tick saliva helping overcome the first line of defense to injury and early interactions at the tick-host skin interface appear to be essential in successful TBV transmission and infection of susceptible vertebrate hosts. The local host skin site of tick attachment, modulated by tick saliva, is an important focus of virus replication. Immunomodulation of the tick attachment site also promotes co-feeding transmission of viruses from infected to non-infected ticks in the absence of host viraemia (non-viraemic transmission). Future research should be aimed at identification of the key tick salivary molecules promoting virus transmission, and a molecular description of tick-host-virus interactions and of tick-mediated skin immunomodulation. Such insights will enable the rationale design of anti-tick vaccines that protect against disease caused by tick-borne viruses.

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Section: Vaccinesmentioning

confidence: 99%

Tick-Borne Viruses and Biological Processes at the Tick-Host-Virus Interface

Kazimírová

Thangamani

Bartíková

et al. 2017

Front. Cell. Infect. Microbiol.

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“…Results using next generation sequencing technologies have advanced our understanding of the mechanisms by which A. phagocytophilum infection affects gene expression, protein content and microbiota in the vertebrate host and tick vector (Ge and Rikihisa, 2006; Sukumaran et al, 2006; de la Fuente et al, 2010, 2016a,b,c,d, 2017, Neelakanta et al, 2010; Rikihisa, 2011; Severo et al, 2012; Ayllón et al, 2013, 2015; Hajdušek et al, 2013; Villar et al, 2015a; Cabezas-Cruz et al, 2016, 2017; Gulia-Nuss et al, 2016; Abraham et al, 2017; Mansfield et al, 2017). However, less information is available on the bacterial molecules involved in pathogen infection and multiplication (Ge and Rikihisa, 2007; Huang et al, 2010; Lin et al, 2011; Troese et al, 2011; Mastronunzio et al, 2012; Oliva Chávez et al, 2015; Seidman et al, 2015; Villar et al, 2015b; Truchan et al, 2016).…”

Section: Introductionmentioning

confidence: 99%

Anaplasma phagocytophilum MSP4 and HSP70 Proteins Are Involved in Interactions with Host Cells during Pathogen Infection

Contreras

Alberdi

Mateos-Hernández

et al. 2017

Front. Cell. Infect. Microbiol.

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Anaplasma phagocytophilum transmembrane and surface proteins play a role during infection and multiplication in host neutrophils and tick vector cells. Recently, A. phagocytophilum Major surface protein 4 (MSP4) and Heat shock protein 70 (HSP70) were shown to be localized on the bacterial membrane, with a possible role during pathogen infection in ticks. In this study, we hypothesized that A. phagocytophilum MSP4 and HSP70 have similar functions in tick-pathogen and host-pathogen interactions. To address this hypothesis, herein we characterized the role of these bacterial proteins in interaction and infection of vertebrate host cells. The results showed that A. phagocytophilum MSP4 and HSP70 are involved in host-pathogen interactions, with a role for HSP70 during pathogen infection. The analysis of the potential protective capacity of MSP4 and MSP4-HSP70 antigens in immunized sheep showed that MSP4-HSP70 was only partially protective against pathogen infection. This limited protection may be associated with several factors, including the recognition of non-protective epitopes by IgG in immunized lambs. Nevertheless, these antigens may be combined with other candidate protective antigens for the development of vaccines for the control of human and animal granulocytic anaplasmosis. Focusing on the characterization of host protective immune mechanisms and protein-protein interactions at the host-pathogen interface may lead to the discovery and design of new effective protective antigens.

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“…This challenge could have been the reason for failure of the recombinant AQP1 protein as vaccine against I. ricinus [15]. Future AQP1-anti-tick vaccines therefore should at least be based on reverse vaccinology methods focusing on unique tick peptide motifs that might constitute vaccine development pipeline [47]. Peptide based vaccines use specific peptide fragments that induce high specific immune response thereby increase vaccine efficacy and reduce potential adverse effects caused by whole protein vaccination [48].…”

Section: Discussionmentioning

confidence: 99%

In Silico Analysis of Ixodid Tick Aqauporin-1 Protein as a Candidate Anti-Tick Vaccine Antigen

Ndekezi

Nkamwesiga

Ochwo

et al. 2019

Preprint

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21Ticks are arthropod vectors of pathogens of both Veterinary and Public health importance.22 Ticks are largely controlled by acaricide application. However, acaricide efficacy is hampered by 23 high cost, the need for regular application and selection of multi-acaricide resistant tick 24 populations. In light of this, future tick control approaches are poised to rely on integration of 25 rational acaricide application and other methods such as vaccination. To contribute to systematic 26 research-guided efforts to produce anti-tick vaccines, we carried out an in silico tick Aquaporin-1 27 protein (AQP1) analysis to identify unique tick AQP1 peptide motifs that can be used in future 28 peptide anti-tick vaccine development. We used multiple sequence alignment (MSA), motif 29 analysis, homology modeling, and structural analysis to identify unique tick AQP1 peptide motifs. 30 BepiPred, Chou & Fasman-Turn, Karplus & Schulz Flexibility and Parker-Hydrophilicity 31 prediction models were used to asses these motifs' abilities to induce antibody mediated immune 32 responses. Tick AQP1 (MK334178) protein homology was largely similar to the bovine AQP1 33 (PDB:1J4N) (23 % sequence similarity; Structural superimposition RMS=1.475). The highest 34 similarities were observed in the transmembrane domains while differences were observed in the 35 extra and intra cellular protein loops. Two unique tick AQP1 (MK334178) motifs, M7 (residues 36 106-125, p=5.4e-25) and M8 (residues 85-104, p=3.3e-24) were identified. These two motifs are 37 located on the extra-cellular AQP1 domain and showed the highest Parker-Hydrophilicity 38 prediction immunogenic scores of 1.153 and 2.612 respectively. The M7 and M8 motifs are a good 39 starting point for the development of potential peptide-based anti-tick vaccine. Further analyses 40 such as in vivo immunization assays are required to validate these findings. 41 42 Key words: Aquaporin-1 protein, Immunogenicity; Tick control; Peptide motifs 3 43 Background 44 Ticks are arthropod vectors of pathogens of both Veterinary and Public health concern in 45 tropical and sub-tropical regions of the world [1,2]. In 2007, the average annual cost of tick borne 46 diseases (TBDs) management was estimated to be 4.20 US Dollars per head of cattle [3]. Ticks 47 are associated with both direct and indirect constraints to livestock health and production [1,2].48 Their direct constraints to livestock production include, but are not limited to, blood loss (anemia), 49 discomfort, skin-and-hide quality loss, and tick paralysis (Fig 1) [4]. Their indirect constraints to 50 livestock production and health relate to transmission of diseases of veterinary importance 51 including: anaplasmosis (Anaplasma spp), babesiosis (Babesia spp), theileriosis (Theileria spp.), 52 and heartwater (Cowdria ruminatium) [1]. In addition, ticks transmit zoonotic pathogens belonging 53 to Babesia spp., Borrelia spp., Rickettsia spp., Ehrlichia spp., Francisella tularensis, Coxiella 54 burnetii, and viruses such as Nairovirus (Bunyaviri...

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Strategies for new and improved vaccines against ticks and tick‐borne diseases

Cited by 110 publications

References 175 publications

Tick-Borne Viruses and Biological Processes at the Tick-Host-Virus Interface

Tick-Borne Viruses and Biological Processes at the Tick-Host-Virus Interface

Anaplasma phagocytophilum MSP4 and HSP70 Proteins Are Involved in Interactions with Host Cells during Pathogen Infection

In Silico Analysis of Ixodid Tick Aqauporin-1 Protein as a Candidate Anti-Tick Vaccine Antigen

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