Apyrase with anti-platelet aggregation activity from the nymph of the camel tick Hyalomma dromedarii

Masoud, Hassan M. M.; Helmy, Mohamed S.; Darwish, Doaa A.; Abdel-Monsef, Mohamed M.; Ibrahim, Mona E.

doi:10.1007/s10493-020-00471-9

Cited by 10 publications

(6 citation statements)

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“…Apyrase has been identified in the saliva of most haematophagous vectors, including soft and hard ticks. This enzyme hydrolyses ATP and ADP to AMP, and prevents platelet and neutrophil aggregation and thrombus formation, thus facilitating blood feeding [ 47 , 48 ]. A recombinant form of the salivary apyrase of O. moubata induced protective, strong humoral responses in animal vaccine trials that reduced tick feeding and survival [ 47 ].…”

Section: Resultsmentioning

confidence: 99%

Proteomics informed by transcriptomics for a qualitative and quantitative analysis of the sialoproteome of adult Ornithodoros moubata ticks

et al. 2021

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Background The argasid tick Ornithodoros moubata is the main vector in mainland Africa of African swine fever virus and the spirochete Borrelia duttoni, which causes human relapsing fever. The elimination of populations of O. moubata would contribute to the prevention and control of these two serious diseases. Anti-tick vaccines are an eco-friendly and sustainable means of eliminating tick populations. Tick saliva forms part of the tick-host interface, and knowledge of its composition is key to the identification and selection of vaccine candidate antigens. The aim of the present work is to increase the body of data on the composition of the saliva proteome of adult O. moubata ticks, particularly of females, since in-depth knowledge of the O. moubata sialome will allow the identification and selection of novel salivary antigens as targets for tick vaccines. Methods We analysed samples of female and male saliva using two different mass spectrometry (MS) approaches: data-dependent acquisition liquid chromatography-tandem MS (LC–MS/MS) and sequential window acquisition of all theoretical fragment ion spectra–MS (SWATH-MS). To maximise the number of proteins identified, a proteomics informed by transcriptomics analysis was applied using the O. moubata salivary transcriptomic dataset previously obtained by RNA-Seq. Results SWATH-MS proved to be superior to LC–MS/MS for the study of female saliva, since it identified 61.2% more proteins than the latter, the reproducibility of results was enhanced with its use, and it provided a quantitative picture of salivary components. In total, we identified 299 non-redundant proteins in the saliva of O. moubata, and quantified the expression of 165 of these in both male and female saliva, among which 13 were significantly overexpressed in females and 40 in males. These results indicate important quantitative differences in the saliva proteome between the sexes. Conclusions This work expands our knowledge of the O. moubata sialome, particularly that of females, by increasing the number of identified novel salivary proteins, which have different functions at the tick–host feeding interface. This new knowledge taken together with information on the O. moubata sialotranscriptome will allow a more rational selection of salivary candidates as antigen targets for tick vaccine development. Graphical Abstract

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Section: Resultsmentioning

confidence: 99%

Proteomics informed by transcriptomics for a qualitative and quantitative analysis of the sialoproteome of adult Ornithodoros moubata ticks

et al. 2021

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“…albopictus and other hematophagous arthropods during blood feeding that functions as platelet aggregation inhibitor. (25) The 67 kDa molecular weight protein in our study is thought to contain apyrase and α-glucosidase. The latter acts as an allergen that will induce IgE in humans.…”

Section: Discussionmentioning

confidence: 74%

“…The D7 family functions as a vasodilator, immunomodulator, and anticoagulant. (33) The protein of 47 kDa is serpin, that acts as anticoagulant and anti-inflammatory, (23,25,26) where as the band of 67 kDa is apyrase, that acts as allergen and anticoagulant. The abovementioned three proteins are thought to trigger modulation of the host's immune response because they comprise proteins that act as allergens and immunomodulators.…”

Section: Discussionmentioning

confidence: 99%

Detection of immunogenic protein from salivary gland of Aedes albopictus

et al. 2021

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BackgroundDengue virus is transmitted by several species of Aedes mosquitoes, with Aedes albopictus as secondary vector. During blood feeding, these vectors inject saliva into the vertebrate hosts. The saliva contains anticoagulant, anti-inflammatory and immunogenic factors. The objective of this research was to detect immunogenic proteins from Ae.albopictus salivary glands reacting with sera of people living in dengue endemic areas. MethodsThe identification of immunogenic proteins of Ae. albopictus salivary gland used one-dimensional gel electrophoresis (sodium dodecyl sulfate polyacrylamide gel electrophoresis), and western blot analysis, respectively. To determine the immunogenic nature of the candidate proteins, the antigens from the salivary gland of Ae. albopictus were reacted with sera from healthy persons, dengue hemorrhagic fever (DHF) patients, and neonates, each of the groups comprising 10 samples. ResultsThe protein profiles of Ae. albopictus salivary glands showed 13 bands with molecular weights from 16 kDa up to 97 kDa, i.e. 16, 17, 26, 28, 31, 32, 45, 55, 60, 67, 73, 76, and 97 kDa. According to western blot analysis result, the 31 kDa proteins were recognized in all endemic population sera, both in DHF patients and healthy persons. In contrast, protein bands of 47 and 67 kDa were only recognized by the sera of DHF patients. ConclusionThree immunogenic proteins of 31, 47 and 67 kDa were detected from Ae. albopictus salivary glands. These immunogenic proteins may be developed as candidate biomarkers for bite exposure to Ae. albopictus and as vector-based DHF vaccines.

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“…Apyrase has been identi ed in the saliva of most hematophagous vectors including soft and hard ticks. It is an enzyme that hydrolyses ATP and ADP to AMP and prevents platelet and neutrophil aggregation and thrombus formation, facilitating blood feeding [46,47]. A recombinant form of the salivary apyrase of O. moubata induced protective, strong humoral responses in animal vaccine trials that reduced tick feeding and survival [46].…”

Section: Quanti Cation Of the Proteins Identi Ed In The Female And Male Saliva By Swath-msmentioning

confidence: 99%

Proteomics Informed by Transcriptomics for a Qualitative and Quantitative Analysis of the Sialoproteome of Ornithodoros Moubata Adult Ticks

Oleaga

Carnero-Morán

Valero

et al. 2021

Preprint

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Background The argasid tick Ornithodoros moubata is the main vector in mainland Africa of the African swine fever virus and the spirochete Borrelia duttoni, which causes human relapsing fever. Elimination of O. moubata populations would contribute to the prevention and control of these two severe diseases. The development of anti-tick vaccines is an eco-friendly and sustainable method for the elimination of tick populations. The tick saliva forms part of the tick-host interface and knowing its composition is key for the identification and selection of vaccine candidate antigens. The aim of the present work is to expand the data on the saliva proteome composition of O. moubata adult ticks, particularly of female ticks, since a more in-depth knowledge of the O. moubata sialome will allow identifying and selecting novel salivary antigens as targets for tick vaccines. Methods We have analysed samples of female and male saliva using two different mass spectrometry approaches: data-dependent acquisition LC-MS/MS and sequential window acquisition of all theoretical fragment ion spectra mass spectrometry (SWATH-MS). To maximise the number of protein identifications, a proteomics informed by transcriptomics (PIT) analysis was applied using the O. moubata salivary transcriptomic dataset previously obtained by RNAseq. Results The SWATH-MS proved to be superior to LC-MS/MS in the study of female saliva since it increased by 60% the number of identified proteins, enhanced the reproducibility of the results and provided a quantitative image of the saliva components. As a whole, we have identified 299 non-redundant proteins in the O. moubata saliva and quantified the expression of 165 of them in both male and female saliva, among which 13 were significantly overexpressed in females and 40 in males. These results evidence important quantitative differences between sexes in the saliva proteome. Conclusions This work expand our knowledge of the O. moubata sialome, particularly of female ticks, by increasing the identification of novel salivary proteins and functions at the tick–host feeding interface. The integration of this new knowledge together with the information from the O. moubata sialotranscriptome will allow a more rational selection of the salivary candidates as antigen targets for tick vaccine development.

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Apyrase with anti-platelet aggregation activity from the nymph of the camel tick Hyalomma dromedarii

Cited by 10 publications

References 53 publications

Proteomics informed by transcriptomics for a qualitative and quantitative analysis of the sialoproteome of adult Ornithodoros moubata ticks

Proteomics informed by transcriptomics for a qualitative and quantitative analysis of the sialoproteome of adult Ornithodoros moubata ticks

Detection of immunogenic protein from salivary gland of Aedes albopictus

Proteomics Informed by Transcriptomics for a Qualitative and Quantitative Analysis of the Sialoproteome of Ornithodoros Moubata Adult Ticks

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