Functional bovine immunoglobulins in Boophilus microplus hemolymph

Vaz, Itabajara da Silva; Martinez, Regina Helena Moraes; Oliveira, Alexandre Tavares Duarte de; Heck, Augusto; Logullo, Carlos; Gonzales, João Carlos; Dewes, Homero; Masuda, Aoi

doi:10.1016/0304-4017(95)00851-9

Cited by 43 publications

(18 citation statements)

References 15 publications

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“…The presence of immunoglobulin chains in tick saliva could be explained as a part of the tick self-defense system, since immunoglobulin remains as an active protein in tick hemolymph [172]. In addition, the existence of immunoglobulin-binding proteins in both the tick salivary gland and hemolymph indicates that hemolymph and salivary gland cooperate to remove foreign proteins that could be deleterious for tick development during feeding [48].…”

Section: Resultsmentioning

confidence: 99%

Proteomic Analysis of Cattle Tick Rhipicephalus (Boophilus) microplus Saliva: A Comparison between Partially and Fully Engorged Females

et al. 2014

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The cattle tick Rhipicephalus (Boophilus) microplus is one of the most harmful parasites affecting bovines. Similarly to other hematophagous ectoparasites, R. microplus saliva contains a collection of bioactive compounds that inhibit host defenses against tick feeding activity. Thus, the study of tick salivary components offers opportunities for the development of immunological based tick control methods and medicinal applications. So far, only a few proteins have been identified in cattle tick saliva. The aim of this work was to identify proteins present in R. microplus female tick saliva at different feeding stages. Proteomic analysis of R. microplus saliva allowed identifying peptides corresponding to 187 and 68 tick and bovine proteins, respectively. Our data confirm that (i) R. microplus saliva is complex, and (ii) that there are remarkable differences in saliva composition between partially engorged and fully engorged female ticks. R. microplus saliva is rich mainly in (i) hemelipoproteins and other transporter proteins, (ii) secreted cross-tick species conserved proteins, (iii) lipocalins, (iv) peptidase inhibitors, (v) antimicrobial peptides, (vii) glycine-rich proteins, (viii) housekeeping proteins and (ix) host proteins. This investigation represents the first proteomic study about R. microplus saliva, and reports the most comprehensive Ixodidae tick saliva proteome published to date. Our results improve the understanding of tick salivary modulators of host defense to tick feeding, and provide novel information on the tick-host relationship.

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Section: Resultsmentioning

confidence: 99%

Proteomic Analysis of Cattle Tick Rhipicephalus (Boophilus) microplus Saliva: A Comparison between Partially and Fully Engorged Females

et al. 2014

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“…It was demonstrated that ticks transport intact proteins across the digestive system to the hemolymph. After blood ingestion, host blood proteins such as albumin and immunoglobulin cross the midgut epithelium of ticks, and are detected in tick tissues, including secretion into saliva [ 15 , 152 , 153 ]. This finding suggests that the presence of host proteins in tick saliva may be a real and common recycling system present in ticks, not a result of contamination during saliva collection.…”

Section: Resultsmentioning

confidence: 99%

Saliva from nymph and adult females of Haemaphysalis longicornis: a proteomic study

et al. 2015

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BackgroundHaemaphysalis longicornis is a major vector of Theileria spp., Anaplasma phagocytophilum, Babesia spp. and Coxiella burnetti in East Asian countries. All life stages of ixodid ticks have a destructive pool-feeding style in which they create a pool-feeding site by lacerating host tissue and secreting a variety of biologically active compounds that allows the tick to evade host responses, enabling the uptake of a blood meal. The identification and functional characterization of tick saliva proteins can be useful to elucidate the molecular mechanisms involved in tick development and to conceive new anti-tick control methods.MethodsH. longicornis tick saliva was collected from fully engorged nymphs and fully engorged adults induced by dopamine or pilocarpine, respectively. Saliva was digested with trypsin for LC-MS/MS sequencing and peptides were searched against tick and rabbit sequences.ResultsA total of 275 proteins were identified, of which 135 were tick and 100 were rabbit proteins. Of the tick proteins, 30 proteins were identified exclusively in fully engorged nymph saliva, 74 in fully engorged adult females, and 31 were detected in both stages. The identified tick proteins include heme/iron metabolism-related proteins, oxidation/detoxification proteins, enzymes, proteinase inhibitors, tick-specific protein families, and cytoskeletal proteins. Proteins involved in signal transduction, transport and metabolism of carbohydrate, energy, nucleotide, amino acids and lipids were also detected. Of the rabbit proteins, 13 were present in nymph saliva, 48 in adult saliva, and 30 were present in both. The host proteins include immunoglobulins, complement system proteins, antimicrobial proteins, serum albumin, peroxiredoxin, serotransferrin, apolipoprotein, hemopexin, proteinase inhibitors, and hemoglobin/red blood cells-related products.ConclusionsThis study allows the identification of H. longicornis saliva proteins. In spontaneously detached tick saliva various proteins were identified, although results obtained with saliva of fully engorged ticks need to be carefully interpreted. However, it is interesting to note that proteins identified in this study were also described in other tick saliva proteomes using partially engorged tick saliva, including hemelipoprotein, proteases, protease inhibitors, proteins related to structural functions, transporter activity, metabolic processes, and others. In conclusion, these data can provide a deeper understanding to the biology of H. longicornis.Electronic supplementary materialThe online version of this article (doi:10.1186/s13071-015-0918-y) contains supplementary material, which is available to authorized users.

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“…Another important B. microplus enzyme implicated in this process is the aspartic proteinase BYC (Boophilus Yolk procathepsin) (Logullo et al 1998). Ticks fed on BYCvaccinated bovines presented functional bovine immunoglobulins circulating in haemolymph (Da Silva Vaz Jr et al 1996). Moreover, cattle vaccinated with BYC presented a partially protective immune response against B. microplus infestation, mainly due to a decreased number of fertile eggs (Da Silva Vaz Jr et al 1998).…”

Section: Discussionmentioning

confidence: 99%

A Boophilus microplus vitellin-degrading cysteine endopeptidase

et al. 2003

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Here we describe the purification and characterization of a vitellin (VT) degrading cysteine endopeptidase (VTDCE) from eggs of the hard tick Boophilus microplus. A homogeneous enzyme preparation was obtained by chromatographic fractionation on ion-exchange and gel filtration columns and an autolysis step. This step consisted of incubation of a semipurified enzyme (after the first ion-exchange chromatography) at pH 4 . 0 that dissociated the enzyme from VT, to which VTDCE is naturally tightly associated. The enzyme purity was confirmed by capillary and native gel electrophoresis, and SDS-PAGE suggested the enzyme is a dimer of 17 and 22 kDa. VTDCE was active upon several synthetic substrates, with a preference for a hydrophobic or a basic residue in P 1 , and a hydrophobic residue in P 2 . VTDCE also hydrolysed haemoglobin, albumin, gelatin and vitellin. VTDCE is inactive in the absence of DTT and was totally inhibited by E-64, indicating it is a cysteine endopeptidase. Our results suggest that VTDCE is a major enzyme involved in yolk processing during B. microplus embryogenesis.

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Functional bovine immunoglobulins in Boophilus microplus hemolymph

Cited by 43 publications

References 15 publications

Proteomic Analysis of Cattle Tick Rhipicephalus (Boophilus) microplus Saliva: A Comparison between Partially and Fully Engorged Females

Proteomic Analysis of Cattle Tick Rhipicephalus (Boophilus) microplus Saliva: A Comparison between Partially and Fully Engorged Females

Saliva from nymph and adult females of Haemaphysalis longicornis: a proteomic study

A Boophilus microplus vitellin-degrading cysteine endopeptidase

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